Binding Site Information of Target

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Target General Information
Drug Binding Sites of Target
References
Target General Information  Top
Target ID T54065 Target Info
Target Name Bacterial Phosphoshikimate1-carboxyvinyltransferase (Bact aroA)
Synonyms aroA of Escherichia coli; EPSPS of Escherichia coli; EPSP synthase of Escherichia coli; 5-enolpyruvylshikimate-3-phosphate synthase of Escherichia coli
Target Type Literature-reported Target
Gene Name Bact aroA
Biochemical Class Alkyl aryl transferase
UniProt ID
AROA_ECOLI
Drug Binding Sites of Target  Top
Ligand Name: Glyphosate Ligand Info
Structure Description STRUCTURE OF EPSP SYNTHASE LIGANDED WITH SHIKIMATE-3-PHOSPHATE AND GLYPHOSATE PDB:1G6S
Method X-ray diffraction Resolution 1.50 Å Mutation No [1]
PDB Sequence
MESLTLQPIA
10
RVDGTINLPG
20
SKSVSNRALL
30
LAALAHGKTV
40
LTNLLDSDDV
50

RHMLNALTAL
60
GVSYTLSADR
70
TRCEIIGNGG
80
PLHAEGALEL
90
FLGNAGTAMR
100

PLAAALCLGS
110
NDIVLTGEPR
120
MKERPIGHLV
130
DALRLGGAKI
140
TYLEQENYPP
150

LRLQGGFTGG
160
NVDVDGSVSS
170
QFLTALLMTA
180
PLAPEDTVIR
190
IKGDLVSKPY
200

IDITLNLMKT
210
FGVEIENQHY
220
QQFVVKGGQS
230
YQSPGTYLVE
240
GDASSASYFL
250

AAAAIKGGTV
260
KVTGIGRNSM
270
QGDIRFADVL
280
EKMGATICWG
290
DDYISCTRGE
300

LNAIDMDMNH
310
IPDAAMTIAT
320
AALFAKGTTT
330
LRNIYNWRVK
340
ETDRLFAMAT
350

ELRKVGAEVE
360
EGHDYIRITP
370
PEKLNFAEIA
380
TYNDHRMAMC
390
FSLVALSDTP
400

VTILDPKCTA
410
KTFPDYFEQL
420
ARISQAA
Residue
Distance (Å)
LYS22
2.895
ASP49
4.325
ASN94
3.106
ALA95
3.870
GLY96
2.844
THR97
3.817
ARG100
3.896
ARG124
2.845
GLN171
2.877
Residue
Distance (Å)
ASP313
3.073
LYS340
4.217
GLU341
2.874
ARG344
2.838
HIS385
3.328
ARG386
2.614
LYS411
2.943
THR412
4.634
Click to View More Binding Site Information of This Target and Ligand Pair
Ligand Name: Shikimate-3-Phosphate Ligand Info
Structure Description STRUCTURE OF EPSP SYNTHASE LIGANDED WITH SHIKIMATE-3-PHOSPHATE AND GLYPHOSATE PDB:1G6S
Method X-ray diffraction Resolution 1.50 Å Mutation No [1]
PDB Sequence
MESLTLQPIA
10
RVDGTINLPG
20
SKSVSNRALL
30
LAALAHGKTV
40
LTNLLDSDDV
50

