3KQA
MurA dead-end complex with terreic acid
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 |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0008360 | biological_process | regulation of cell shape |
| C | 0008760 | molecular_function | UDP-N-acetylglucosamine 1-carboxyvinyltransferase activity |
| C | 0009252 | biological_process | peptidoglycan biosynthetic process |
| C | 0016740 | molecular_function | transferase activity |
| C | 0016765 | molecular_function | transferase activity, transferring alkyl or aryl (other than methyl) groups |
| C | 0019277 | biological_process | UDP-N-acetylgalactosamine biosynthetic process |
| C | 0051301 | biological_process | cell division |
| C | 0071555 | biological_process | cell wall organization |
| D | 0003824 | molecular_function | catalytic activity |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0008360 | biological_process | regulation of cell shape |
| D | 0008760 | molecular_function | UDP-N-acetylglucosamine 1-carboxyvinyltransferase activity |
| D | 0009252 | biological_process | peptidoglycan biosynthetic process |
| D | 0016740 | molecular_function | transferase activity |
| D | 0016765 | molecular_function | transferase activity, transferring alkyl or aryl (other than methyl) groups |
| D | 0019277 | biological_process | UDP-N-acetylgalactosamine biosynthetic process |
| D | 0051301 | biological_process | cell division |
| D | 0071555 | biological_process | cell wall organization |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE TR9 A 500 |
| Chain | Residue |
| A | CYS115 |
| A | HOH470 |
| A | HOH502 |
| A | HOH514 |
| B | GLU130 |
| B | HOH429 |
| A | ALA116 |
| A | LEU138 |
| A | CA420 |
| A | CA421 |
| A | HOH450 |
| A | HOH451 |
| A | HOH457 |
| A | HOH464 |
| site_id | AC2 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE TR9 B 500 |
| Chain | Residue |
| A | GLU130 |
| B | CYS115 |
| B | ALA116 |
| B | LYS137 |
| B | LEU138 |
| B | CA421 |
| B | CA422 |
| B | HOH458 |
| B | HOH466 |
| B | HOH503 |
| B | HOH524 |
| B | HOH531 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE TR9 C 500 |
| Chain | Residue |
| C | CYS115 |
| C | ALA116 |
| C | LEU138 |
| C | CA420 |
| C | CA421 |
| C | HOH489 |
| D | PHE127 |
| D | GLU130 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE TR9 D 500 |
| Chain | Residue |
| C | ILE126 |
| C | PHE127 |
| C | GLU130 |
| D | CYS115 |
| D | ALA116 |
| D | LEU138 |
| D | CA420 |
| D | CA421 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CA A 420 |
| Chain | Residue |
| A | LEU138 |
| A | HOH451 |
| A | HOH457 |
| A | TR9500 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA A 421 |
| Chain | Residue |
| A | ALA116 |
| A | HOH446 |
| A | HOH464 |
| A | HOH470 |
| A | TR9500 |
| A | HOH502 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA B 420 |
| Chain | Residue |
| A | ILE136 |
| B | ILE136 |
| B | HOH465 |
| B | HOH483 |
| B | HOH520 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA B 421 |
| Chain | Residue |
| B | LEU138 |
| B | HOH466 |
| B | TR9500 |
| B | HOH524 |
| B | HOH542 |
| site_id | AC9 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE CA B 422 |
| Chain | Residue |
| B | ALA116 |
| B | HOH425 |
| B | HOH476 |
| B | HOH490 |
| B | TR9500 |
| B | HOH503 |
| B | HOH531 |
| site_id | BC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA B 423 |
| Chain | Residue |
| B | PHE104 |
| B | GLN106 |
| B | HOH528 |
| B | HOH575 |
| C | ASN148 |
| site_id | BC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CA C 420 |
| Chain | Residue |
| C | ALA116 |
| C | HOH489 |
| C | TR9500 |
| site_id | BC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CA C 421 |
| Chain | Residue |
| C | LEU138 |
| C | TR9500 |
| D | GLU130 |
| site_id | BC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CA D 420 |
| Chain | Residue |
| C | GLU130 |
| D | LEU138 |
| D | HOH434 |
| D | TR9500 |
| site_id | BC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CA D 421 |
| Chain | Residue |
| D | ALA116 |
| D | HOH460 |
| D | TR9500 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: Proton donor => ECO:0000269|PubMed:20392080, ECO:0000269|PubMed:22378791, ECO:0007744|PDB:3LTH |
| Chain | Residue | Details |
| A | CYS115 | |
| B | CYS115 | |
| C | CYS115 | |
| D | CYS115 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:22378791, ECO:0007744|PDB:3SWQ |
| Chain | Residue | Details |
| A | LYS22 | |
| B | LYS22 | |
| C | LYS22 | |
| D | LYS22 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00111 |
| Chain | Residue | Details |
| A | ARG91 | |
| B | ARG91 | |
| C | ARG91 | |
| D | ARG91 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:20392080, ECO:0000269|PubMed:22378791, ECO:0007744|PDB:3LTH, ECO:0007744|PDB:3SWQ |
| Chain | Residue | Details |
| A | ARG120 | |
| D | ARG120 | |
| D | ASP305 | |
| D | ILE327 | |
| A | ASP305 | |
| A | ILE327 | |
| B | ARG120 | |
| B | ASP305 | |
| B | ILE327 | |
| C | ARG120 | |
| C | ASP305 | |
| C | ILE327 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:22378791, ECO:0007744|PDB:3SWQ |
| Chain | Residue | Details |
| A | LYS160 | |
| B | LYS160 | |
| C | LYS160 | |
| D | LYS160 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | MOD_RES: 2-(S-cysteinyl)pyruvic acid O-phosphothioketal => ECO:0000269|PubMed:22378791 |
| Chain | Residue | Details |
| A | CYS115 | |
| B | CYS115 | |
| C | CYS115 | |
| D | CYS115 |
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 | CYS115 | 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 |
| 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 | CYS115 | activator, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor, proton relay |
| B | ARG120 | 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 |
| site_id | MCSA3 |
| Number of Residues | 6 |
| Details | M-CSA 369 |
| Chain | Residue | Details |
| C | LYS22 | electrostatic stabiliser, hydrogen bond donor, proton acceptor, proton donor |
| C | ASN23 | electrostatic stabiliser, hydrogen bond donor |
| C | CYS115 | activator, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor, proton relay |
| C | ARG120 | electrostatic stabiliser, proton acceptor, proton donor |
| C | ASP305 | activator, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| C | ARG397 | electrostatic stabiliser, hydrogen bond donor, proton acceptor, proton donor |
| site_id | MCSA4 |
| Number of Residues | 6 |
| Details | M-CSA 369 |
| Chain | Residue | Details |
| D | LYS22 | electrostatic stabiliser, hydrogen bond donor, proton acceptor, proton donor |
| D | ASN23 | electrostatic stabiliser, hydrogen bond donor |
| D | CYS115 | activator, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor, proton relay |
| D | ARG120 | electrostatic stabiliser, proton acceptor, proton donor |
| D | ASP305 | activator, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| D | ARG397 | electrostatic stabiliser, hydrogen bond donor, proton acceptor, proton donor |
