Target Binding Site Detail

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Target General Information
Ligand General Information
Drug Binding Sites of Target
References
Target General Information  Top
Target ID T16308 Target Info
Target Name Rotamase Pin1 (PIN1)
Synonyms Prolyl isomerase Pin1; Peptidyl-prolyl cis-trans isomerase Pin1; Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1; Peptidyl prolyl cis/trans isomerase Pin1; PPIase Pin1
Target Type Clinical trial Target
Gene Name PIN1
Biochemical Class Cis-trans-isomerase
UniProt ID
PIN1_HUMAN
Ligand General Information  Top
Ligand Name 2-(2-{2-[2-(2-Methoxy-ethoxy)-ethoxy]-ethoxy}-ethoxy)-ethanol Ligand Info
Canonical SMILES COCCOCCOCCOCCOCCO
InChI 1S/C11H24O6/c1-13-4-5-15-8-9-17-11-10-16-7-6-14-3-2-12/h12H,2-11H2,1H3
InChIKey SLNYBUIEAMRFSZ-UHFFFAOYSA-N
PubChem Compound ID 90255
Drug Binding Sites of Target  Top
PDB ID: 1PIN      PIN1 PEPTIDYL-PROLYL CIS-TRANS ISOMERASE FROM HOMO SAPIENS
Method X-ray diffraction Resolution 1.35 Å Mutation No [1]
PDB Sequence
KLPPGWEKRM
15
SRSSGRVYYF
25
NHITNASQWE
35
RPSGGKNGQG
50
EPARVRCSHL
60

LVKHSQSRRP
70
SSWRQEKITR
80
TKEEALELIN
90
GYIQKIKSGE
100
EDFESLASQF
110

SDCSSAKARG
120
DLGAFSRGQM
130
QKPFEDASFA
140
LRTGEMSGPV
150
FTDSGIHIIL
160

RTE
Residue
Distance (Å)
SER16
4.325
TYR23
3.585
SER32
3.525
GLN33
3.641
TRP34
2.917
ASN90
3.774
Residue
Distance (Å)
ILE96
3.793
LYS97
3.308
GLY144
4.022
MET146
3.911
LEU160
3.828
PDB ID: 2ZQT      Crystal structure of a mutant PIN1 PEPTIDYL-PROLYL CIS-TRANS ISOMERASE
Method X-ray diffraction Resolution 1.46 Å Mutation Yes [2]
PDB Sequence
KLPPGWEKRM
15
SRSSGRVYYF
25
NHITNASQWE
35
RPSGGKNGQG
50
EPARVRCSHL
60

LVKHSQSRRP
70
SSWRQEKITR
80
TKEEALELIN
90
GYIQKIKSGE
100
EDFESLASQF
110

SDCSSAKARG
120
DLGAFSRGQA
130
QKPFEDASFA
140
LRTGEMSGPV
150
FTDSGIHIIL
160

RTE
Residue
Distance (Å)
SER16
4.122
TYR23
3.421
SER32
3.469
GLN33
3.733
Residue
Distance (Å)
TRP34
3.461
ASN90
3.857
LYS97
3.210
PDB ID: 2ZQS      Crystal structure of a mutant PIN1 PEPTIDYL-PROLYL CIS-TRANS ISOMERASE
Method X-ray diffraction Resolution 1.90 Å Mutation Yes [3]
PDB Sequence
KLPPGWEKRM
15
SRSSGRVYYF
25
NHITNASQWE
35
RPSGGKNGQG
50
EPARVRCSHL
60

LVKHSQSRRP
70
SSWRQEKITR
80
TKEEALELIN
90
GYIQKIKSGE
100
EDFESLASQF
110

SDASSAKARG
120
DLGAFSRGQM
130
QKPFEDASFA
140
LRTGEMSGPV
150
FTDSGIHIIL
160

RTE
Residue
Distance (Å)
SER16
4.559
TYR23
3.674
SER32
3.673
GLN33
3.864
Residue
Distance (Å)
TRP34
3.334
ASN90
4.312
LYS97
3.255
PDB ID: 2ZR4      Crystal structure of a mutant PIN1 peptidyl-prolyl cis-trans isomerase
Method X-ray diffraction Resolution 2.00 Å Mutation Yes [4]
PDB Sequence
KLPPGWEKRM
15
SRSSGRVYYF
25
NHITNAAQWE
35
RPSGGKNGQG
50
EPARVRCSHL
60

LVKHSQSRRP
70
SSWRQEKITR
80
TKEEALELIN
90
GYIQKIKSGE
100
EDFESLASQF
110

SDCSSAKARG
120
DLGAFSRGQM
130
QKPFEDASFA
140
LRTGEMSGPV
150
FTDSGIHIIL
160

RTE
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .1PG or .1PG2 or .1PG3 or :31PG;style chemicals stick;color identity;select .A:16 or .A:23 or .A:30 or .A:31 or .A:32 or .A:33 or .A:34 or .A:93 or .A:97 or .A:146 or .A:147 or .A:148 or .A:149; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
SER16
3.250
TYR23
3.573
ASN30
3.523
ALA31
3.711
ALA32
3.550
GLN33
4.620
TRP34
3.236
Residue
Distance (Å)
ILE93
3.438
LYS97
2.943
MET146
3.672
SER147
3.126
GLY148
3.422
PRO149
4.804
PDB ID: 2ZQV      Crystal structure of a mutant PIN1 PEPTIDYL-PROLYL CIS-TRANS ISOMERASE
Method X-ray diffraction Resolution 2.50 Å Mutation Yes [5]
PDB Sequence
KLPPGWEKRM
15
SRSSGRVYYA
25
NHITNASQWE
35
RPSGGKNGQG
50
EPARVRCSHL
60

