Research workbench
Minimal human cftr first nucleotide binding domain as a head-to-tail dimer with delta F508
Analyse Minimal human cftr first nucleotide binding domain as a head-to-tail dimer with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2PZF
- Type
- protein
- Length
- 440 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cystic fibrosis transmembrane conductance regulator
- EC
- 3.6.3.49
- UniProt
- P13569
- Ligands
- ATP, MG
- Pockets
- 2 · best druggability 0.78
Structure
x-ray diffraction · 2 distinct chains · 34% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cystic fibrosis transmembrane conductance regulator (EC 3.6.3.49) | protein | 224 | 34% helix, 27% strand | P13569 |
| B | Cystic fibrosis transmembrane conductance regulator (EC 3.6.3.49) | protein | 216 | 33% helix, 27% strand | P13569 |
Ligands and binding sites
- ATP · Adenosine-5'-triphosphate · ligand · 2 copies · chains A, B
- MG · Magnesium ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1171 | 0.78 | 0.80 | 126 | MG, ATP |
| 2 | 84 | 0.73 | 0.96 | 23 | empty |
Interfaces
1 interface between chains.
- A–B · 1017 Ų buried · 4 hydrogen bonds · protein-protein
Compared structures
- 2PZF · Minimal human CFTR first nucleotide binding domain as a head-to-tail dimer with delta F508 · the same entry in another collection · chain A against A, TM-score 1.00
- P13569 · AlphaFold monomer V2.0 prediction for cystic fibrosis transmembrane conductance regulator… · a predicted model of the same protein · chain B against A, TM-score 0.97
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P13569
- Elsewhere: RCSB PDB 2PZF · PDBe 2PZF · UniProt P13569
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