1FXJ
CRYSTAL STRUCTURE OF N-ACETYLGLUCOSAMINE 1-PHOSPHATE URIDYLTRANSFERASE
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0000902 | biological_process | cell morphogenesis |
| A | 0003977 | molecular_function | UDP-N-acetylglucosamine diphosphorylase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006048 | biological_process | UDP-N-acetylglucosamine biosynthetic process |
| A | 0009252 | biological_process | peptidoglycan biosynthetic process |
| A | 0019134 | molecular_function | glucosamine-1-phosphate N-acetyltransferase activity |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0000902 | biological_process | cell morphogenesis |
| B | 0003977 | molecular_function | UDP-N-acetylglucosamine diphosphorylase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006048 | biological_process | UDP-N-acetylglucosamine biosynthetic process |
| B | 0009252 | biological_process | peptidoglycan biosynthetic process |
| B | 0019134 | molecular_function | glucosamine-1-phosphate N-acetyltransferase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 B 332 |
| Chain | Residue |
| B | ARG18 |
| B | ASN227 |
| B | GLN231 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 A 332 |
| Chain | Residue |
| A | ARG18 |
| A | ASN227 |
| A | GLN231 |
| A | HOH363 |
| A | HOH407 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE MES A 333 |
| Chain | Residue |
| A | ALA13 |
| A | GLY14 |
| A | TYR103 |
| A | ASP105 |
| A | GLY225 |
| A | ASN227 |
| A | HOH413 |
| A | LEU11 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 14 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01631, ECO:0000269|PubMed:10428949, ECO:0000269|PubMed:11329257, ECO:0000269|PubMed:17473010 |
| Chain | Residue | Details |
| A | LEU11 | |
| B | GLY81 | |
| B | TYR103 | |
| B | GLY140 | |
| B | GLU154 | |
| B | ASN169 | |
| A | GLN76 | |
| A | GLY81 | |
| A | TYR103 | |
| A | GLY140 | |
| A | GLU154 | |
| A | ASN169 | |
| B | LEU11 | |
| B | GLN76 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01631 |
| Chain | Residue | Details |
| A | LYS25 | |
| A | ASN227 | |
| B | LYS25 | |
| B | ASN227 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:17473010, ECO:0007744|PDB:2OI5 |
| Chain | Residue | Details |
| A | ASP105 | |
| B | ASP105 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1hv9 |
| Chain | Residue | Details |
| A | ARG18 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1hv9 |
| Chain | Residue | Details |
| B | ARG18 |
| site_id | MCSA1 |
| Number of Residues | 1 |
| Details | M-CSA 811 |
| Chain | Residue | Details |
| A | ARG18 | electrostatic stabiliser |
| site_id | MCSA2 |
| Number of Residues | 1 |
| Details | M-CSA 811 |
| Chain | Residue | Details |
| B | ARG18 | electrostatic stabiliser |
