1R0Y
Cystic fibrosis transmembrane conductance regulator (CFTR) nucleotide-binding domain one (NBD1) with ADP
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005524 | molecular_function | ATP binding |
| A | 0016887 | molecular_function | ATP hydrolysis activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0016887 | molecular_function | ATP hydrolysis activity |
| C | 0005524 | molecular_function | ATP binding |
| C | 0016887 | molecular_function | ATP hydrolysis activity |
| D | 0005524 | molecular_function | ATP binding |
| D | 0016887 | molecular_function | ATP hydrolysis activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE ADP A 7 |
| Chain | Residue |
| A | HOH125 |
| A | LYS464 |
| A | THR465 |
| A | SER466 |
| B | MET498 |
| A | TRP401 |
| A | LEU409 |
| A | GLU410 |
| A | GLN413 |
| A | PHE430 |
| A | GLY461 |
| A | SER462 |
| A | GLY463 |
| site_id | AC2 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE ADP B 8 |
| Chain | Residue |
| A | MET498 |
| B | TRP401 |
| B | GLN413 |
| B | PHE430 |
| B | GLY461 |
| B | SER462 |
| B | GLY463 |
| B | LYS464 |
| B | THR465 |
| B | SER466 |
| site_id | AC3 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE ADP C 9 |
| Chain | Residue |
| C | TRP401 |
| C | GLN413 |
| C | PHE430 |
| C | VAL440 |
| C | GLY461 |
| C | SER462 |
| C | GLY463 |
| C | LYS464 |
| C | THR465 |
| C | SER466 |
| C | MET498 |
| site_id | AC4 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE ADP D 10 |
| Chain | Residue |
| D | HOH318 |
| D | HOH321 |
| D | TRP401 |
| D | LEU409 |
| D | GLY461 |
| D | SER462 |
| D | GLY463 |
| D | LYS464 |
| D | THR465 |
| D | SER466 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ACY A 1 |
| Chain | Residue |
| A | LEU541 |
| A | GLY542 |
| A | GLY545 |
| A | VAL546 |
| A | THR547 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE ACY B 2 |
| Chain | Residue |
| A | LEU578 |
| B | HOH14 |
| B | LEU541 |
| B | GLY542 |
| B | GLY545 |
| B | VAL546 |
| B | THR547 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE ACY C 3 |
| Chain | Residue |
| C | HOH197 |
| C | LEU541 |
| C | GLY542 |
| C | GLY545 |
| C | VAL546 |
| C | THR547 |
| D | LEU578 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ACY D 4 |
| Chain | Residue |
| D | HOH308 |
| D | LEU541 |
| D | GLY542 |
| D | GLY545 |
| D | VAL546 |
| D | THR547 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ACY D 5 |
| Chain | Residue |
| C | LYS532 |
| C | SER549 |
| D | HOH281 |
| D | LYS532 |
| D | GLN552 |
| site_id | BC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ACY A 6 |
| Chain | Residue |
| A | HOH34 |
| A | SER549 |
| B | LYS532 |
| B | GLN552 |
Functional Information from PROSITE/UniProt
| site_id | PS00211 |
| Number of Residues | 15 |
| Details | ABC_TRANSPORTER_1 ABC transporters family signature. LSGGQRARISLARAV |
| Chain | Residue | Details |
| A | LEU548-VAL562 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P13569","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 28 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00434","evidenceCode":"ECO:0000255"},{"source":"PDB","id":"1Q3H","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1R0X","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1R0Z","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1R10","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1XF9","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1XFA","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3SI7","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PDB","id":"1Q3H","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1R0X","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1R0Z","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1XFA","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 8 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P13569","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"Phosphoserine; by PKA","evidences":[{"source":"UniProtKB","id":"P13569","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | Lipidation: {"description":"S-palmitoyl cysteine","evidences":[{"source":"UniProtKB","id":"P13569","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
