3SWQ
E. Cloacae MurA in complex with Enolpyruvyl-UNAG
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 PGE A 420 |
| Chain | Residue |
| A | GLN108 |
| A | GLU140 |
| A | TYR142 |
| A | LYS144 |
| site_id | AC2 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE PEG A 421 |
| Chain | Residue |
| A | ARG220 |
| A | EDO433 |
| A | HOH492 |
| A | HOH610 |
| A | HOH672 |
| A | GLU36 |
| A | ALA102 |
| A | ARG103 |
| A | ARG150 |
| A | GLU219 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO A 422 |
| Chain | Residue |
| A | ARG120 |
| A | HIS125 |
| A | GLY164 |
| A | EPU440 |
| A | HOH458 |
| A | HOH491 |
| A | HOH581 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO A 423 |
| Chain | Residue |
| A | ASN79 |
| A | SER81 |
| A | PRO83 |
| A | HIS285 |
| A | GLY286 |
| A | HOH501 |
| site_id | AC5 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE EDO A 424 |
| Chain | Residue |
| A | ARG252 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO A 425 |
| Chain | Residue |
| A | ILE205 |
| A | SER206 |
| A | GLN208 |
| A | HOH655 |
| A | HOH724 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO A 426 |
| Chain | Residue |
| A | LYS160 |
| A | VAL161 |
| A | ARG295 |
| A | ALA297 |
| A | HOH473 |
| A | HOH737 |
| A | HOH812 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO A 427 |
| Chain | Residue |
| A | ALA116 |
| A | MET333 |
| A | HOH609 |
| A | HOH815 |
| A | HOH826 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO A 428 |
| Chain | Residue |
| A | VAL192 |
| A | ASN196 |
| A | GLN208 |
| A | HOH849 |
| site_id | BC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO A 429 |
| Chain | Residue |
| A | ILE126 |
| A | ILE339 |
| A | HIS344 |
| A | EDO434 |
| A | HOH460 |
| site_id | BC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO A 430 |
| Chain | Residue |
| A | GLU37 |
| A | ALA200 |
| A | LEU201 |
| A | GLY202 |
| A | GLY222 |
| A | GLY223 |
| A | HOH813 |
| site_id | BC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO A 431 |
| Chain | Residue |
| A | ALA154 |
| A | HIS155 |
| A | THR179 |
| site_id | BC4 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE EDO A 432 |
| Chain | Residue |
| A | GLY118 |
| A | ALA119 |
| A | ILE327 |
| A | PHE328 |
| A | GLU329 |
| A | ASN330 |
| A | HOH626 |
| A | HOH838 |
| A | HOH850 |
| site_id | BC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO A 433 |
| Chain | Residue |
| A | GLU36 |
| A | ARG103 |
| A | PEG421 |
| site_id | BC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO A 434 |
| Chain | Residue |
| A | PRO121 |
| A | VAL122 |
| A | EDO429 |
| A | HOH484 |
| site_id | BC7 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO A 435 |
| Chain | Residue |
| A | GLN7 |
| A | GLY8 |
| A | PRO9 |
| A | THR10 |
| A | LYS63 |
| A | VAL64 |
| A | ASN412 |
| site_id | BC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO A 436 |
| Chain | Residue |
| A | VAL199 |
| A | GLY202 |
| A | ALA203 |
| A | HOH648 |
| A | HOH795 |
| site_id | BC9 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO A 437 |
| Chain | Residue |
| A | GLY133 |
| A | HOH470 |
| A | HOH811 |
| site_id | CC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO A 438 |
| Chain | Residue |
| A | GLU65 |
| A | TRP71 |
| A | HOH624 |
| site_id | CC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ACT A 439 |
| Chain | Residue |
| A | GLU329 |
| A | ILE347 |
| A | GLU348 |
| A | SER349 |
| A | HOH756 |
| A | LYS160 |
| site_id | CC3 |
| Number of Residues | 31 |
| Details | BINDING SITE FOR RESIDUE EPU A 440 |
| Chain | Residue |
| A | LYS22 |
| A | ASN23 |
| A | TRP95 |
| A | ALA119 |
| A | ARG120 |
| A | PRO121 |
| A | VAL122 |
| A | ASP123 |
| A | LEU124 |
| A | HIS125 |
| A | LYS160 |
| A | SER162 |
| A | VAL163 |
| A | GLY164 |
| A | THR304 |
| A | ASP305 |
| A | ILE327 |
| A | PHE328 |
| A | LEU370 |
| A | EDO422 |
| A | HOH452 |
| A | HOH458 |
| A | HOH471 |
| A | HOH477 |
| A | HOH497 |
| A | HOH520 |
| A | HOH551 |
| A | HOH628 |
| A | HOH638 |
| A | HOH661 |
| A | HOH704 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"20392080","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22378791","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3LTH","evidenceCode":"ECO:0007744"}]} |
| 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":"3SWQ","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 | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"20392080","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22378791","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3LTH","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3SWQ","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"22378791","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3SWQ","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"2-(S-cysteinyl)pyruvic acid O-phosphothioketal","evidences":[{"source":"PubMed","id":"22378791","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
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 | ALA119 | activator, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor, proton relay |
| A | LEU124 | electrostatic stabiliser, proton acceptor, proton donor |
| A | GLN309 | activator, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| A | ARG401 | electrostatic stabiliser, hydrogen bond donor, proton acceptor, proton donor |