RHMLNALTAL
60
GVSYTLSADR
70
TRCEIIGNGG
80
PLHAEGALEL
90
FLGNAGTAMR
100

PLAAALCLGS
110
NDIVLTGEPR
120
MKERPIGHLV
130
DALRLGGAKI
140
TYLEQENYPP
150

LRLQGGFTGG
160
NVDVDGSVSS
170
QFLTALLMTA
180
PLAPEDTVIR
190
IKGDLVSKPY
200

IDITLNLMKT
210
FGVEIENQHY
220
QQFVVKGGQS
230
YQSPGTYLVE
240
GDASSASYFL
250

AAAAIKGGTV
260
KVTGIGRNSM
270
QGDIRFADVL
280
EKMGATICWG
290
DDYISCTRGE
300

LNAIDMDMNH
310
IPDAAMTIAT
320
AALFAKGTTT
330
LRNIYNWRVK
340
ETDRLFAMAT
350

ELRKVGAEVE
360
EGHDYIRITP
370
PEKLNFAEIA
380
TYNDHRMAMC
390
FSLVALSDTP
400

VTILDPKCTA
410
KTFPDYFEQL
420
ARISQAA
Residue
Distance (Å)
LYS22
2.764
SER23
2.609
ARG27
2.736
THR97
3.471
ARG100
4.808
VAL168
4.037
SER169
2.640
SER170
2.597
GLN171
3.425
Residue
Distance (Å)
THR174
4.723
VAL196
4.919
SER197
2.652
TYR200
3.287
PRO312
4.246
ASP313
2.708
ASN336
2.976
LYS340
2.665
Click to View More Binding Site Information of This Target and Ligand Pair
Ligand Name: Glyphosate Ligand Info
Structure Description E. coli EPSP synthase (T97I) liganded with S3P and glyphosate PDB:3FJZ
Method X-ray diffraction Resolution 1.70 Å Mutation Yes [2]
PDB Sequence
MESLTLQPIA
10
RVDGTINLPG
20
SKSVSNRALL
30
LAALAHGKTV
40
LTNLLDSDDV
50

RHMLNALTAL
60
GVSYTLSADR
70
TRCEIIGNGG
80
PLHAEGALEL
90
FLGNAGIAMR
100

PLAAALCLGS
110
NDIVLTGEPR
120
MKERPIGHLV
130
DALRLGGAKI
140
TYLEQENYPP
150

LRLQGGFTGG
160
NVDVDGSVSS
170
QFLTALLMTA
180
PLAPEDTVIR
190
IKGDLVSKPY
200

IDITLNLMKT
210
FGVEIENQHY
220
QQFVVKGGQS
230
YQSPGTYLVE
240
GDASSASYFL
250

AAAAIKGGTV
260
KVTGIGRNSM
270
QGDIRFADVL
280
EKMGATICWG
290
DDYISCTRGE
300

LNAIDMDMNH
310
IPDAAMTIAT
320
AALFAKGTTT
330
LRNIYNWRVK
340
ETDRLFAMAT
350

ELRKVGAEVE
360
EGHDYIRITP
370
PEKLNFAEIA
380
TYNDHRMAMC
390
FSLVALSDTP
400

VTILDPKCTA
410
KTFPDYFEQL
420
ARISQAA
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .GPF or .GPF2 or .GPF3 or :3GPF;style chemicals stick;color identity;select .A:22 or .A:49 or .A:94 or .A:95 or .A:96 or .A:97 or .A:100 or .A:124 or .A:171 or .A:313 or .A:340 or .A:341 or .A:344 or .A:385 or .A:386 or .A:411 or .A:412; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
LYS22
2.819
ASP49
4.330
ASN94
3.094
ALA95
3.850
GLY96
2.819
ILE97
3.934
ARG100
3.881
ARG124
2.821
GLN171
2.806
Residue
Distance (Å)
ASP313
3.094
LYS340
4.253
GLU341
2.932
ARG344
2.878
HIS385
3.254
ARG386
2.465
LYS411
2.935
THR412
4.641
Click to View More Binding Site Information of This Target and Ligand Pair
Ligand Name: L-serine Ligand Info
Structure Description E. coli EPSP synthase (T97I) liganded with S3P and glyphosate PDB:3FJZ
Method X-ray diffraction Resolution 1.70 Å Mutation Yes [2]
PDB Sequence
MESLTLQPIA
10
RVDGTINLPG
20
SKSVSNRALL
30
LAALAHGKTV
40
LTNLLDSDDV
50

