Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005524 | molecular_function | ATP binding |
A | 0016020 | cellular_component | membrane |
A | 0016887 | molecular_function | ATP hydrolysis activity |
A | 0055085 | biological_process | transmembrane transport |
A | 0140359 | molecular_function | ABC-type transporter activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE MG A 801 |
Chain | Residue |
A | SER534 |
A | GLN575 |
A | ASP658 |
A | ACP900 |
site_id | AC2 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE ACP A 900 |
Chain | Residue |
A | GLY530 |
A | SER531 |
A | GLY532 |
A | LYS533 |
A | SER534 |
A | THR535 |
A | TYR544 |
A | GLN575 |
A | MG801 |
A | HOH2055 |
A | ASP264 |
A | TYR501 |
A | ALA503 |
A | ILE509 |
A | SER529 |
site_id | AC3 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE GLY A 1717 |
Chain | Residue |
A | ARG170 |
A | TYR234 |
A | ARG242 |
site_id | AC4 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE LMT A 1720 |
Chain | Residue |
A | ASP197 |
A | TYR200 |
A | THR201 |
A | PRO203 |
A | LEU214 |
A | GLY418 |
A | MET421 |
A | THR427 |
A | VAL428 |
A | ASN484 |
A | LYS486 |
A | HOH2033 |
site_id | AC5 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE CDL A 1721 |
Chain | Residue |
A | PRO312 |
A | ASN313 |
A | ASN313 |
A | THR316 |
A | THR316 |
A | PHE317 |
A | PHE317 |
A | SER405 |
A | SER405 |
A | LYS416 |
A | LYS416 |
A | LMT1724 |
A | LMT1724 |
site_id | AC6 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE LMT A 1723 |
site_id | AC7 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE LMT A 1724 |
Chain | Residue |
A | SER405 |
A | SER412 |
A | TYR415 |
A | LYS416 |
A | LEU420 |
A | SER423 |
A | HIS425 |
A | CDL1721 |
A | CDL1721 |
A | HOH2032 |
site_id | AC8 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CDL A 1727 |
Chain | Residue |
A | PHE191 |
A | LEU214 |
A | PHE222 |
A | ASN407 |
Functional Information from PROSITE/UniProt
site_id | PS00211 |
Number of Residues | 15 |
Details | ABC_TRANSPORTER_1 ABC transporters family signature. LSGGQKQRIAIARAL |
Chain | Residue | Details |
A | LEU634-LEU648 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | LEU171-PHE191 | |
A | LEU216-MET236 | |
A | ASN313-GLY333 | |
A | LEU408-VAL428 | |
A | LEU431-PHE451 | |
site_id | SWS_FT_FI2 |
Number of Residues | 382 |
Details | TOPO_DOM: Mitochondrial matrix => ECO:0000255 |
Chain | Residue | Details |
A | LEU192-CYS215 | |
A | ARG334-ASN407 | |
A | TYR452-ALA738 | |
site_id | SWS_FT_FI3 |
Number of Residues | 76 |
Details | TOPO_DOM: Mitochondrial intermembrane => ECO:0000255 |
Chain | Residue | Details |
A | GLN237-PRO312 | |
A | GLY429-GLU430 | |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | BINDING: |
Chain | Residue | Details |
A | GLY527 | |
Chain | Residue | Details |
A | LYS265 | |
Chain | Residue | Details |
A | CYS582 | |