MolNFT v1 · #18903 · protein
Mouse cftr NBD1 with AMP.PNP
1Q3H · Cystic fibrosis transmembrane conductance regulator: “Mouse cftr NBD1 with AMP.PNP”. X-ray diffraction, 2 ligands (ANP, MG), 12 pockets (best druggability 0.69). MolNFT v1 #18903 on GenesisL1: 3D structure, binding sites and pockets…
- PDB
- 1Q3H
- Type
- protein
- Length
- 1,062 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cystic fibrosis transmembrane conductance regulator
- UniProt
- P26361
- Ligands
- ANP, MG
- Pockets
- 12 · best druggability 0.69
Structure
x-ray diffraction · 4 distinct chains · 42% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cystic fibrosis transmembrane conductance regulator | protein | 265 | 42% helix, 23% strand | P26361 |
| B | Cystic fibrosis transmembrane conductance regulator | protein | 267 | 42% helix, 22% strand | P26361 |
| C | Cystic fibrosis transmembrane conductance regulator | protein | 266 | 42% helix, 23% strand | P26361 |
| D | Cystic fibrosis transmembrane conductance regulator | protein | 264 | 41% helix, 23% strand | P26361 |
Ligands and binding sites
- ANP · Phosphoaminophosphonic acid-adenylate ester · ligand · 4 copies · chains A, B, C, D
- MG · Magnesium ion · metal · 4 copies · chains A, B, C, D
- ACY · Acetic acid · additive · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
12 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 576 | 0.69 | 0.78 | 56 | empty |
| 2 | 334 | 0.63 | 0.79 | 49 | MG, ANP |
| 3 | 298 | 0.56 | 0.76 | 37 | empty |
| 4 | 220 | 0.52 | 0.77 | 22 | empty |
| 5 | 169 | 0.45 | 0.75 | 32 | MG, ANP |
Interfaces
3 interfaces between chains.
- A–B · 862 Ų buried · 5 hydrogen bonds · protein-protein
- A–D · 599 Ų buried · 5 hydrogen bonds · protein-protein
- B–C · 302 Ų buried · 3 hydrogen bonds · protein-protein
Compared structures
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 P26361
- Elsewhere: RCSB PDB 1Q3H · PDBe 1Q3H · UniProt P26361
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