RHMLNALTAL
60
GVSYTLSADR
70
TRCEIIGNGG
80
PLHAEGALEL
90
FLGNAGIAMR
100

PLAAALCLGS
110
NDIVLTGEPR
120
MKERPIGHLV
130
DALRLGGAKI
140
TYLEQENYPP
150

LRLQGGFTGG
160
NVDVDGSVSS
170
QFLTALLMTA
180
PLAPEDTVIR
190
IKGDLVSKPY
200

IDITLNLMKT
210
FGVEIENQHY
220
QQFVVKGGQS
230
YQSPGTYLVE
240
GDASSASYFL
250

AAAAIKGGTV
260
KVTGIGRNSM
270
QGDIRFADVL
280
EKMGATICWG
290
DDYISCTRGE
300

LNAIDMDMNH
310
IPDAAMTIAT
320
AALFAKGTTT
330
LRNIYNWRVK
340
ETDRLFAMAT
350

ELRKVGAEVE
360
EGHDYIRITP
370
PEKLNFAEIA
380
TYNDHRMAMC
390
FSLVALSDTP
400

VTILDPKCTA
410
KTFPDYFEQL
420
ARISQAA
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .SER or .SER2 or .SER3 or :3SER;style chemicals stick;color identity;select .A:240 or .A:264 or .A:265 or .A:266 or .A:268 or .A:269 or .A:270 or .A:271 or .A:274; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
GLU240
3.501
GLY264
4.922
ILE265
3.469
GLY266
2.936
ASN268
3.679
Residue
Distance (Å)
SER269
0.080
MET270
3.222
GLN271
4.175
ILE274
3.782
Ligand Name: Shikimic acid Ligand Info
Structure Description EPSP synthase liganded with shikimate PDB:2AA9
Method X-ray diffraction Resolution 1.50 Å Mutation No [3]
PDB Sequence
MESLTLQPIA
10
RVDGTINLPG
20
SKSVSNRALL
30
LAALAHGKTV
40
LTNLLDSDDV
50

RHMLNALTAL
60
GVSYTLSADR
70
TRCEIIGNGG
80
PLHAEGALEL
90
FLGNAGTAMR
100

PLAAALCLGS
110
NDIVLTGEPR
120
MKERPIGHLV
130
DALRLGGAKI
140
TYLEQENYPP
150

LRLQGGFTGG
160
NVDVDGSVSS
170
QFLTALLMTA
180
PLAPEDTVIR
190
IKGDLVSKPY
200

IDITLNLMKT
210
FGVEIENQHY
220
QQFVVKGGQS
230
YQSPGTYLVE
240
GDASSASYFL
250

AAAAIKGGTV
260
KVTGIGRNSM
270
QGDIRFADVL
280
EKMGATICWG
290
DDYISCTRGE
300

LNAIDMDMNH
310
IPDAAMTIAT
320
AALFAKGTTT
330
LRNIYNWRVK
340
ETDRLFAMAT
350

ELRKVGAEVE
360
EGHDYIRITP
370
PEKLNFAEIA
380
TYNDHRMAMC
390
FSLVALSDTP
400

VTILDPKCTA
410
KTFPDYFEQL
420
ARISQAA
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .SKM or .SKM2 or .SKM3 or :3SKM;style chemicals stick;color identity;select .A:22 or .A:23 or .A:27 or .A:97 or .A:169 or .A:170 or .A:171 or .A:174 or .A:200 or .A:312 or .A:313 or .A:340 or .A:341; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
LYS22
3.101
SER23
2.730
ARG27
2.742
THR97
3.477
SER169
4.808
SER170
3.953
GLN171
2.939
Residue
Distance (Å)
THR174
4.708
TYR200
3.299
PRO312
4.227
ASP313
2.651
LYS340
2.664
GLU341
4.925
Click to View More Binding Site Information of This Target and Ligand Pair
Ligand Name: [3R-[3A,4A,5B(S*)]]-5-(1-Carboxy-1-phosphonoethoxy)-4-hydroxy-3-(phosphonooxy)-1-cyclohexene-1-carboxylic acid Ligand Info
Structure Description EPSPS liganded with the (S)-phosphonate analog of the tetrahedral reaction intermediate PDB:1X8R
Method X-ray diffraction Resolution 1.50 Å Mutation No [4]
PDB Sequence
MESLTLQPIA
10
RVDGTINLPG
20
SKSVSNRALL
30
LAALAHGKTV
40
LTNLLDSDDV
50

