3TW6
Structure of Rhizobium etli pyruvate carboxylase T882A with the allosteric activator, acetyl coenzyme-A
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 |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0004736 | molecular_function | pyruvate carboxylase activity |
| C | 0005524 | molecular_function | ATP binding |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0006090 | biological_process | pyruvate metabolic process |
| C | 0006094 | biological_process | gluconeogenesis |
| C | 0016874 | molecular_function | ligase activity |
| C | 0044281 | biological_process | small molecule metabolic process |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0003824 | molecular_function | catalytic activity |
| D | 0004736 | molecular_function | pyruvate carboxylase activity |
| D | 0005524 | molecular_function | ATP binding |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0006090 | biological_process | pyruvate metabolic process |
| D | 0006094 | biological_process | gluconeogenesis |
| D | 0016874 | molecular_function | ligase activity |
| D | 0044281 | biological_process | small molecule metabolic process |
| D | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL A 1600 |
| Chain | Residue |
| A | GLY63 |
| A | PRO64 |
| A | ILE65 |
| A | GLU66 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL A 1601 |
| Chain | Residue |
| A | TYR987 |
| A | LYS989 |
| A | VAL990 |
| site_id | AC3 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE ADP A 2000 |
| Chain | Residue |
| A | VAL211 |
| A | HIS216 |
| A | GLN240 |
| A | ASN243 |
| A | LEU285 |
| A | GLU297 |
| A | MG2002 |
| A | LYS209 |
| A | LEU210 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN A 2001 |
| Chain | Residue |
| A | ASP549 |
| A | KCX718 |
| A | HIS747 |
| A | HIS749 |
| A | HOH1251 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG A 2002 |
| Chain | Residue |
| A | GLU283 |
| A | GLU297 |
| A | ADP2000 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG A 2005 |
| Chain | Residue |
| A | MET534 |
| A | ARG535 |
| A | GLU537 |
| A | ASP768 |
| A | HOH1182 |
| A | HOH1245 |
| site_id | AC7 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE COA A 4011 |
| Chain | Residue |
| A | ARG429 |
| A | ARG469 |
| A | GLN470 |
| A | ASP471 |
| A | ARG472 |
| A | THR1031 |
| A | LEU1032 |
| A | ASN1055 |
| B | ARG43 |
| B | PHE44 |
| B | HOH1343 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL B 1600 |
| Chain | Residue |
| B | GLY63 |
| B | ILE65 |
| B | GLU66 |
| site_id | AC9 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL B 1601 |
| Chain | Residue |
| B | TYR987 |
| B | LYS989 |
| B | VAL990 |
| site_id | BC1 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE ADP B 2000 |
| Chain | Residue |
| B | LYS124 |
| B | LYS166 |
| B | GLY171 |
| B | GLY173 |
| B | ARG174 |
| B | MET176 |
| B | GLU208 |
| B | LYS209 |
| B | LEU210 |
| B | VAL211 |
| B | HIS216 |
| B | GLN240 |
| B | ASN243 |
| B | GLU283 |
| B | LEU285 |
| B | GLU297 |
| B | THR454 |
| B | HOH1222 |
| B | HOH1223 |
| B | MG2002 |
| site_id | BC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN B 2001 |
| Chain | Residue |
| B | ASP549 |
| B | KCX718 |
| B | HIS747 |
| B | HIS749 |
| B | HOH1376 |
| site_id | BC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG B 2002 |
| Chain | Residue |
| B | GLU283 |
| B | GLU297 |
| B | HOH1228 |
| B | ADP2000 |
| site_id | BC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE BTI B 2003 |
| Chain | Residue |
| B | ARG353 |
| B | THR355 |
| B | ASP399 |
| B | ASN434 |
| B | LYS1119 |
| B | HOH1235 |
| site_id | BC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG B 2005 |
| Chain | Residue |
| B | MET534 |
| B | ARG535 |
| B | GLU537 |
| B | ASP768 |
| B | HOH1348 |
| B | HOH1349 |
| site_id | BC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL C 1600 |
| Chain | Residue |
| C | GLY63 |
| C | PRO64 |
| C | ILE65 |
| C | GLU66 |
