6PAR
Structure of a bacterial Atm1-family ABC exporter with MgAMPPNP bound
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 |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0005524 | molecular_function | ATP binding |
| C | 0005886 | cellular_component | plasma membrane |
| C | 0006811 | biological_process | monoatomic ion transport |
| C | 0016020 | cellular_component | membrane |
| C | 0016887 | molecular_function | ATP hydrolysis activity |
| C | 0042626 | molecular_function | ATPase-coupled transmembrane transporter activity |
| C | 0046689 | biological_process | response to mercury ion |
| C | 0055085 | biological_process | transmembrane transport |
| C | 0140359 | molecular_function | ABC-type transporter activity |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0005524 | molecular_function | ATP binding |
| D | 0005886 | cellular_component | plasma membrane |
| D | 0006811 | biological_process | monoatomic ion transport |
| D | 0016020 | cellular_component | membrane |
| D | 0016887 | molecular_function | ATP hydrolysis activity |
| D | 0042626 | molecular_function | ATPase-coupled transmembrane transporter activity |
| D | 0046689 | biological_process | response to mercury ion |
| D | 0055085 | biological_process | transmembrane transport |
| D | 0140359 | molecular_function | ABC-type transporter activity |
| E | 0000166 | molecular_function | nucleotide binding |
| E | 0005524 | molecular_function | ATP binding |
| E | 0005886 | cellular_component | plasma membrane |
| E | 0006811 | biological_process | monoatomic ion transport |
| E | 0016020 | cellular_component | membrane |
| E | 0016887 | molecular_function | ATP hydrolysis activity |
| E | 0042626 | molecular_function | ATPase-coupled transmembrane transporter activity |
| E | 0046689 | biological_process | response to mercury ion |
| E | 0055085 | biological_process | transmembrane transport |
| E | 0140359 | molecular_function | ABC-type transporter activity |
| F | 0000166 | molecular_function | nucleotide binding |
| F | 0005524 | molecular_function | ATP binding |
| F | 0005886 | cellular_component | plasma membrane |
| F | 0006811 | biological_process | monoatomic ion transport |
| F | 0016020 | cellular_component | membrane |
| F | 0016887 | molecular_function | ATP hydrolysis activity |
| F | 0042626 | molecular_function | ATPase-coupled transmembrane transporter activity |
| F | 0046689 | biological_process | response to mercury ion |
| F | 0055085 | biological_process | transmembrane transport |
| F | 0140359 | molecular_function | ABC-type transporter activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 20 |
| Details | binding site for residue ANP A 701 |
| Chain | Residue |
| A | TYR370 |
| A | SER401 |
| A | THR402 |
| A | GLN442 |
| A | HIS554 |
| A | MG702 |
| B | PHE479 |
| B | LYS497 |
| B | SER499 |
| B | GLY500 |
| B | GLY501 |
| A | ARG374 |
| B | GLU502 |
| A | ILE376 |
| A | PRO395 |
| A | SER396 |
| A | GLY397 |
| A | ALA398 |
| A | GLY399 |
| A | LYS400 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | binding site for residue MG A 702 |
| Chain | Residue |
| A | SER401 |
| A | GLN442 |
| A | ANP701 |
| site_id | AC3 |
| Number of Residues | 21 |
| Details | binding site for residue ANP B 701 |
| Chain | Residue |
| A | PHE479 |
| A | LYS497 |
| A | SER499 |
| A | GLY500 |
| A | GLY501 |
| A | GLU502 |
| A | ALA527 |
| B | TYR370 |
| B | ARG374 |
| B | ILE376 |
| B | SER396 |
| B | GLY397 |
| B | ALA398 |
| B | GLY399 |
| B | LYS400 |
| B | SER401 |
| B | THR402 |
| B | TYR411 |
| B | GLN442 |
| B | HIS554 |
| B | MG702 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | binding site for residue MG B 702 |
| Chain | Residue |
| B | SER401 |
| B | GLN442 |
| B | ANP701 |
| site_id | AC5 |
| Number of Residues | 18 |
| Details | binding site for residue ANP C 701 |
| Chain | Residue |
| C | TYR370 |
| C | ARG374 |
| C | PRO395 |
| C | SER396 |
| C | GLY397 |
| C | ALA398 |
| C | GLY399 |
| C | LYS400 |
| C | SER401 |
| C | THR402 |
| C | GLN442 |
| C | MG702 |
| D | LYS497 |
| D | SER499 |
| D | GLY500 |
| D | GLY501 |
| D | GLU502 |
| D | ALA527 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | binding site for residue MG C 702 |
| Chain | Residue |
| C | SER401 |
| C | GLN442 |
| C | ASP522 |
| C | ANP701 |
| site_id | AC7 |
| Number of Residues | 18 |
| Details | binding site for residue ANP D 701 |
| Chain | Residue |
| C | LYS497 |
| C | SER499 |
| C | GLY500 |
| C | GLU502 |
| C | ALA527 |
| D | TYR370 |
| D | ARG374 |
| D | ILE376 |