RHMLNALTAL
60
GVSYTLSADR
70
TRCEIIGNGG
80
PLHAEGALEL
90
FLGNAGTAMR
100

PLAAALCLGS
110
NDIVLTGEPR
120
MKERPIGHLV
130
DALRLGGAKI
140
TYLEQENYPP
150

LRLQGGFTGG
160
NVDVDGSVSS
170
QFLTALLMTA
180
PLAPEDTVIR
190
IKGDLVSKPY
200

IDITLNLMKT
210
FGVEIENQHY
220
QQFVVKGGQS
230
YQSPGTYLVE
240
GDASSASYFL
250

AAAAIKGGTV
260
KVTGIGRNSM
270
QGDIRFADVL
280
EKMGATICWG
290
DDYISCTRGE
300

LNAIDMDMNH
310
IPDAAMTIAT
320
AALFAKGTTT
330
LRNIYNWRVK
340
ETDRLFAMAT
350

ELRKVGAEVE
360
EGHDYIRITP
370
PEKLNFAEIA
380
TYNDHRMAMC
390
FSLVALSDTP
400

VTILDPKCTA
410
KTFPDYFEQL
420
ARISQAA
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .SC1 or .SC12 or .SC13 or :3SC1;style chemicals stick;color identity;select .A:22 or .A:23 or .A:27 or .A:49 or .A:94 or .A:95 or .A:96 or .A:97 or .A:100 or .A:124 or .A:168 or .A:169 or .A:170 or .A:171 or .A:174 or .A:196 or .A:197 or .A:200 or .A:312 or .A:313 or .A:336 or .A:340 or .A:341 or .A:344 or .A:385 or .A:386 or .A:411 or .A:412; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
LYS22
2.570
SER23
2.734
ARG27
2.716
ASP49
4.188
ASN94
3.609
ALA95
4.609
GLY96
3.551
THR97
3.383
ARG100
4.375
ARG124
2.733
VAL168
4.091
SER169
2.669
SER170
2.529
GLN171
2.759
Residue
Distance (Å)
THR174
4.795
VAL196
4.920
SER197
2.559
TYR200
3.353
PRO312
4.088
ASP313
2.985
ASN336
2.863
LYS340
2.725
GLU341
2.588
ARG344
3.061
HIS385
2.856
ARG386
3.421
LYS411
2.600
THR412
4.252
Ligand Name: (3r,4s,5r)-5-[(1r)-1-Carboxy-2,2-Difluoro-1-(Phosphonooxy)ethoxy]-4-Hydroxy-3-(Phosphonooxy)cyclohex-1-Ene-1-Carboxylic Acid Ligand Info
Structure Description E. coli EPSPS liganded with (R)-difluoromethyl tetrahedral reaction intermediate analog PDB:2PQ9
Method X-ray diffraction Resolution 1.60 Å Mutation No [5]
PDB Sequence
MESLTLQPIA
10
RVDGTINLPG
20
SKSVSNRALL
30
LAALAHGKTV
40
LTNLLDSDDV
50

