Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0006811 | biological_process | monoatomic ion transport |
| A | 0016020 | cellular_component | membrane |
| A | 0016887 | molecular_function | ATP hydrolysis activity |
| A | 0042626 | molecular_function | ATPase-coupled transmembrane transporter activity |
| A | 0046689 | biological_process | response to mercury ion |
| A | 0055085 | biological_process | transmembrane transport |
| A | 0140359 | molecular_function | ABC-type transporter activity |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005886 | cellular_component | plasma membrane |
| B | 0006811 | biological_process | monoatomic ion transport |
| B | 0016020 | cellular_component | membrane |
| B | 0016887 | molecular_function | ATP hydrolysis activity |
| B | 0042626 | molecular_function | ATPase-coupled transmembrane transporter activity |
| B | 0046689 | biological_process | response to mercury ion |
| B | 0055085 | biological_process | transmembrane transport |
| B | 0140359 | molecular_function | ABC-type transporter activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE LDA A 701 |
| Chain | Residue |
| A | ALA117 |
| A | ARG146 |
| A | GLY147 |
| A | THR148 |
| A | ILE330 |
| A | ASP331 |
| A | MSE335 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE LDA A 702 |
| Chain | Residue |
| B | ILE144 |
| B | THR148 |
| B | LDA702 |
| A | ASP217 |
| A | TYR247 |
| site_id | AC3 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE GDS A 703 |
| Chain | Residue |
| A | LYS149 |
| A | ARG206 |
| A | ARG210 |
| A | LEU265 |
| A | ARG323 |
| B | LYS149 |
| B | ARG206 |
| B | MSE320 |
| B | ARG323 |
| B | GDS703 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PO4 A 704 |
| Chain | Residue |
| A | ARG114 |
| A | HIS115 |
| A | HOH907 |
| B | ARG252 |
| site_id | AC5 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE PO4 A 705 |
| Chain | Residue |
| A | PRO395 |
| A | SER396 |
| A | GLY397 |
| A | ALA398 |
| A | GLY399 |
| A | LYS400 |
| A | SER401 |
| A | HOH897 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE LDA A 706 |
| Chain | Residue |
| A | ALA51 |
| A | LYS61 |
| A | ASN179 |
| A | ASP300 |
| A | PHE303 |
| site_id | AC7 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE LDA A 708 |
| site_id | AC8 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE LDA A 709 |
| site_id | AC9 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE LDA A 710 |
| site_id | BC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE LDA B 701 |
| Chain | Residue |
| A | THR148 |
| B | ASP217 |
| B | TYR247 |
| B | TYR254 |
| site_id | BC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE LDA B 702 |
| Chain | Residue |
| A | LDA702 |
| B | THR113 |
| B | ARG146 |
| B | GLY147 |
| B | THR148 |
| B | ASP331 |
| B | GLU334 |
| B | MSE335 |
| site_id | BC3 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE GDS B 703 |
| Chain | Residue |
| A | TYR156 |
| A | LEU265 |
| A | LEU268 |
| A | ASN269 |
| A | GLN272 |
| A | ASP316 |
| A | MSE317 |
| A | LEU318 |
| A | GLY319 |
| A | MSE320 |
| A | GDS703 |
| B | TYR156 |
| B | LEU268 |
| B | ASN269 |
| B | GLN272 |
| B | ASP316 |
| B | MSE317 |
| B | LEU318 |
| B | GLY319 |
| B | MSE320 |
| site_id | BC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PO4 B 704 |
| Chain | Residue |
| B | SER396 |
| B | GLY399 |
| B | LYS400 |
| B | SER401 |
| B | HOH956 |
| B | HOH961 |
| site_id | BC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PO4 B 705 |
| Chain | Residue |
| A | ARG252 |
| B | ARG114 |
| B | HIS115 |
| B | HOH900 |
| B | HOH925 |
| site_id | BC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE LDA B 706 |
| Chain | Residue |
| B | PHE58 |
| B | ASN179 |
| B | PHE303 |
| site_id | BC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE LDA B 708 |
| Chain | Residue |
| B | ARG13 |
| B | ASP15 |
| B | GLY16 |
| B | LDA709 |
| site_id | BC8 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE LDA B 709 |
| Chain | Residue |
| B | TYR322 |
| B | LDA708 |
Functional Information from PROSITE/UniProt
| site_id | PS00211 |
| Number of Residues | 15 |
| Details | ABC_TRANSPORTER_1 ABC transporters family signature. LSGGEKQRVAIARTL |
| Chain | Residue | Details |
| A | LEU498-LEU512 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 134 |
| Details | Transmembrane: {"description":"Helical"} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 96 |
| Details | Topological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"24604198","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 30 |
| Details | Topological domain: {"description":"Periplasmic","evidences":[{"source":"PubMed","id":"24604198","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI4 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P40416","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI5 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"24604198","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4MRP","evidenceCode":"ECO:0007744"}]} |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"Q9NP58","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI7 |
| Number of Residues | 22 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00434","evidenceCode":"ECO:0000255"}]} |
