4C9J
Structure of yeast mitochondrial ADP/ATP carrier isoform 3 inhibited by carboxyatractyloside (P212121 crystal form)
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 | 0009061 | biological_process | anaerobic respiration |
A | 0015297 | molecular_function | antiporter activity |
A | 0015886 | biological_process | heme transport |
A | 0042802 | molecular_function | identical protein binding |
A | 0055085 | biological_process | transmembrane transport |
A | 0140021 | biological_process | mitochondrial ADP transmembrane transport |
A | 1990544 | biological_process | mitochondrial ATP transmembrane transport |
B | 0005471 | molecular_function | ATP:ADP antiporter activity |
B | 0005739 | cellular_component | mitochondrion |
B | 0005743 | cellular_component | mitochondrial inner membrane |
B | 0009061 | biological_process | anaerobic respiration |
B | 0015297 | molecular_function | antiporter activity |
B | 0015886 | biological_process | heme transport |
B | 0042802 | molecular_function | identical protein binding |
B | 0055085 | biological_process | transmembrane transport |
B | 0140021 | biological_process | mitochondrial ADP transmembrane transport |
B | 1990544 | biological_process | mitochondrial ATP transmembrane transport |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE CXT A 401 |
Chain | Residue |
A | ARG85 |
A | ASN93 |
A | LYS97 |
A | GLY188 |
A | ARG193 |
A | SER234 |
A | ASP238 |
A | ARG241 |
site_id | AC2 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE CDL A 800 |
Chain | Residue |
A | ARG77 |
A | GLY78 |
A | ASN79 |
A | THR80 |
A | LEU162 |
A | THR163 |
A | CDL801 |
B | LEU72 |
B | ILE73 |
B | CDL800 |
A | TRP76 |
site_id | AC3 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE CDL A 801 |
Chain | Residue |
A | ILE40 |
A | GLY58 |
A | ILE59 |
A | VAL60 |
A | LYS167 |
A | LEU170 |
A | PHE274 |
A | GLY276 |
A | GLY278 |
A | ILE281 |
A | LEU282 |
A | CDL800 |
site_id | AC4 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE CDL A 802 |
Chain | Residue |
A | ILE175 |
A | ALA176 |
A | TYR179 |
A | GLY181 |
A | PHE182 |
A | MET183 |
A | VAL187 |
A | LEU237 |
A | MET244 |
A | GLY256 |
A | ALA257 |
A | ILE258 |
B | PHE116 |
site_id | AC5 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE CXT B 401 |
Chain | Residue |
B | ARG85 |
B | ASN93 |
B | LYS97 |
B | SER130 |
B | GLY188 |
B | ARG193 |
B | SER234 |
B | ASP238 |
B | ARG241 |
site_id | AC6 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE CDL B 800 |
Chain | Residue |
A | LEU72 |
A | CDL800 |
B | TRP76 |
B | ARG77 |
B | GLY78 |
B | ASN79 |
B | THR80 |
B | GLY161 |
B | LEU162 |
B | THR163 |
site_id | AC7 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE CDL B 801 |
Chain | Residue |
B | SER57 |
B | GLY58 |
B | ILE59 |
B | VAL60 |
B | LYS167 |
B | PHE274 |
B | GLY276 |
B | CYS277 |
B | GLY278 |
B | ALA279 |
B | ILE281 |
site_id | AC8 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE CDL B 802 |
Chain | Residue |
B | LEU132 |
B | ILE175 |
B | ALA176 |
B | TYR179 |
B | GLY181 |
B | PHE182 |
B | MET183 |
B | PRO184 |
B | LEU237 |
B | GLY256 |
B | ALA257 |
B | ILE258 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 54 |
Details | TRANSMEM: Helical; Name=1 => ECO:0000269|PubMed:24474793 |
Chain | Residue | Details |
A | PHE12-LEU39 | |
B | PHE12-LEU39 |
site_id | SWS_FT_FI2 |
Number of Residues | 48 |
Details | TRANSMEM: Helical; Name=2 => ECO:0000269|PubMed:24474793 |
Chain | Residue | Details |
A | THR80-PHE104 | |
B | THR80-PHE104 |
site_id | SWS_FT_FI3 |
Number of Residues | 40 |
Details | TRANSMEM: Helical; Name=3 => ECO:0000269|PubMed:24474793 |
Chain | Residue | Details |
A | TYR112-LEU132 | |
B | TYR112-LEU132 |
site_id | SWS_FT_FI4 |
Number of Residues | 42 |
Details | TRANSMEM: Helical; Name=4 => ECO:0000269|PubMed:24474793 |
Chain | Residue | Details |
A | PHE182-LEU203 | |
B | PHE182-LEU203 |
site_id | SWS_FT_FI5 |
Number of Residues | 40 |
Details | TRANSMEM: Helical; Name=5 => ECO:0000269|PubMed:24474793 |
Chain | Residue | Details |
A | LEU217-LEU237 | |
B | LEU217-LEU237 |
site_id | SWS_FT_FI6 |
Number of Residues | 40 |
Details | TRANSMEM: Helical; Name=6 => ECO:0000250|UniProtKB:P18239 |
Chain | Residue | Details |
A | CYS277-LEU297 | |
B | CYS277-LEU297 |
site_id | SWS_FT_FI7 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000305|PubMed:24474793 |
Chain | Residue | Details |
A | ARG85 | |
A | LYS97 | |
A | ARG241 | |
B | ARG85 | |
B | LYS97 | |
B | ARG241 |