Target Binding Site Detail
| Target General Information | Top | ||||
|---|---|---|---|---|---|
| Target ID | T12409 | Target Info | |||
| Target Name | Bacterial Glucosamine-6-phosphate synthase (Bact glmS) | ||||
| Synonyms | glmS; L-glutamine-D-fructose-6-phosphate amidotransferase; Hexosephosphate aminotransferase; Glucosamine--fructose-6-phosphate aminotransferase; GFAT; D-fructose-6-phosphate amidotransferase | ||||
| Target Type | Clinical trial Target | ||||
| Gene Name | Bact glmS | ||||
| Biochemical Class | Transaminase | ||||
| UniProt ID | |||||
| Ligand General Information | Top | ||||
|---|---|---|---|---|---|
| Ligand Name | Glucosamine 6-phosphate | Ligand Info | |||
| Canonical SMILES | C(C1C(C(C(C(O1)O)N)O)O)OP(=O)(O)O | ||||
| InChI | 1S/C6H14NO8P/c7-3-5(9)4(8)2(15-6(3)10)1-14-16(11,12)13/h2-6,8-10H,1,7H2,(H2,11,12,13)/t2-,3-,4-,5-,6+/m1/s1 | ||||
| InChIKey | XHMJOUIAFHJHBW-UKFBFLRUSA-N | ||||
| PubChem Compound ID | 439217 | ||||
| Drug Binding Sites of Target | Top | |||||
|---|---|---|---|---|---|---|
| PDB ID: 2VF5 Glucosamine-6-phosphate synthase in complex with glucosamine-6- phosphate | ||||||
| Method | X-ray diffraction | Resolution | 2.90 Å | Mutation | No | [1] |
| PDB Sequence |
GDKGIYRHYM
252 QKEIYEQPNA262 IKNTLTGRIS272 HGQVDLSELG282 PNADELLSKV292 EHIQILACGT 302 SYNSGMVSRY312 WFESLAGIPC322 DVEIASEFRY332 RKSAVRRNSL342 MITLSQSGET 352 ADTLAGLRLS362 KELGYLGSLA372 ICNVPGSSLV382 RESDLALMTN392 AGTEIGVAST 402 KAFTTQLTVL412 LMLVAKLSRL422 KGLDASIEHD432 IVHGLQALPS442 RIEQMLSQDK 452 RIEALAEDFS462 DKHHALFLGR472 GDQYPIALEG482 ALKLKEISYI492 HAEAYAAGEL 502 KHGPLALIDA512 DMPVIVVAPN522 NELLEKLKSN532 IEEVRARGGQ542 LYVFADQDAG 552 FVSSDNMHII562 EMPHVEEVIA572 PIFYTVPLQL582 LAYHVALIKG592 TDVDQPRNLA 602 KSVTVE
|
|||||
|
|
CYS300
3.014
GLY301
3.593
THR302
2.560
SER303
2.839
LEU346
4.347
SER347
3.043
GLN348
2.701
SER349
2.380
GLY350
4.597
THR352
2.693
|
|||||
| PDB ID: 1MOQ ISOMERASE DOMAIN OF GLUCOSAMINE 6-PHOSPHATE SYNTHASE COMPLEXED WITH GLUCOSAMINE 6-PHOSPHATE | ||||||
| Method | X-ray diffraction | Resolution | 1.57 Å | Mutation | No | [2] |
| PDB Sequence |
GDKGIYRHYM
252 QKEIYEQPNA262 IKNTLTGRIS272 HGQVDLSELG282 PNADELLSKV292 EHIQILACGT 302 SYNSGMVSRY312 WFESLAGIPC322 DVEIASEFRY332 RKSAVRRNSL342 MITLSQSGET 352 ADTLAGLRLS362 KELGYLGSLA372 ICNVPGSSLV382 RESDLALMTN392 AGTEIGVAST 402 KAFTTQLTVL412 LMLVAKLSRL422 KGLDASIEHD432 IVHGLQALPS442 RIEQMLSQDK 452 RIEALAEDFS462 DKHHALFLGR472 GDQYPIALEG482 ALKLKEISYI492 HAEAYAAGEL 502 KHGPLALIDA512 DMPVIVVAPN522 NELLEKLKSN532 IEEVRARGGQ542 LYVFADQDAG 552 FVSSDNMHII562 EMPHVEEVIA572 PIFYTVPLQL582 LAYHVALIKG592 TDVDQPRNLA 602 KSVTVE
|
|||||
|
|
CYS300
3.500
GLY301
3.734
THR302
2.823
SER303
2.658
LEU346
4.280
SER347
2.773
GLN348
2.807
SER349
2.740
GLY350
4.499
THR352
2.726
|
|||||
| References | Top | ||||
|---|---|---|---|---|---|
| REF 1 | Ordering of C-terminal loop and glutaminase domains of glucosamine-6-phosphate synthase promotes sugar ring opening and formation of the ammonia channel. J Mol Biol. 2008 Apr 4;377(4):1174-85. | ||||
| REF 2 | Involvement of the C terminus in intramolecular nitrogen channeling in glucosamine 6-phosphate synthase: evidence from a 1.6 A crystal structure of the isomerase domain. Structure. 1998 Aug 15;6(8):1047-55. | ||||
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