3TWD
glmuC1 in complex with an antibacterial inhibitor
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003977 | molecular_function | UDP-N-acetylglucosamine diphosphorylase activity |
| A | 0006048 | biological_process | UDP-N-acetylglucosamine biosynthetic process |
| A | 0016740 | molecular_function | transferase activity |
| A | 0019134 | molecular_function | glucosamine-1-phosphate N-acetyltransferase activity |
| B | 0003977 | molecular_function | UDP-N-acetylglucosamine diphosphorylase activity |
| B | 0006048 | biological_process | UDP-N-acetylglucosamine biosynthetic process |
| B | 0016740 | molecular_function | transferase activity |
| B | 0019134 | molecular_function | glucosamine-1-phosphate N-acetyltransferase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE SO4 B 1 |
| Chain | Residue |
| B | HOH4 |
| B | HOH158 |
| B | HOH183 |
| B | ARG333 |
| B | LYS351 |
| B | HIS363 |
| B | TYR366 |
| B | ASN386 |
| B | LYS392 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE SO4 A 2 |
| Chain | Residue |
| A | HOH12 |
| A | HOH104 |
| A | HOH142 |
| A | ARG333 |
| A | LYS351 |
| A | HIS363 |
| A | TYR366 |
| A | ASN386 |
| A | LYS392 |
| site_id | AC3 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE GOB A 1 |
| Chain | Residue |
| A | HOH114 |
| A | HOH205 |
| A | ASN377 |
| A | GLY379 |
| A | ALA380 |
| A | CYS385 |
| A | TYR387 |
| A | ASP388 |
| A | PHE402 |
| A | GLY404 |
| A | SER405 |
| A | VAL410 |
| A | ALA411 |
| A | ALA422 |
| A | ALA423 |
| A | ARG440 |
| A | PRO452 |
| A | HOH472 |
| site_id | AC4 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE GOB B 454 |
| Chain | Residue |
| B | HOH116 |
| B | HOH220 |
| B | ASN377 |
| B | GLY379 |
| B | ALA380 |
| B | CYS385 |
| B | ASN386 |
| B | TYR387 |
| B | ASP388 |
| B | PHE402 |
| B | GLY404 |
| B | SER405 |
| B | VAL410 |
| B | ALA411 |
| B | ALA422 |
| B | ALA423 |
| B | ARG440 |
| B | TRP449 |
| B | PRO452 |
| B | HOH455 |
| B | HOH472 |
Functional Information from PROSITE/UniProt
| site_id | PS00101 |
| Number of Residues | 29 |
| Details | HEXAPEP_TRANSFERASES Hexapeptide-repeat containing-transferases signature. VGsdTqLvapVtVGkgAtIAagTtVtrnV |
| Chain | Residue | Details |
| A | VAL403-VAL431 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_01631","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01631","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"11329257","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17473010","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01631","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"11329257","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17473010","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21984832","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01631","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"17473010","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21984832","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01631","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