| D | SER396 |
| D | GLY397 |
| D | ALA398 |
| D | GLY399 |
| D | LYS400 |
| D | SER401 |
| D | THR402 |
| D | GLN442 |
| D | HIS554 |
| D | MG702 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | binding site for residue MG D 702 |
| Chain | Residue |
| D | SER401 |
| D | GLN442 |
| D | ANP701 |
| site_id | AC9 |
| Number of Residues | 19 |
| Details | binding site for residue ANP E 701 |
| Chain | Residue |
| E | THR402 |
| E | GLN442 |
| E | HIS554 |
| E | MG702 |
| F | PHE479 |
| F | LYS497 |
| F | SER499 |
| F | GLY500 |
| F | GLY501 |
| F | GLU502 |
| E | TYR370 |
| E | ARG374 |
| E | PRO395 |
| E | SER396 |
| E | GLY397 |
| E | ALA398 |
| E | GLY399 |
| E | LYS400 |
| E | SER401 |
| site_id | AD1 |
| Number of Residues | 3 |
| Details | binding site for residue MG E 702 |
| Chain | Residue |
| E | SER401 |
| E | GLN442 |
| E | ANP701 |
| site_id | AD2 |
| Number of Residues | 20 |
| Details | binding site for residue ANP F 701 |
| Chain | Residue |
| E | PHE479 |
| E | LYS497 |
| E | SER499 |
| E | GLY500 |
| E | GLY501 |
| E | GLU502 |
| E | ALA527 |
| F | TYR370 |
| F | ARG374 |
| F | PRO395 |
| F | SER396 |
| F | GLY397 |
| F | ALA398 |
| F | GLY399 |
| F | LYS400 |
| F | SER401 |
| F | THR402 |
| F | GLN442 |
| F | HIS554 |
| F | MG702 |
| site_id | AD3 |
| Number of Residues | 3 |
| Details | binding site for residue MG F 702 |
| Chain | Residue |
| F | SER401 |
| F | GLN442 |
| F | ANP701 |
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 | 2598 |
| Details | TOPO_DOM: Cytoplasmic => ECO:0000269|PubMed:24604198 |
| Chain | Residue | Details |
| A | MET1-ARG38 | |
| C | GLU106-MET154 | |
| C | THR203-GLY266 | |
| C | ARG323-GLU608 | |
| D | MET1-ARG38 | |
| D | GLU106-MET154 | |
| D | THR203-GLY266 | |
| D | ARG323-GLU608 | |
| E | MET1-ARG38 | |
| E | GLU106-MET154 | |
| E | THR203-GLY266 | |
| A | GLU106-MET154 | |
| E | ARG323-GLU608 | |
| F | MET1-ARG38 | |
| F | GLU106-MET154 | |
| F | THR203-GLY266 | |
| F | ARG323-GLU608 | |
| A | THR203-GLY266 | |
| A | ARG323-GLU608 | |
| B | MET1-ARG38 | |
| B | GLU106-MET154 | |
| B | THR203-GLY266 | |
| B | ARG323-GLU608 | |
| C | MET1-ARG38 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 762 |
| Details | TRANSMEM: Helical |
| Chain | Residue | Details |
| A | VAL39-TYR60 | |
| B | PHE180-ILE202 | |
| B | LEU267-ALA285 | |
| B | LEU301-TYR322 | |
| C | VAL39-TYR60 | |
| C | PHE83-PHE105 | |
| C | LEU155-LEU178 | |
| C | PHE180-ILE202 | |
| C | LEU267-ALA285 | |
| C | LEU301-TYR322 | |
| D | VAL39-TYR60 | |
| A | PHE83-PHE105 | |
| D | PHE83-PHE105 | |
| D | LEU155-LEU178 | |
| D | PHE180-ILE202 | |
| D | LEU267-ALA285 | |
| D | LEU301-TYR322 | |
| E | VAL39-TYR60 | |
| E | PHE83-PHE105 | |
| E | LEU155-LEU178 | |
| E | PHE180-ILE202 | |
| E | LEU267-ALA285 | |
| A | LEU155-LEU178 | |
| E | LEU301-TYR322 | |
| F | VAL39-TYR60 | |
| F | PHE83-PHE105 | |
| F | LEU155-LEU178 | |
| F | PHE180-ILE202 | |
| F | LEU267-ALA285 | |
| F | LEU301-TYR322 | |
| A | PHE180-ILE202 | |
| A | LEU267-ALA285 | |
| A | LEU301-TYR322 | |
| B | VAL39-TYR60 | |
| B | PHE83-PHE105 | |
| B | LEU155-LEU178 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 216 |
| Details | TOPO_DOM: Periplasmic => ECO:0000269|PubMed:24604198 |
| Chain | Residue | Details |
| A | LYS61-ALA82 | |
| D | LYS61-ALA82 | |
| D | ASN179 | |
| D | TRP286-ASP300 | |
| E | LYS61-ALA82 | |
| E | ASN179 | |
| E | TRP286-ASP300 | |
| F | LYS61-ALA82 | |
| F | ASN179 | |
| F | TRP286-ASP300 | |
| A | ASN179 | |
| A | TRP286-ASP300 | |
| B | LYS61-ALA82 | |
| B | ASN179 | |
| B | TRP286-ASP300 | |
| C | LYS61-ALA82 | |
| C | ASN179 | |
| C | TRP286-ASP300 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:P40416 |
| Chain | Residue | Details |
| A | ARG206 | |
| B | ARG206 | |
| C | ARG206 | |
| D | ARG206 | |
| E | ARG206 | |
| F | ARG206 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:24604198, ECO:0007744|PDB:4MRP |
| Chain | Residue | Details |
| A | ASN269 | |
| E | ASP316 | |
| F | ASN269 | |
| F | ASP316 | |
| A | ASP316 | |
| B | ASN269 | |
| B | ASP316 | |
| C | ASN269 | |
| C | ASP316 | |
| D | ASN269 | |
| D | ASP316 | |
| E | ASN269 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:Q9NP58 |
| Chain | Residue | Details |
| A | TYR370 | |
| B | TYR370 | |
| C | TYR370 | |
| D | TYR370 | |
| E | TYR370 | |
| F | TYR370 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00434 |
| Chain | Residue | Details |
| A | GLY394 | |
| B | GLY394 | |
| C | GLY394 | |
| D | GLY394 | |
| E | GLY394 | |
| F | GLY394 |
