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 | 0016887 | molecular_function | ATP hydrolysis activity |
| A | 0022857 | molecular_function | transmembrane transporter activity |
| A | 0051301 | biological_process | cell division |
| A | 0055085 | biological_process | transmembrane transport |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005886 | cellular_component | plasma membrane |
| B | 0016887 | molecular_function | ATP hydrolysis activity |
| B | 0022857 | molecular_function | transmembrane transporter activity |
| B | 0051301 | biological_process | cell division |
| B | 0055085 | biological_process | transmembrane transport |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0005524 | molecular_function | ATP binding |
| C | 0005886 | cellular_component | plasma membrane |
| C | 0016887 | molecular_function | ATP hydrolysis activity |
| C | 0022857 | molecular_function | transmembrane transporter activity |
| C | 0051301 | biological_process | cell division |
| C | 0055085 | biological_process | transmembrane transport |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 21 |
| Details | binding site for residue ADP A 301 |
| Chain | Residue |
| A | TYR13 |
| A | THR45 |
| A | GLY65 |
| A | ADP302 |
| A | HOH412 |
| A | HOH422 |
| A | HOH431 |
| A | HOH486 |
| A | HOH502 |
| A | HOH535 |
| A | HOH557 |
| A | ASN15 |
| A | HOH566 |
| A | HOH568 |
| A | ALA19 |
| A | PRO38 |
| A | GLY40 |
| A | ALA41 |
| A | GLY42 |
| A | LYS43 |
| A | SER44 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | binding site for residue ADP A 302 |
| Chain | Residue |
| A | ASN15 |
| A | LEU78 |
| A | ADP301 |
| A | HOH405 |
| A | HOH431 |
| A | HOH439 |
| A | HOH567 |
| site_id | AC3 |
| Number of Residues | 23 |
| Details | binding site for residue ADP B 301 |
| Chain | Residue |
| A | GLY128 |
| A | LEU129 |
| A | HIS131 |
| A | GLU144 |
| A | ARG147 |
| A | HOH432 |
| A | HOH440 |
| B | TYR13 |
| B | GLY16 |
| B | THR17 |
| B | ALA19 |
| B | PRO38 |
| B | GLY40 |
| B | ALA41 |
| B | GLY42 |
| B | LYS43 |
| B | SER44 |
| B | THR45 |
| B | HOH411 |
| B | HOH440 |
| B | HOH443 |
| B | HOH451 |
| B | HOH475 |
| site_id | AC4 |
| Number of Residues | 18 |
| Details | binding site for residue ADP C 301 |
| Chain | Residue |
| A | LYS95 |
| A | LYS96 |
| A | HOH443 |
| C | TYR13 |
| C | ASN15 |
| C | THR17 |
| C | ALA19 |
| C | PRO38 |
| C | GLY40 |
| C | ALA41 |
| C | GLY42 |
| C | LYS43 |
| C | SER44 |
| C | THR45 |
| C | HOH432 |
| C | HOH458 |
| C | HOH462 |
| C | HOH518 |
| site_id | AC5 |
| Number of Residues | 9 |
| Details | binding site for residue ADP C 302 |
| Chain | Residue |
| A | VAL69 |
| C | TYR99 |
| C | MET121 |
| C | VAL133 |
| C | ARG134 |
| C | HOH445 |
| C | HOH503 |
| C | HOH511 |
| C | HOH544 |
Functional Information from PROSITE/UniProt
| site_id | PS00211 |
| Number of Residues | 15 |
| Details | ABC_TRANSPORTER_1 ABC transporters family signature. LSGGEQQRIAIARAI |
| Chain | Residue | Details |
| A | LEU140-ILE154 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 450 |
| Details | Domain: {"description":"ABC transporter","evidences":[{"source":"PROSITE-ProRule","id":"PRU00434","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 21 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00434","evidenceCode":"ECO:0000255"}]} |