MolNFT v1 · #138086 · protein
Phosphorylated, ATP-bound structure of zebrafish cystic fibrosis transmembrane conductance regulator (cftr)
5W81: “Phosphorylated, ATP-bound structure of zebrafish cystic fibrosis transmembrane conductance regulator (cftr)”. Electron microscopy, 2 ligands (ATP, MG), 20 pockets (best druggability 0.88). MolNFT v1 #138086 on GenesisL1: 3D…
- PDB
- 5W81
- Type
- protein
- Length
- 1,173 residues
- Chains
- 1
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cystic fibrosis transmembrane conductance regulator
- EC
- 3.6.3.49
- UniProt
- Q1LX78
- Ligands
- ATP, MG
- Pockets
- 20 · best druggability 0.88
Structure
electron microscopy · 1 distinct chain · 61% helix, 9% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cystic fibrosis transmembrane conductance regulator (EC 3.6.3.49) | protein | 1173 | 61% helix, 9% strand | Q1LX78 |
Ligands and binding sites
- ATP · Adenosine-5'-triphosphate · ligand · 2 copies · chains A
- MG · Magnesium ion · metal · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 12 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 931 | 0.88 | 0.89 | 105 | empty |
| 2 | 785 | 0.85 | 0.87 | 94 | ATP, MG |
| 3 | 370 | 0.80 | 0.90 | 54 | MG |
| 4 | 352 | 0.78 | 0.88 | 53 | empty |
| 5 | 131 | 0.67 | 0.89 | 35 | empty |
Compared structures
- 5W81 · Phosphorylated, ATP-bound structure of zebrafish cystic fibrosis transmembrane… · the same entry in another collection · chain A against A, TM-score 1.00
- Q1LX78 · AlphaFold monomer V2.0 prediction for cystic fibrosis transmembrane conductance regulator… · a predicted model of the same protein · chain A against A, TM-score 0.98
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 Q1LX78
- Elsewhere: RCSB PDB 5W81 · PDBe 5W81 · UniProt Q1LX78
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