23PG
Cryo-EM structure of human ABCB7 in complex with CoPP:GSH/ADPVO4
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005515 | molecular_function | protein binding |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0005743 | cellular_component | mitochondrial inner membrane |
| A | 0006783 | biological_process | heme biosynthetic process |
| A | 0006879 | biological_process | intracellular iron ion homeostasis |
| A | 0015232 | molecular_function | heme transmembrane transporter activity |
| A | 0015886 | biological_process | heme transport |
| A | 0016226 | biological_process | iron-sulfur cluster assembly |
| A | 0031966 | cellular_component | mitochondrial membrane |
| A | 0034755 | biological_process | iron ion transmembrane transport |
| A | 0042626 | molecular_function | ATPase-coupled transmembrane transporter activity |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0043190 | cellular_component | ATP-binding cassette (ABC) transporter complex |
| A | 0055085 | biological_process | transmembrane transport |
| A | 0070455 | biological_process | positive regulation of heme biosynthetic process |
| A | 0140466 | biological_process | iron-sulfur cluster export from the mitochondrion |
| A | 0140481 | molecular_function | ABC-type iron-sulfur cluster transporter activity |
| A | 1903331 | biological_process | positive regulation of iron-sulfur cluster assembly |
| A | 1903427 | biological_process | negative regulation of reactive oxygen species biosynthetic process |
| B | 0005515 | molecular_function | protein binding |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005739 | cellular_component | mitochondrion |
| B | 0005743 | cellular_component | mitochondrial inner membrane |
| B | 0006783 | biological_process | heme biosynthetic process |
| B | 0006879 | biological_process | intracellular iron ion homeostasis |
| B | 0015232 | molecular_function | heme transmembrane transporter activity |
| B | 0015886 | biological_process | heme transport |
| B | 0016226 | biological_process | iron-sulfur cluster assembly |
| B | 0031966 | cellular_component | mitochondrial membrane |
| B | 0034755 | biological_process | iron ion transmembrane transport |
| B | 0042626 | molecular_function | ATPase-coupled transmembrane transporter activity |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0042803 | molecular_function | protein homodimerization activity |
| B | 0043190 | cellular_component | ATP-binding cassette (ABC) transporter complex |
| B | 0055085 | biological_process | transmembrane transport |
| B | 0070455 | biological_process | positive regulation of heme biosynthetic process |
| B | 0140466 | biological_process | iron-sulfur cluster export from the mitochondrion |
| B | 0140481 | molecular_function | ABC-type iron-sulfur cluster transporter activity |
| B | 1903331 | biological_process | positive regulation of iron-sulfur cluster assembly |
| B | 1903427 | biological_process | negative regulation of reactive oxygen species biosynthetic process |
Functional Information from PROSITE/UniProt
| site_id | PS00211 |
| Number of Residues | 15 |
| Details | ABC_TRANSPORTER_1 ABC transporters family signature. LSGGEKQRVAIARAI |
| Chain | Residue | Details |
| A | LEU609-ILE623 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 240 |
| Details | Transmembrane: {"description":"Helical","evidences":[{"source":"PROSITE-ProRule","id":"PRU00441","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 244 |
| Details | Topological domain: {"description":"Mitochondrial matrix","evidences":[{"source":"UniProtKB","id":"P40416","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 28 |
| Details | Topological domain: {"description":"Mitochondrial intermembrane","evidences":[{"source":"UniProtKB","id":"P40416","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 14 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P40416","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"Q2G506","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"Q9NP58","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 22 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00434","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q704E8","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"Q704E8","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"Q704E8","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
