MolNFT v1 · #48634 · protein
Minimal human cftr first nucleotide binding domain as a head-to-tail dimer
2PZE · Cystic fibrosis transmembrane conductance regulator: “Minimal human cftr first nucleotide binding domain as a head-to-tail dimer”. X-ray diffraction, 2 ligands (ATP, MG), 1 pocket (best druggability 0.81). MolNFT v1 #48634 on…
- PDB
- 2PZE
- Type
- protein
- Length
- 445 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cystic fibrosis transmembrane conductance regulator
- UniProt
- P13569
- Ligands
- ATP, MG
- Pockets
- 1 · best druggability 0.81
Structure
x-ray diffraction · 2 distinct chains · 33% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cystic fibrosis transmembrane conductance regulator | protein | 226 | 34% helix, 26% strand | P13569 |
| B | Cystic fibrosis transmembrane conductance regulator | protein | 219 | 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
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1188 | 0.81 | 0.82 | 127 | MG, ATP |
Interfaces
1 interface between chains.
- A–B · 873 Ų buried · 6 hydrogen bonds · protein-protein
Compared structures
- 2PZE · Minimal human CFTR first nucleotide binding domain as a head-to-tail dimer · the same entry in another collection · chain B against B, 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 2PZE · PDBe 2PZE · UniProt P13569
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