3SWG
AQUIFEX AEOLICUS MurA in complex with UDP-N-acetylmuramic acid and covalent adduct of PEP with Cys124
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0005737 | cellular_component | cytoplasm |
| 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 | 6 |
| Details | BINDING SITE FOR RESIDUE PG4 A 501 |
| Chain | Residue |
| A | ASP132 |
| A | LYS139 |
| A | VAL145 |
| A | ASN350 |
| A | HOH898 |
| A | HOH928 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PG4 A 502 |
| Chain | Residue |
| A | GLU361 |
| A | LYS326 |
| A | THR352 |
| A | TYR359 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PG4 A 503 |
| Chain | Residue |
| A | GLU255 |
| A | LEU257 |
| A | ARG267 |
| A | ARG288 |
| A | HOH703 |
| A | HOH935 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PGE A 504 |
| Chain | Residue |
| A | LYS165 |
| A | PHE166 |
| A | ASP167 |
| A | ASN192 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PEG A 505 |
| Chain | Residue |
| A | PRO47 |
| A | THR49 |
| A | PHE231 |
| A | THR232 |
| A | HOH901 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PEG A 506 |
| Chain | Residue |
| A | ALA323 |
| A | LYS324 |
| A | VAL363 |
| A | GLU364 |
| A | HOH845 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO A 507 |
| Chain | Residue |
| A | ILE90 |
| A | TYR151 |
| A | TYR153 |
| site_id | AC8 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE EDO A 508 |
| Chain | Residue |
| A | ASN83 |
| site_id | AC9 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE EDO A 509 |
| Chain | Residue |
| A | ARG112 |
| A | GLY114 |
| site_id | BC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO A 510 |
| Chain | Residue |
| A | GLU146 |
| A | ARG148 |
| A | TYR153 |
| site_id | BC2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE EDO A 511 |
| Chain | Residue |
| A | ARG60 |
| A | ARG67 |
| site_id | BC3 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE EDO A 512 |
| Chain | Residue |
| A | PHE290 |
| site_id | BC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO A 513 |
| Chain | Residue |
| A | ASN284 |
| A | GLY285 |
| A | ASN286 |
| site_id | BC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO A 514 |
| Chain | Residue |
| A | LYS214 |
| A | TYR221 |
| A | ARG365 |
| site_id | BC6 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE EDO A 515 |
| Chain | Residue |
| A | HIS163 |
| A | GLU191 |
| site_id | BC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO A 516 |
| Chain | Residue |
| A | GLU187 |
| A | LYS223 |
| A | GLN390 |
| site_id | BC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO A 517 |
| Chain | Residue |
| A | LEU43 |
| A | GLU45 |
| A | GLU226 |
| A | HOH701 |
| A | HOH863 |
| site_id | BC9 |
| Number of Residues | 32 |
| Details | BINDING SITE FOR RESIDUE EPZ A 518 |
| Chain | Residue |
| A | LYS31 |
| A | ASN32 |
| A | ALA101 |
| A | ARG129 |
| A | PRO130 |
| A | ILE131 |
| A | ASP132 |
| A | GLN133 |
| A | LEU168 |
| A | THR170 |
| A | VAL171 |
| A | THR172 |
| A | THR310 |
| A | ASP311 |
| A | ILE333 |
| A | PHE334 |
| A | VAL353 |
| A | LEU376 |
| A | HOH604 |
| A | HOH609 |
| A | HOH615 |
| A | HOH624 |
| A | HOH628 |
| A | HOH633 |
| A | HOH635 |
| A | HOH638 |
| A | HOH640 |
| A | HOH641 |
| A | HOH648 |
| A | HOH804 |
| A | HOH805 |
| A | HOH807 |
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":"2YVW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3SWG","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":"2YVW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3SWG","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 |
