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 |