RHMLNALTAL
60
GVSYTLSADR
70
TRCEIIGNGG
80
PLHAEGALEL
90
FLGNAGTAMR
100

PLAAALCLGS
110
NDIVLTGEPR
120
MKERPIGHLV
130
DALRLGGAKI
140
TYLEQENYPP
150

LRLQGGFTGG
160
NVDVDGSVSS
170
QFLTALLMTA
180
PLAPEDTVIR
190
IKGDLVSKPY
200

IDITLNLMKT
210
FGVEIENQHY
220
QQFVVKGGQS
230
YQSPGTYLVE
240
GDASSASYFL
250

AAAAIKGGTV
260
KVTGIGRNSM
270
QGDIRFADVL
280
EKMGATICWG
290
DDYISCTRGE
300

LNAIDMDMNH
310
IPDAAMTIAT
320
AALFAKGTTT
330
LRNIYNWRVK
340
ETDRLFAMAT
350

ELRKVGAEVE
360
EGHDYIRITP
370
PEKLNFAEIA
380
TYNDHRMAMC
390
FSLVALSDTP
400

VTILDPKCTA
410
KTFPDYFEQL
420
ARISQAA
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .GG9 or .GG92 or .GG93 or :3GG9;style chemicals stick;color identity;select .A:22 or .A:23 or .A:27 or .A:49 or .A:94 or .A:95 or .A:96 or .A:97 or .A:100 or .A:124 or .A:168 or .A:169 or .A:170 or .A:171 or .A:174 or .A:196 or .A:197 or .A:200 or .A:312 or .A:313 or .A:336 or .A:340 or .A:341 or .A:344 or .A:385 or .A:386 or .A:411 or .A:412; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
LYS22
2.742
SER23
2.734
ARG27
2.790
ASP49
4.327
ASN94
3.236
ALA95
3.863
GLY96
2.784
THR97
3.448
ARG100
4.352
ARG124
2.742
VAL168
4.142
SER169
2.666
SER170
2.509
GLN171
2.975
Residue
Distance (Å)
THR174
4.896
VAL196
5.000
SER197
2.550
TYR200
3.369
PRO312
4.162
ASP313
2.958
ASN336
2.881
LYS340
2.765
GLU341
3.984
ARG344
2.790
HIS385
3.077
ARG386
2.945
LYS411
2.672
THR412
4.468
Ligand Name: 5-(1-Carboxy-1-phosphonooxy-ethoxyl)-4-hydroxy-3-phosphonooxy-cyclohex-1-enecarboxylic acid Ligand Info
Structure Description EPSP synthase (Asp313Ala) liganded with tetrahedral reaction intermediate PDB:1Q36
Method X-ray diffraction Resolution 1.60 Å Mutation Yes [6]
PDB Sequence
MESLTLQPIA
10
RVDGTINLPG
20
SKSVSNRALL
30
LAALAHGKTV
40
LTNLLDSDDV
50

RHMLNALTAL
60
GVSYTLSADR
70
TRCEIIGNGG
80
PLHAEGALEL
90
FLGNAGTAMR
100

PLAAALCLGS
110
NDIVLTGEPR
120
MKERPIGHLV
130
DALRLGGAKI
140
TYLEQENYPP
150

LRLQGGFTGG
160
NVDVDGSVSS
170
QFLTALLMTA
180
PLAPEDTVIR
190
IKGDLVSKPY
200

IDITLNLMKT
210
FGVEIENQHY
220
QQFVVKGGQS
230
YQSPGTYLVE
240
GDASSASYFL
250

AAAAIKGGTV
260
KVTGIGRNSM
270
QGDIRFADVL
280
EKMGATICWG
290
DDYISCTRGE
300

LNAIDMDMNH
310
IPAAAMTIAT
320
AALFAKGTTT
330
LRNIYNWRVK
340
ETDRLFAMAT
350

ELRKVGAEVE
360
EGHDYIRITP
370
PEKLNFAEIA
380
TYNDHRMAMC
390
FSLVALSDTP
400

VTILDPKCTA
410
KTFPDYFEQL
420
ARISQAA
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .SKP or .SKP2 or .SKP3 or :3SKP;style chemicals stick;color identity;select .A:22 or .A:23 or .A:27 or .A:49 or .A:94 or .A:95 or .A:96 or .A:97 or .A:100 or .A:124 or .A:168 or .A:169 or .A:170 or .A:171 or .A:174 or .A:196 or .A:197 or .A:200 or .A:312 or .A:313 or .A:336 or .A:340 or .A:341 or .A:344 or .A:385 or .A:386 or .A:411 or .A:412; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
LYS22
2.666
SER23
2.700
ARG27
2.684
ASP49
4.302
ASN94
3.284
ALA95
3.865
GLY96
2.809
THR97
3.367
ARG100
4.342
ARG124
2.789
VAL168
4.108
SER169
2.657
SER170
2.602
GLN171
2.844
Residue
Distance (Å)
THR174
4.873
VAL196
4.905
SER197
2.617
TYR200
3.321
PRO312
4.134
ALA313
4.390
ASN336
2.911
LYS340
2.623
GLU341
3.162
ARG344
2.923
HIS385
3.420
ARG386
2.808
LYS411
2.887
THR412
4.441
Ligand Name: [3R-[3A,4A,5B(R*)]]-5-(1-Carboxy-1-phosphonoethoxy)-4-hydroxy-3-(phosphonooxy)-1-cyclohexene-1-carboxylic acid Ligand Info
Structure Description EPSPS liganded with the (R)-phosphonate analog of the tetrahedral reaction intermediate PDB:1X8T
Method X-ray diffraction Resolution 1.90 Å Mutation No [4]
PDB Sequence
MESLTLQPIA
10
RVDGTINLPG
20
SKSVSNRALL
30
LAALAHGKTV
40
LTNLLDSDDV
50

