2RL1
Crystal structure of UDP-N-acetylglucosamine enolpyruvyl transferase from Haemophilus influenzae in complex with UDP-N-acetylglucosamine
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0008360 | biological_process | regulation of cell shape |
| A | 0008760 | molecular_function | UDP-N-acetylglucosamine 1-carboxyvinyltransferase activity |
| A | 0009252 | biological_process | peptidoglycan biosynthetic process |
| A | 0016740 | molecular_function | transferase activity |
| A | 0016765 | molecular_function | transferase activity, transferring alkyl or aryl (other than methyl) groups |
| A | 0019277 | biological_process | UDP-N-acetylgalactosamine biosynthetic process |
| A | 0051301 | biological_process | cell division |
| A | 0071555 | biological_process | cell wall organization |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE SO4 A 713 |
| Chain | Residue |
| A | ARG93 |
| A | CYS117 |
| A | ARG399 |
| A | HOH717 |
| A | HOH727 |
| A | HOH779 |
| A | HOH793 |
| A | HOH798 |
| A | HOH1018 |
| site_id | AC2 |
| Number of Residues | 28 |
| Details | BINDING SITE FOR RESIDUE UD1 A 712 |
| Chain | Residue |
| A | ASN23 |
| A | ALA94 |
| A | TRP97 |
| A | ALA121 |
| A | ARG122 |
| A | PRO123 |
| A | ASP125 |
| A | LEU126 |
| A | HIS127 |
| A | LYS162 |
| A | SER164 |
| A | GLY166 |
| A | THR306 |
| A | ASP307 |
| A | ILE329 |
| A | PHE330 |
| A | ARG333 |
| A | HOH714 |
| A | HOH716 |
| A | HOH719 |
| A | HOH725 |
| A | HOH744 |
| A | HOH792 |
| A | HOH795 |
| A | HOH886 |
| A | HOH979 |
| A | HOH1028 |
| A | HOH1058 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"HAMAP-Rule","id":"MF_00111","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"22378791","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"22378791","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"3SWE","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00111","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"22378791","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3SWE","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"2-(S-cysteinyl)pyruvic acid O-phosphothioketal","evidences":[{"source":"HAMAP-Rule","id":"MF_00111","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"22378791","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1uae |
| Chain | Residue | Details |
| A | CYS117 | |
| A | ASP307 | |
| A | ASN23 | |
| A | ARG399 |
