3SWI
E. Cloacae MurA in complex with Enolpyruvyl-UDP-N-acetylgalactosamine and covalent adduct of PEP with CYS115
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 | 4 |
Details | BINDING SITE FOR RESIDUE MOE A 420 |
Chain | Residue |
A | PRO121 |
A | HIS125 |
A | GLY164 |
A | UPN427 |
site_id | AC2 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE MOE A 421 |
Chain | Residue |
A | LYS248 |
A | VAL250 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE PG0 A 422 |
Chain | Residue |
A | TYR142 |
A | LYS144 |
A | HOH529 |
A | SER81 |
A | GLN108 |
A | GLU140 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE PG0 A 423 |
Chain | Residue |
A | LYS55 |
A | GLN59 |
A | LEU86 |
A | ILE244 |
A | GLY286 |
site_id | AC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE PG0 A 424 |
Chain | Residue |
A | VAL192 |
A | ASP193 |
A | ASN196 |
A | LEU229 |
A | GLN255 |
site_id | AC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG A 425 |
Chain | Residue |
A | QPA115 |
A | UD2426 |
A | HOH472 |
A | HOH500 |
A | HOH537 |
site_id | AC7 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE UD2 A 426 |
Chain | Residue |
A | LYS88 |
A | THR89 |
A | GLY114 |
A | QPA115 |
A | GLU337 |
A | MET366 |
A | THR368 |
A | ARG391 |
A | TYR393 |
A | HIS394 |
A | MG425 |
A | HOH469 |
A | HOH472 |
A | HOH537 |
site_id | AC8 |
Number of Residues | 18 |
Details | BINDING SITE FOR RESIDUE UPN A 427 |
Chain | Residue |
A | LYS22 |
A | ASN23 |
A | TRP95 |
A | ALA119 |
A | ARG120 |
A | PRO121 |
A | VAL122 |
A | ASP123 |
A | LEU124 |
A | LYS160 |
A | SER162 |
A | VAL163 |
A | GLY164 |
A | ASP305 |
A | ILE327 |
A | MOE420 |
A | HOH441 |
A | HOH442 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | ACT_SITE: Proton donor => ECO:0000269|PubMed:20392080, ECO:0000269|PubMed:22378791, ECO:0007744|PDB:3LTH |
Chain | Residue | Details |
A | QPA115 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000305|PubMed:22378791, ECO:0007744|PDB:3SWQ |
Chain | Residue | Details |
A | LYS22 |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00111 |
Chain | Residue | Details |
A | ARG91 |
site_id | SWS_FT_FI4 |
Number of Residues | 3 |
Details | BINDING: BINDING => ECO:0000269|PubMed:20392080, ECO:0000269|PubMed:22378791, ECO:0007744|PDB:3LTH, ECO:0007744|PDB:3SWQ |
Chain | Residue | Details |
A | ARG120 | |
A | ASP305 | |
A | ILE327 |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000269|PubMed:22378791, ECO:0007744|PDB:3SWQ |
Chain | Residue | Details |
A | LYS160 |
site_id | SWS_FT_FI6 |
Number of Residues | 1 |
Details | MOD_RES: 2-(S-cysteinyl)pyruvic acid O-phosphothioketal => ECO:0000269|PubMed:22378791 |
Chain | Residue | Details |
A | QPA115 |
Catalytic Information from CSA
site_id | MCSA1 |
Number of Residues | 6 |
Details | M-CSA 369 |
Chain | Residue | Details |
A | LYS22 | electrostatic stabiliser, hydrogen bond donor, proton acceptor, proton donor |
A | ASN23 | electrostatic stabiliser, hydrogen bond donor |
A | QPA115 | activator, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor, proton relay |
A | ARG120 | electrostatic stabiliser, proton acceptor, proton donor |
A | ASP305 | activator, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
A | ARG397 | electrostatic stabiliser, hydrogen bond donor, proton acceptor, proton donor |