RHMLNALTAL
60
GVSYTLSADR
70
TRCEIIGNGG
80
PLHAEGALEL
90
FLGNAGTAMR
100

PLAAALCLGS
110
NDIVLTGEPR
120
MKERPIGHLV
130
DALRLGGAKI
140
TYLEQENYPP
150

LRLQGGFTGG
160
NVDVDGSVSS
170
QFLTALLMTA
180
PLAPEDTVIR
190
IKGDLVSKPY
200

IDITLNLMKT
210
FGVEIENQHY
220
QQFVVKGGQS
230
YQSPGTYLVE
240
GDASSASYFL
250

AAAAIKGGTV
260
KVTGIGRNSM
270
QGDIRFADVL
280
EKMGATICWG
290
DDYISCTRGE
300

LNAIDMDMNH
310
IPDAAMTIAT
320
AALFAKGTTT
330
LRNIYNWRVK
340
ETDRLFAMAT
350

ELRKVGAEVE
360
EGHDYIRITP
370
PEKLNFAEIA
380
TYNDHRMAMC
390
FSLVALSDTP
400

VTILDPKCTA
410
KTFPDYFEQL
420
ARISQAA
Click to Show 3D Structure of This Binding Site
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Residue
Distance (Å)
LYS22
2.640
SER23
2.798
ARG27
2.732
ASP49
4.188
GLY96
4.910
THR97
3.470
ARG100
4.901
VAL168
4.062
SER169
2.535
SER170
2.572
GLN171
2.954
THR174
4.633
VAL196
4.752
Residue
Distance (Å)
SER197
2.520
TYR200
3.351
PRO312
4.059
ASP313
2.741
ASN336
2.786
LYS340
2.630
GLU341
3.398
ARG344
2.994
HIS385
2.725
ARG386
2.912
LYS411
3.576
THR412
4.218
References  Top
REF 1 Interaction of the herbicide glyphosate with its target enzyme 5-enolpyruvylshikimate 3-phosphate synthase in atomic detail. Proc Natl Acad Sci U S A. 2001 Feb 13;98(4):1376-80.
REF 2 Structural basis of glyphosate resistance resulting from the double mutation Thr97 -> Ile and Pro101 -> Ser in 5-enolpyruvylshikimate-3-phosphate synthase from Escherichia coli. J Biol Chem. 2009 Apr 10;284(15):9854-60.
REF 3 Molecular basis for the glyphosate-insensitivity of the reaction of 5-enolpyruvylshikimate 3-phosphate synthase with shikimate. FEBS Lett. 2005 Oct 24;579(25):5773-80.
REF 4 Interaction of phosphonate analogues of the tetrahedral reaction intermediate with 5-enolpyruvylshikimate-3-phosphate synthase in atomic detail. Biochemistry. 2005 Mar 8;44(9):3241-8.
REF 5 Differential inhibition of class I and class II 5-enolpyruvylshikimate-3-phosphate synthases by tetrahedral reaction intermediate analogues. Biochemistry. 2007 Nov 20;46(46):13344-51.
REF 6 A new view of the mechanisms of UDP-N-acetylglucosamine enolpyruvyl transferase (MurA) and 5-enolpyruvylshikimate-3-phosphate synthase (AroA) derived from X-ray structures of their tetrahedral reaction intermediate states. J Biol Chem. 2003 Dec 5;278(49):49215-22.

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