LVKHSQSRRP
70
SSWRQEKITR
80
TKEEALELIN
90
GYIQKIKSGE
100
EDFESLASQF
110

SDCSSAKARG
120
DLGAFSRGQM
130
QKPFEDASFA
140
LRTGEMSGPV
150
FTDSGIHIIL
160

RTE
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .1PG or .1PG2 or .1PG3 or :31PG;style chemicals stick;color identity;select .A:96 or .A:97 or .A:98 or .A:99; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
ILE96
4.384
LYS97
3.378
Residue
Distance (Å)
SER98
3.216
GLY99
3.572
PDB ID: 2ZR5      Crystal structure of a mutant PIN1 peptidyl-prolyl cis-trans isomerase
Method X-ray diffraction Resolution 2.60 Å Mutation Yes [6]
PDB Sequence
KLPPGWEKRM
15
SRSSGRVYYF
25
NHITNASQWE
35
RPSGGKNGQG
50
EPARVRCSHL
60

LVAHSQSRRP
70
SSWRQEKITR
80
TKEEALELIN
90
GYIQKIKSGE
100
EDFESLASQF
110

SDCSSAKARG
120
DLGAFSRGQM
130
QKPFEDASFA
140
LRTGEMSGPV
150
FTDSGIHIIL
160

RTE
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .1PG or .1PG2 or .1PG3 or :31PG;style chemicals stick;color identity;select .A:16 or .A:21 or .A:23 or .A:30 or .A:31 or .A:32 or .A:33 or .A:34 or .A:93 or .A:97 or .A:147 or .A:148 or .A:149; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
SER16
3.098
ARG21
4.572
TYR23
3.522
ASN30
3.612
ALA31
4.427
SER32
3.999
GLN33
3.814
Residue
Distance (Å)
TRP34
3.298
ILE93
3.600
LYS97
2.552
SER147
4.668
GLY148
3.610
PRO149
3.792
PDB ID: 2ZR6      Crystal structure of a mutant PIN1 peptidyl-prolyl cis-trans isomerase
Method X-ray diffraction Resolution 3.20 Å Mutation Yes [7]
PDB Sequence
KLPPGWEKAM
15
SRSSGRVYYF
25
NHITNASQWE
35
RPSGGKNGQG
50
EPARVRCSHL
60

LVKHSQSRRP
70
SSWRQEKITR
80
TKEEALELIN
90
GYIQKIKSGE
100
EDFESLASQF
110

SDCSSAKARG
120
DLGAFSRGQM
130
QKPFEDASFA
140
LRTGEMSGPV
150
FTDSGIHIIL
160

RTE
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .1PG or .1PG2 or .1PG3 or :31PG;style chemicals stick;color identity;select .A:16 or .A:21 or .A:23 or .A:30 or .A:31 or .A:32 or .A:33 or .A:34 or .A:93 or .A:97 or .A:146 or .A:147 or .A:148 or .A:149; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
SER16
3.711
ARG21
4.778
TYR23
3.491
ASN30
3.399
ALA31
4.134
SER32
3.524
GLN33
4.186
Residue
Distance (Å)
TRP34
3.511
ILE93
3.179
LYS97
3.112
MET146
4.756
SER147
4.208
GLY148
3.316
PRO149
4.434
PDB ID: 4U86      Human Pin1 with cysteine sulfonic acid 113
Method X-ray diffraction Resolution 1.60 Å Mutation No [8]
PDB Sequence
KLPPGWEKAM
15
SRSSGRVYYF
25
NHITNASQWE
35
RPEPARVRCS
58
HLLVKHSQSR
68

RPSSWRQEKI
78
TRTKEEALEL
88
INGYIQKIKS
98
GEEDFESLAS
108
QFSDSSAKAR
119

GDLGAFSRGQ
129
MQKPFEDASF
139
ALRTGEMSGP
149
VFTDSGIHII
159
LRTE
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .1PG or .1PG2 or .1PG3 or :31PG;style chemicals stick;color identity;select .A:16 or .A:23 or .A:30 or .A:31 or .A:32 or .A:33 or .A:34 or .A:93 or .A:97 or .A:146 or .A:147 or .A:148; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
SER16
4.605
TYR23
3.382
ASN30
3.992
ALA31
3.454
SER32
3.119
GLN33
4.018
Residue
Distance (Å)
TRP34
3.349
ILE93
3.501
LYS97
2.913
MET146
4.245
SER147
4.194
GLY148
3.917
References  Top
REF 1 Structural and functional analysis of the mitotic rotamase Pin1 suggests substrate recognition is phosphorylation dependent. Cell. 1997 Jun 13;89(6):875-86.
REF 2 Structural studies on PIN1 mutants
REF 3 Structural studies on PIN1 mutants
REF 4 Structural studies on PIN1 mutants
REF 5 Structural studies on PIN1 mutants
REF 6 Structural studies on PIN1 mutants
REF 7 Structural studies on PIN1 mutants
REF 8 Pin1 cysteine-113 oxidation inhibits its catalytic activity and cellular function in Alzheimer's disease. Neurobiol Dis. 2015 Apr;76:13-23.

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