1OKC
structure of mitochondrial ADP/ATP carrier in complex with carboxyatractyloside
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005471 | molecular_function | ATP:ADP antiporter activity |
A | 0005739 | cellular_component | mitochondrion |
A | 0005743 | cellular_component | mitochondrial inner membrane |
A | 0005757 | cellular_component | mitochondrial permeability transition pore complex |
A | 0015297 | molecular_function | antiporter activity |
A | 0015866 | biological_process | ADP transport |
A | 0017077 | molecular_function | oxidative phosphorylation uncoupler activity |
A | 0031966 | cellular_component | mitochondrial membrane |
A | 0046902 | biological_process | regulation of mitochondrial membrane permeability |
A | 0055085 | biological_process | transmembrane transport |
A | 0140021 | biological_process | mitochondrial ADP transmembrane transport |
A | 1901029 | biological_process | negative regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway |
A | 1901526 | biological_process | positive regulation of mitophagy |
A | 1902600 | biological_process | proton transmembrane transport |
A | 1990544 | biological_process | mitochondrial ATP transmembrane transport |
A | 1990845 | biological_process | adaptive thermogenesis |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 18 |
Details | BINDING SITE FOR RESIDUE CXT A 401 |
Chain | Residue |
A | ARG79 |
A | PHE230 |
A | ASP231 |
A | ARG234 |
A | HOH2004 |
A | HOH2038 |
A | HOH2076 |
A | HOH2077 |
A | HOH2078 |
A | HOH2079 |
A | ASN87 |
A | LYS91 |
A | GLY123 |
A | LEU127 |
A | GLY182 |
A | ILE183 |
A | ARG187 |
A | SER227 |
site_id | AC2 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE CDL A 800 |
Chain | Residue |
A | TRP70 |
A | ARG71 |
A | GLY72 |
A | ASN73 |
A | LEU74 |
A | TRP109 |
A | LEU140 |
A | PC1980 |
A | HOH2024 |
A | HOH2080 |
site_id | AC3 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE CDL A 801 |
Chain | Residue |
A | ILE53 |
A | ILE54 |
A | PHE270 |
A | GLY272 |
A | ALA273 |
A | TRP274 |
A | SER275 |
A | PC1983 |
A | HOH2083 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CDL A 802 |
Chain | Residue |
A | CYS128 |
A | PHE176 |
A | ASN177 |
A | GLN181 |
A | LEU289 |
site_id | AC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE LDM A 903 |
Chain | Residue |
A | PRO266 |
A | PHE269 |
A | PHE270 |
A | LDM904 |
site_id | AC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE LDM A 904 |
Chain | Residue |
A | VAL226 |
A | PRO229 |
A | PHE230 |
A | TRP257 |
A | LDM903 |
site_id | AC7 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE PC1 A 980 |
Chain | Residue |
A | LEU74 |
A | PHE108 |
A | TRP109 |
A | THR154 |
A | GLY155 |
A | LEU156 |
A | GLY157 |
A | ASN158 |
A | GLY192 |
A | ASP195 |
A | THR196 |
A | CDL800 |
site_id | AC8 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE PC1 A 981 |
Chain | Residue |
A | LYS106 |
A | GLN107 |
A | PHE108 |
A | TRP109 |
A | ARG110 |
A | ALA113 |
A | PC1982 |
A | PC1982 |
site_id | AC9 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE PC1 A 982 |
Chain | Residue |
A | PHE66 |
A | LEU67 |
A | ARG110 |
A | ALA113 |
A | PC1981 |
A | PC1981 |
A | HOH2082 |
site_id | BC1 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE PC1 A 983 |
Chain | Residue |
A | CDL801 |
A | HOH2083 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 25 |
Details | TOPO_DOM: Mitochondrial intermembrane => ECO:0000305 |
Chain | Residue | Details |
A | SER1-PHE7 | |
A | GLY100-TRP109 | |
A | MET200-ILE210 |
site_id | SWS_FT_FI2 |
Number of Residues | 29 |
Details | TRANSMEM: Helical; Name=1 => ECO:0000269|PubMed:14603310, ECO:0000269|PubMed:16226253 |
Chain | Residue | Details |
A | LEU8-VAL37 |
site_id | SWS_FT_FI3 |
Number of Residues | 124 |
Details | TOPO_DOM: Mitochondrial matrix => ECO:0000305 |
Chain | Residue | Details |
A | GLN38-LEU74 | |
A | TYR131-VAL178 | |
A | THR232-ALA273 |
site_id | SWS_FT_FI4 |
Number of Residues | 24 |
Details | TRANSMEM: Helical; Name=2 => ECO:0000269|PubMed:14603310, ECO:0000269|PubMed:16226253 |
Chain | Residue | Details |
A | ALA75-LEU99 |
site_id | SWS_FT_FI5 |
Number of Residues | 20 |
Details | TRANSMEM: Helical; Name=3 => ECO:0000269|PubMed:14603310, ECO:0000269|PubMed:16226253 |
Chain | Residue | Details |
A | ARG110-VAL130 |
site_id | SWS_FT_FI6 |
Number of Residues | 20 |
Details | TRANSMEM: Helical; Name=4 => ECO:0000269|PubMed:14603310, ECO:0000269|PubMed:16226253 |
Chain | Residue | Details |
A | SER179-GLY199 |
site_id | SWS_FT_FI7 |
Number of Residues | 20 |
Details | TRANSMEM: Helical; Name=5 => ECO:0000269|PubMed:14603310, ECO:0000269|PubMed:16226253 |
Chain | Residue | Details |
A | VAL211-ASP231 |
site_id | SWS_FT_FI8 |
Number of Residues | 17 |
Details | TRANSMEM: Helical; Name=6 => ECO:0000269|PubMed:14603310, ECO:0000269|PubMed:16226253 |
Chain | Residue | Details |
A | TRP274-ASP291 |
site_id | SWS_FT_FI9 |
Number of Residues | 3 |
Details | BINDING: BINDING => ECO:0000305|PubMed:14603310 |
Chain | Residue | Details |
A | TYR80 | |
A | ASP92 | |
A | ARG235 |
site_id | SWS_FT_FI10 |
Number of Residues | 1 |
Details | MOD_RES: N-acetylserine => ECO:0000269|PubMed:7076130 |
Chain | Residue | Details |
A | ASP2 |
site_id | SWS_FT_FI11 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q05962 |
Chain | Residue | Details |
A | PHE7 |
site_id | SWS_FT_FI12 |
Number of Residues | 1 |
Details | MOD_RES: N6-methyllysine => ECO:0000255 |
Chain | Residue | Details |
A | GLY52 |
site_id | SWS_FT_FI13 |
Number of Residues | 3 |
Details | MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P48962 |
Chain | Residue | Details |
A | GLY147 | |
A | GLY245 | |
A | GLY272 |
site_id | SWS_FT_FI14 |
Number of Residues | 1 |
Details | MOD_RES: S-nitrosocysteine => ECO:0000250|UniProtKB:Q05962 |
Chain | Residue | Details |
A | ILE160 |