3SWA
E. Cloacae MurA R120A complex with UNAG 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 |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0008360 | biological_process | regulation of cell shape |
| B | 0008760 | molecular_function | UDP-N-acetylglucosamine 1-carboxyvinyltransferase activity |
| B | 0009252 | biological_process | peptidoglycan biosynthetic process |
| B | 0016740 | molecular_function | transferase activity |
| B | 0016765 | molecular_function | transferase activity, transferring alkyl or aryl (other than methyl) groups |
| B | 0019277 | biological_process | UDP-N-acetylgalactosamine biosynthetic process |
| B | 0051301 | biological_process | cell division |
| B | 0071555 | biological_process | cell wall organization |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO A 420 |
| Chain | Residue |
| A | GLU400 |
| A | ARG401 |
| A | LYS405 |
| A | HOH660 |
| A | HOH709 |
| A | HOH792 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO A 421 |
| Chain | Residue |
| A | ASN330 |
| A | ARG331 |
| A | PHE332 |
| A | SER349 |
| A | GLU325 |
| A | PHE328 |
| A | GLU329 |
| site_id | AC3 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE EDO A 422 |
| Chain | Residue |
| A | GLU348 |
| A | SER349 |
| A | ASN350 |
| A | THR351 |
| A | HOH525 |
| B | PRO121 |
| B | VAL122 |
| B | ASP123 |
| B | LEU138 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO A 423 |
| Chain | Residue |
| A | ARG91 |
| A | ALA92 |
| A | ILE94 |
| A | TRP95 |
| A | UD1425 |
| A | HOH557 |
| A | HOH810 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO A 424 |
| Chain | Residue |
| A | GLU37 |
| A | PRO38 |
| A | HOH766 |
| site_id | AC6 |
| Number of Residues | 31 |
| Details | BINDING SITE FOR RESIDUE UD1 A 425 |
| Chain | Residue |
| A | ASN23 |
| A | TRP95 |
| A | ALA119 |
| A | PRO121 |
| A | VAL122 |
| A | ASP123 |
| A | LEU124 |
| A | HIS125 |
| A | SER162 |
| A | VAL163 |
| A | GLY164 |
| A | THR304 |
| A | ASP305 |
| A | ILE327 |
| A | PHE328 |
| A | ARG331 |
| A | EDO423 |
| A | HOH426 |
| A | HOH434 |
| A | HOH436 |
| A | HOH444 |
| A | HOH450 |
| A | HOH493 |
| A | HOH557 |
| A | HOH566 |
| A | HOH568 |
| A | HOH661 |
| A | HOH720 |
| A | HOH721 |
| A | HOH728 |
| A | HOH734 |
| site_id | AC7 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE EDO B 420 |
| Chain | Residue |
| A | PRO121 |
| A | VAL122 |
| A | ASP123 |
| A | LEU138 |
| B | GLU348 |
| B | SER349 |
| B | ASN350 |
| B | THR351 |
| B | HOH683 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO B 421 |
| Chain | Residue |
| B | GLU325 |
| B | PHE328 |
| B | GLU329 |
| B | ASN330 |
| B | ARG331 |
| B | PHE332 |
| B | SER349 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO B 422 |
| Chain | Residue |
| B | GLN7 |
| B | ASN412 |
| B | ILE413 |
| B | HOH572 |
| site_id | BC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO B 423 |
| Chain | Residue |
| B | ARG91 |
| B | ALA92 |
| B | ILE94 |
| B | UD1426 |
| B | HOH466 |
| B | HOH570 |
| B | HOH606 |
| site_id | BC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO B 424 |
| Chain | Residue |
| B | ASP2 |
| B | TYR393 |
| B | ARG415 |
| site_id | BC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO B 425 |
| Chain | Residue |
| B | THR10 |
| B | ARG11 |
| B | SER245 |
| B | ILE382 |
| B | HOH658 |
| site_id | BC4 |
| Number of Residues | 29 |
| Details | BINDING SITE FOR RESIDUE UD1 B 426 |
| Chain | Residue |
| B | TRP95 |
| B | ALA119 |
| B | PRO121 |
| B | VAL122 |
| B | ASP123 |
| B | LEU124 |
| B | HIS125 |
| B | SER162 |
| B | VAL163 |
| B | GLY164 |
| B | THR304 |
| B | ASP305 |
| B | ILE327 |
| B | PHE328 |
| B | ARG331 |
| B | EDO423 |
| B | HOH429 |
| B | HOH437 |
| B | HOH455 |
| B | HOH458 |
| B | HOH466 |
| B | HOH494 |
| B | HOH583 |
| B | HOH591 |
| B | HOH606 |
| B | HOH641 |
| B | HOH661 |
| B | HOH668 |
| B | ASN23 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton donor => ECO:0000269|PubMed:20392080, ECO:0000269|PubMed:22378791, ECO:0007744|PDB:3LTH |
| Chain | Residue | Details |
| A | QPA115 | |
| B | QPA115 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:22378791, ECO:0007744|PDB:3SWQ |
| Chain | Residue | Details |
| A | LYS22 | |
| B | LYS22 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00111 |
| Chain | Residue | Details |
| A | ARG91 | |
| B | ARG91 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:20392080, ECO:0000269|PubMed:22378791, ECO:0007744|PDB:3LTH, ECO:0007744|PDB:3SWQ |
| Chain | Residue | Details |
| A | ALA120 | |
| A | ASP305 | |
| A | ILE327 | |
| B | ALA120 | |
| B | ASP305 | |
| B | ILE327 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:22378791, ECO:0007744|PDB:3SWQ |
| Chain | Residue | Details |
| A | LYS160 | |
| B | LYS160 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | MOD_RES: 2-(S-cysteinyl)pyruvic acid O-phosphothioketal => ECO:0000269|PubMed:22378791 |
| Chain | Residue | Details |
| A | QPA115 | |
| B | 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 | ALA120 | 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 |
| site_id | MCSA2 |
| Number of Residues | 6 |
| Details | M-CSA 369 |
| Chain | Residue | Details |
| B | LYS22 | electrostatic stabiliser, hydrogen bond donor, proton acceptor, proton donor |
| B | ASN23 | electrostatic stabiliser, hydrogen bond donor |
| B | QPA115 | activator, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor, proton relay |
| B | ALA120 | electrostatic stabiliser, proton acceptor, proton donor |
| B | ASP305 | activator, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| B | ARG397 | electrostatic stabiliser, hydrogen bond donor, proton acceptor, proton donor |