| site_id | BC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL C 1601 |
| Chain | Residue |
| C | TYR987 |
| C | LYS989 |
| C | VAL990 |
| site_id | BC8 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE ADP C 2000 |
| Chain | Residue |
| C | LEU210 |
| C | VAL211 |
| C | HIS216 |
| C | GLN240 |
| C | GLU283 |
| C | GLU297 |
| C | THR454 |
| C | HOH1302 |
| C | MG2002 |
| C | PAE2003 |
| C | LYS166 |
| C | MET176 |
| C | GLU208 |
| C | LYS209 |
| site_id | BC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN C 2001 |
| Chain | Residue |
| C | ASP549 |
| C | KCX718 |
| C | HIS747 |
| C | HIS749 |
| C | HOH1160 |
| site_id | CC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG C 2002 |
| Chain | Residue |
| C | GLU283 |
| C | GLU297 |
| C | HOH1302 |
| C | ADP2000 |
| C | PAE2003 |
| site_id | CC2 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE PAE C 2003 |
| Chain | Residue |
| C | LYS245 |
| C | GLU283 |
| C | GLU297 |
| C | ASN299 |
| C | ARG301 |
| C | GLN303 |
| C | VAL304 |
| C | GLU305 |
| C | HOH1302 |
| C | HOH1304 |
| C | ADP2000 |
| C | MG2002 |
| site_id | CC3 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE COA C 4011 |
| Chain | Residue |
| C | ARG427 |
| C | ARG429 |
| C | LYS468 |
| C | ARG469 |
| C | GLN470 |
| C | ASP471 |
| C | ARG472 |
| C | ALA473 |
| C | ILE1026 |
| C | THR1031 |
| C | LEU1032 |
| D | PHE44 |
| D | HOH1263 |
| D | HOH1329 |
| site_id | CC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL D 1600 |
| Chain | Residue |
| D | GLY63 |
| D | PRO64 |
| D | ILE65 |
| D | GLU66 |
| site_id | CC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL D 1601 |
| Chain | Residue |
| D | TYR987 |
| D | LYS989 |
| D | VAL990 |
| site_id | CC6 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE ADP D 2000 |
| Chain | Residue |
| D | LYS166 |
| D | MET176 |
| D | LYS209 |
| D | LEU210 |
| D | VAL211 |
| D | HIS216 |
| D | GLN240 |
| D | ASN243 |
| D | GLU283 |
| D | LEU285 |
| D | GLU297 |
| D | THR454 |
| D | MG2002 |
| site_id | CC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN D 2001 |
| Chain | Residue |
| D | ASP549 |
| D | KCX718 |
| D | HIS747 |
| D | HIS749 |
| D | HOH1340 |
| site_id | CC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG D 2002 |
| Chain | Residue |
| D | GLU283 |
| D | GLU297 |
| D | ADP2000 |
| site_id | CC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG D 2005 |
| Chain | Residue |
| D | MET534 |
| D | ARG535 |
| D | GLU537 |
| D | ASP768 |
| D | HOH1156 |
| D | HOH1353 |
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 | 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 |
| site_id | MCSA3 |
| Number of Residues | 11 |
| Details | M-CSA 223 |
| Chain | Residue | Details |
| C | GLU283 | metal ligand |
| C | GLY753 | metal ligand |
| C | LYS886 | proton acceptor, proton donor, proton relay |
| C | GLU297 | metal ligand |
| C | ASN299 | metal ligand |
| C | GLU305 | electrostatic stabiliser, proton acceptor, proton donor |
| C | ARG353 | activator, electrostatic stabiliser |
| C | ASP549 | hydrogen bond acceptor, hydrogen bond donor, metal ligand, proton acceptor, proton donor |
| C | ASP655 | activator, metal ligand |
| C | KCX718 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| C | THR751 | metal ligand |
| site_id | MCSA4 |
| Number of Residues | 11 |
| Details | M-CSA 223 |
| Chain | Residue | Details |
| D | GLU283 | metal ligand |
| D | GLY753 | metal ligand |
| D | LYS886 | proton acceptor, proton donor, proton relay |
| D | GLU297 | metal ligand |
| D | ASN299 | metal ligand |
| D | GLU305 | electrostatic stabiliser, proton acceptor, proton donor |
| D | ARG353 | activator, electrostatic stabiliser |
| D | ASP549 | hydrogen bond acceptor, hydrogen bond donor, metal ligand, proton acceptor, proton donor |
| D | ASP655 | activator, metal ligand |
| D | KCX718 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| D | THR751 | metal ligand |
