6GKD
human NBD1 of CFTR in complex with nanobodies D12 and G3a
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005524 | molecular_function | ATP binding |
| A | 0016887 | molecular_function | ATP hydrolysis activity |
| F | 0005524 | molecular_function | ATP binding |
| F | 0016887 | molecular_function | ATP hydrolysis activity |
| I | 0005524 | molecular_function | ATP binding |
| I | 0016887 | molecular_function | ATP hydrolysis activity |
| L | 0005524 | molecular_function | ATP binding |
| L | 0016887 | molecular_function | ATP hydrolysis activity |
| O | 0005524 | molecular_function | ATP binding |
| O | 0016887 | molecular_function | ATP hydrolysis activity |
| R | 0005524 | molecular_function | ATP binding |
| R | 0016887 | molecular_function | ATP hydrolysis activity |
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 | 6 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:15528182, ECO:0000269|PubMed:20150177, ECO:0007744|PDB:1XMI, ECO:0007744|PDB:1XMJ, ECO:0007744|PDB:2BBO, ECO:0007744|PDB:2BBS, ECO:0007744|PDB:2BBT, ECO:0007744|PDB:2PZE, ECO:0007744|PDB:2PZF, ECO:0007744|PDB:2PZG |
| Chain | Residue | Details |
| A | TRP401 | |
| F | TRP401 | |
| I | TRP401 | |
| L | TRP401 | |
| O | TRP401 | |
| R | TRP401 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:20150177, ECO:0007744|PDB:2PZE, ECO:0007744|PDB:2PZF, ECO:0007744|PDB:2PZG |
| Chain | Residue | Details |
| A | SER466 | |
| F | SER466 | |
| I | SER466 | |
| L | SER466 | |
| O | SER466 | |
| R | SER466 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00434, ECO:0000269|PubMed:15528182, ECO:0007744|PDB:1XMI, ECO:0007744|PDB:1XMJ, ECO:0007744|PDB:2BBO, ECO:0007744|PDB:2BBS, ECO:0007744|PDB:2BBT |
| Chain | Residue | Details |
| A | PHE490 | |
| F | PHE490 | |
| I | PHE490 | |
| L | PHE490 | |
| O | PHE490 | |
| R | PHE490 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:15528182, ECO:0007744|PDB:1XMI, ECO:0007744|PDB:2BBO, ECO:0007744|PDB:2BBS |
| Chain | Residue | Details |
| A | GLN525 | |
| F | GLN525 | |
| I | GLN525 | |
| L | GLN525 | |
| O | GLN525 | |
| R | GLN525 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 6 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:20068231 |
| Chain | Residue | Details |
| A | LEU581 | |
| F | LEU581 | |
| I | LEU581 | |
| L | LEU581 | |
| O | LEU581 | |
| R | LEU581 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 6 |
| Details | LIPID: S-palmitoyl cysteine => ECO:0000269|PubMed:22119790 |
| Chain | Residue | Details |
| A | ILE556 | |
| F | ILE556 | |
| I | ILE556 | |
| L | ILE556 | |
| O | ILE556 | |
| R | ILE556 |
