4MYH
Structure of the Glutathione bound mitochondrial ABC transporter, Atm1
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 | 
| B | 0005524 | molecular_function | ATP binding | 
| B | 0016020 | cellular_component | membrane | 
| B | 0016887 | molecular_function | ATP hydrolysis activity | 
| B | 0055085 | biological_process | transmembrane transport | 
| B | 0140359 | molecular_function | ABC-type transporter activity | 
| C | 0005524 | molecular_function | ATP binding | 
| C | 0016020 | cellular_component | membrane | 
| C | 0016887 | molecular_function | ATP hydrolysis activity | 
| C | 0055085 | biological_process | transmembrane transport | 
| C | 0140359 | molecular_function | ABC-type transporter activity | 
Functional Information from PDB Data
| site_id | AC1 | 
| Number of Residues | 5 | 
| Details | BINDING SITE FOR RESIDUE GSH B 701 | 
| Chain | Residue | 
| B | ARG280 | 
| B | ARG284 | 
| B | ASN343 | 
| B | ASN390 | 
| B | SER394 | 
Functional Information from PROSITE/UniProt
| site_id | PS00211 | 
| Number of Residues | 15 | 
| Details | ABC_TRANSPORTER_1 ABC transporters family signature. ISGGEKQRLAIARVL | 
| Chain | Residue | Details | 
| A | ILE573-LEU587 | 
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 | 
| Number of Residues | 378 | 
| Details | Transmembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]} | 
| Chain | Residue | Details | 
| site_id | SWS_FT_FI2 | 
| Number of Residues | 111 | 
| Details | Topological domain: {"description":"Mitochondrial intermembrane","evidences":[{"source":"PubMed","id":"24604199","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25006243","evidenceCode":"ECO:0000269"}]} | 
| Chain | Residue | Details | 
| site_id | SWS_FT_FI3 | 
| Number of Residues | 1218 | 
| Details | Topological domain: {"description":"Mitochondrial matrix","evidences":[{"source":"PubMed","id":"24604199","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25006243","evidenceCode":"ECO:0000269"}]} | 
| Chain | Residue | Details | 
| site_id | SWS_FT_FI4 | 
| Number of Residues | 870 | 
| Details | Domain: {"description":"ABC transmembrane type-1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00441","evidenceCode":"ECO:0000255"}]} | 
| Chain | Residue | Details | 
| site_id | SWS_FT_FI5 | 
| Number of Residues | 708 | 
| Details | Domain: {"description":"ABC transporter","evidences":[{"source":"PROSITE-ProRule","id":"PRU00434","evidenceCode":"ECO:0000255"}]} | 
| Chain | Residue | Details | 
| site_id | SWS_FT_FI6 | 
| Number of Residues | 21 | 
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"24604199","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4MYH","evidenceCode":"ECO:0007744"}]} | 
| Chain | Residue | Details | 
| site_id | SWS_FT_FI7 | 
| Number of Residues | 3 | 
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"Q2G506","evidenceCode":"ECO:0000250"}]} | 
| Chain | Residue | Details | 
| site_id | SWS_FT_FI8 | 
| Number of Residues | 3 | 
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"Q9NP58","evidenceCode":"ECO:0000250"}]} | 
| Chain | Residue | Details | 
| site_id | SWS_FT_FI9 | 
| Number of Residues | 33 | 
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00434","evidenceCode":"ECO:0000255"}]} | 
| Chain | Residue | Details | 






