3RV3
Crystal structure of E.coli biotin carboxylase in complex with two ADP and one Mg ion
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0003989 | molecular_function | acetyl-CoA carboxylase activity |
| A | 0004075 | molecular_function | biotin carboxylase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006633 | biological_process | fatty acid biosynthetic process |
| A | 0009317 | cellular_component | acetyl-CoA carboxylase complex |
| A | 0016874 | molecular_function | ligase activity |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0045717 | biological_process | negative regulation of fatty acid biosynthetic process |
| A | 0046872 | molecular_function | metal ion binding |
| A | 2001295 | biological_process | malonyl-CoA biosynthetic process |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0003989 | molecular_function | acetyl-CoA carboxylase activity |
| B | 0004075 | molecular_function | biotin carboxylase activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0006633 | biological_process | fatty acid biosynthetic process |
| B | 0009317 | cellular_component | acetyl-CoA carboxylase complex |
| B | 0016874 | molecular_function | ligase activity |
| B | 0042803 | molecular_function | protein homodimerization activity |
| B | 0045717 | biological_process | negative regulation of fatty acid biosynthetic process |
| B | 0046872 | molecular_function | metal ion binding |
| B | 2001295 | biological_process | malonyl-CoA biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE ADP A 1000 |
| Chain | Residue |
| A | TYR82 |
| A | LYS238 |
| A | ASN290 |
| A | ARG292 |
| A | GLN294 |
| A | VAL295 |
| A | GLU296 |
| A | ARG338 |
| A | ASP382 |
| A | HOH547 |
| A | HOH561 |
| A | GLY83 |
| A | HOH699 |
| A | HOH747 |
| A | HOH758 |
| A | GLY162 |
| A | GLY163 |
| A | GLY164 |
| A | GLY165 |
| A | ARG167 |
| A | PHE193 |
| A | GLN237 |
| site_id | AC2 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE ADP A 1002 |
| Chain | Residue |
| A | LYS116 |
| A | LYS159 |
| A | GLY163 |
| A | GLY164 |
| A | GLY165 |
| A | GLY166 |
| A | MET169 |
| A | GLU201 |
| A | LYS202 |
| A | TYR203 |
| A | LEU204 |
| A | HIS209 |
| A | GLN233 |
| A | HIS236 |
| A | GLU276 |
| A | LEU278 |
| A | ILE287 |
| A | GLU288 |
| A | ILE437 |
| A | HOH547 |
| A | HOH668 |
| A | HOH684 |
| A | HOH736 |
| A | HOH758 |
| A | HOH804 |
| A | MG1004 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG A 1004 |
| Chain | Residue |
| A | GLU276 |
| A | GLU288 |
| A | HOH547 |
| A | HOH684 |
| A | HOH804 |
| A | ADP1002 |
| site_id | AC4 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE ADP B 1001 |
| Chain | Residue |
| B | LYS116 |
| B | LYS159 |
| B | GLY164 |
| B | GLY165 |
| B | GLY166 |
| B | MET169 |
| B | GLU201 |
| B | LYS202 |
| B | TYR203 |
| B | LEU204 |
| B | HIS209 |
| B | GLN233 |
| B | HIS236 |
| B | GLU276 |
| B | LEU278 |
| B | ILE287 |
| B | GLU288 |
| B | ILE437 |
| B | HOH545 |
| B | HOH561 |
| B | HOH582 |
| B | HOH732 |
| B | MG1005 |
| site_id | AC5 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE ADP B 1003 |
| Chain | Residue |
| B | HOH807 |
| B | HOH821 |
| B | TYR82 |
| B | GLY83 |
| B | GLY162 |
| B | GLY163 |
| B | GLY164 |
| B | GLY165 |
| B | PHE193 |
| B | LYS238 |
| B | ASN290 |
| B | ARG292 |
| B | GLN294 |
| B | VAL295 |
| B | GLU296 |
| B | ARG338 |
| B | ASP382 |
| B | HOH510 |
| B | HOH523 |
| B | HOH543 |
| B | HOH641 |
| B | HOH651 |
| B | HOH732 |
| B | HOH771 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG B 1005 |
| Chain | Residue |
| B | GLU276 |
| B | GLU288 |
| B | HOH545 |
| B | HOH732 |
| B | ADP1001 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: ACT_SITE => ECO:0000269|PubMed:19213731 |
| Chain | Residue | Details |
| A | ARG292 | |
| B | ARG292 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:10821865, ECO:0000269|PubMed:19213731, ECO:0007744|PDB:1DV2, ECO:0007744|PDB:3G8D |
| Chain | Residue | Details |
| A | LYS116 | |
| A | GLY165 | |
| B | LYS116 | |
| B | GLY165 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:19213731, ECO:0007744|PDB:3G8C, ECO:0007744|PDB:3G8D |
| Chain | Residue | Details |
| A | LYS159 | |
| B | LYS159 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:10821865, ECO:0000269|PubMed:19213731, ECO:0007744|PDB:1DV2, ECO:0007744|PDB:3G8C, ECO:0007744|PDB:3G8D |
| Chain | Residue | Details |
| A | GLU201 | |
| B | GLU201 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 10 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:19213731, ECO:0007744|PDB:3G8C |
| Chain | Residue | Details |
| A | HIS209 | |
| B | ARG338 | |
| A | LYS238 | |
| A | ARG292 | |
| A | VAL295 | |
| A | ARG338 | |
| B | HIS209 | |
| B | LYS238 | |
| B | ARG292 | |
| B | VAL295 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:10821865, ECO:0000269|PubMed:19213731, ECO:0007744|PDB:1DV2, ECO:0007744|PDB:3G8C |
| Chain | Residue | Details |
| A | HIS236 | |
| B | HIS236 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00409 |
| Chain | Residue | Details |
| A | GLU276 | |
| A | GLU288 | |
| A | ASN290 | |
| B | GLU276 | |
| B | GLU288 | |
| B | ASN290 |
