Research workbench
Phosphorylated cystic fibrosis transmembrane conductance regulator (cftr) nucleotide-binding domain one (NBD1) with ATP
Analyse Phosphorylated cystic fibrosis transmembrane conductance regulator (cftr)… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1R0Z
- Type
- protein
- Length
- 1,086 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cystic fibrosis transmembrane conductance regulator
- UniProt
- P26361
- Ligands
- ATP, MG
- Pockets
- 11 · best druggability 0.77
Structure
x-ray diffraction · 4 distinct chains · 41% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cystic fibrosis transmembrane conductance regulator | protein | 275 | 42% helix, 21% strand | P26361 |
| B | Cystic fibrosis transmembrane conductance regulator | protein | 275 | 40% helix, 21% strand | P26361 |
| C | Cystic fibrosis transmembrane conductance regulator | protein | 277 | 41% helix, 22% strand | P26361 |
| D | Cystic fibrosis transmembrane conductance regulator | protein | 259 | 41% helix, 24% strand | P26361 |
Ligands and binding sites
- ATP · Adenosine-5'-triphosphate · 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
11 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 958 | 0.77 | 0.80 | 85 | MG, ATP |
| 2 | 545 | 0.69 | 0.79 | 52 | empty |
| 3 | 666 | 0.68 | 0.77 | 49 | MG, ATP |
| 4 | 653 | 0.68 | 0.77 | 52 | MG, ATP |
| 5 | 309 | 0.57 | 0.76 | 36 | empty |
Interfaces
3 interfaces between chains.
- A–B · 1105 Ų buried · 10 hydrogen bonds · protein-protein
- A–D · 603 Ų buried · 5 hydrogen bonds · protein-protein
- B–C · 304 Ų buried · 5 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 15 modified (phosphorylation).
Compared structures
- 1R0Z · Phosphorylated Cystic fibrosis transmembrane conductance regulator (CFTR)… · the same entry in another collection · chain D against D, TM-score 1.00
- P26361 · AlphaFold monomer V2.0 prediction for cystic fibrosis transmembrane conductance regulator… · a predicted model of the same protein · chain D against A, TM-score 0.93
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 1R0Z · PDBe 1R0Z · UniProt P26361
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.