2QF7
Crystal structure of a complete multifunctional pyruvate carboxylase from Rhizobium etli
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004736 | molecular_function | pyruvate carboxylase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006090 | biological_process | pyruvate metabolic process |
| A | 0006094 | biological_process | gluconeogenesis |
| A | 0016874 | molecular_function | ligase activity |
| A | 0044281 | biological_process | small molecule metabolic process |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0004736 | molecular_function | pyruvate carboxylase activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006090 | biological_process | pyruvate metabolic process |
| B | 0006094 | biological_process | gluconeogenesis |
| B | 0016874 | molecular_function | ligase activity |
| B | 0044281 | biological_process | small molecule metabolic process |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN B 1155 |
| Chain | Residue |
| B | ASP549 |
| B | KCX718 |
| B | HIS747 |
| B | HIS749 |
| B | HOH1335 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG B 1156 |
| Chain | Residue |
| B | GLU283 |
| B | GLU297 |
| B | AGS1161 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG B 1157 |
| Chain | Residue |
| B | AGS1161 |
| B | HOH1673 |
| B | GLU297 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG B 1158 |
| Chain | Residue |
| B | MET534 |
| B | ARG535 |
| B | GLU537 |
| B | ASP768 |
| B | HOH1359 |
| B | HOH1430 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG A 1155 |
| Chain | Residue |
| A | GLU283 |
| A | GLU297 |
| A | AGS1162 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG A 1156 |
| Chain | Residue |
| A | GLU297 |
| A | ASN299 |
| A | AGS1162 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN A 1157 |
| Chain | Residue |
| A | ASP549 |
| A | KCX718 |
| A | HIS747 |
| A | HIS749 |
| A | HOH1476 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG A 1158 |
| Chain | Residue |
| A | MET534 |
| A | ARG535 |
| A | GLU537 |
| A | ASP768 |
| A | HOH1203 |
| A | HOH1375 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CL B 1159 |
| Chain | Residue |
| B | TYR987 |
| B | PRO988 |
| B | LYS989 |
| B | VAL990 |
| B | HOH1270 |
| site_id | BC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL A 1159 |
| Chain | Residue |
| A | TYR987 |
| A | PRO988 |
| A | LYS989 |
| A | VAL990 |
| site_id | BC2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL B 1160 |
| Chain | Residue |
| B | ILE65 |
| B | GLU66 |
| site_id | BC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL A 1160 |
| Chain | Residue |
| A | GLY63 |
| A | PRO64 |
| A | ILE65 |
| A | GLU66 |
| site_id | BC4 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE COA A 1161 |
| Chain | Residue |
| A | ARG427 |
| A | ARG469 |
| A | GLN470 |
| A | ASP471 |
| A | ARG472 |
| A | ALA473 |
| A | ILE1026 |
| A | LYS1030 |
| A | THR1031 |
| A | LEU1032 |
| A | LEU1054 |
| A | ASN1055 |
| A | HOH1764 |
| B | PHE44 |
| B | HOH1624 |
| site_id | BC5 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE AGS B 1161 |
| Chain | Residue |
| B | LYS166 |
| B | MET176 |
| B | GLU208 |
| B | LYS209 |
| B | VAL211 |
| B | HIS216 |
| B | GLN240 |
| B | ASN243 |
| B | LYS245 |
| B | GLU283 |
| B | LEU285 |
| B | ILE296 |
| B | GLU297 |
| B | ASN299 |
| B | THR454 |
| B | MG1156 |
| B | MG1157 |
| B | HOH1638 |
| B | HOH1775 |
| site_id | BC6 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE AGS A 1162 |
| Chain | Residue |
| A | HIS216 |
| A | GLN240 |
| A | ASN243 |
| A | LYS245 |
| A | GLU283 |
| A | LEU285 |
| A | ILE296 |
| A | GLU297 |
| A | ASN299 |
| A | THR454 |
| A | MG1155 |
| A | MG1156 |
| A | HOH1709 |
| A | HOH1760 |
| A | HOH1774 |
| site_id | BC7 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL B 1162 |
| Chain | Residue |
| B | LEU25 |
| B | HIS323 |
| B | PRO333 |
| B | GLY336 |
| B | HOH1317 |
| B | HOH1406 |
| B | HOH1408 |
| B | HOH1747 |
| A | HOH1778 |
| site_id | BC8 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE FMT B 1163 |
| Chain | Residue |
| A | ALA376 |
| A | SER377 |
| B | ARG20 |
| B | LEU383 |
| B | GLY385 |
| B | GLY386 |
| B | HOH1263 |
| site_id | BC9 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE FMT A 1163 |
| Chain | Residue |
| A | ARG20 |
| A | LEU383 |
| A | GLY385 |
| A | GLY386 |
| B | SER375 |
| B | ALA376 |
| B | SER377 |
| B | HOH1276 |
Functional Information from PROSITE/UniProt
| site_id | PS00188 |
| Number of Residues | 18 |
| Details | BIOTIN Biotin-requiring enzymes attachment site. GDvLvsIeAMKMetaIhA |
| Chain | Residue | Details |
| A | GLY1109-ALA1126 |
| site_id | PS00866 |
| Number of Residues | 15 |
| Details | CPSASE_1 Carbamoyl-phosphate synthase subdomain signature 1. YPVMLKASwggGGrG |
| Chain | Residue | Details |
| A | TYR161-GLY175 |
| site_id | PS00867 |
| Number of Residues | 8 |
| Details | CPSASE_2 Carbamoyl-phosphate synthase subdomain signature 2. FIEVNPRI |
| Chain | Residue | Details |
| A | PHE295-ILE302 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | a catalytic site defined by CSA, PubMed 17717183 |
| Chain | Residue | Details |
| A | ASP655 | |
| A | KCX718 | |
| A | ASP549 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | a catalytic site defined by CSA, PubMed 17717183 |
| Chain | Residue | Details |
| B | ASP655 | |
| B | ASP549 |
| site_id | MCSA1 |
| Number of Residues | 11 |
| Details | M-CSA 223 |
| Chain | Residue | Details |
| A | GLU283 | metal ligand |
| A | GLY753 | metal ligand |
| A | LYS886 | proton acceptor, proton donor, proton relay |
| A | GLU297 | metal ligand |
| A | ASN299 | metal ligand |
| A | GLU305 | electrostatic stabiliser, proton acceptor, proton donor |
| A | ARG353 | activator, electrostatic stabiliser |
| A | ASP549 | hydrogen bond acceptor, hydrogen bond donor, metal ligand, proton acceptor, proton donor |
| A | ASP655 | activator, metal ligand |
| A | KCX718 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| A | THR751 | metal ligand |
| site_id | MCSA2 |
| Number of Residues | 11 |
| Details | M-CSA 223 |
| Chain | Residue | Details |
| B | GLU283 | metal ligand |
| B | GLY753 | metal ligand |
| B | LYS886 | proton acceptor, proton donor, proton relay |
| B | GLU297 | metal ligand |
| B | ASN299 | metal ligand |
| B | GLU305 | electrostatic stabiliser, proton acceptor, proton donor |
| B | ARG353 | activator, electrostatic stabiliser |
| B | ASP549 | hydrogen bond acceptor, hydrogen bond donor, metal ligand, proton acceptor, proton donor |
| B | ASP655 | activator, metal ligand |
| B | KCX718 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| B | THR751 | metal ligand |
