MolNFT v1 · #163032 · protein
Extended NHERF1 PDZ2 domain in complex with the PDZ-binding motif of cftr
6RQR · NA(+)/H(+) exchange regulatory cofactor nhe-RF1,CYSTIC…: “Extended NHERF1 PDZ2 domain in complex with the PDZ-binding motif of cftr”. X-ray diffraction, 2 pockets (best druggability 0.34). MolNFT v1 #163032 on GenesisL1: 3D…
- PDB
- 6RQR
- Type
- protein
- Length
- 250 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- NA(+)/H(+) exchange regulatory cofactor nhe-RF1,CYSTIC fibrosis transmembrane conductance…
- EC
- 5.6.1.6
- UniProt
- O14745, P13569
- Pockets
- 2 · best druggability 0.34
Structure
x-ray diffraction · 1 distinct chain · 26% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | NA(+)/H(+) exchange regulatory cofactor nhe-RF1,CYSTIC fibrosis transmembrane conductance regulator (EC 5.6.1.6) | protein | 125 | 26% helix, 26% strand | O14745, P13569 |
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 68 | 0.34 | 0.76 | 12 | empty |
| 2 | 63 | 0.34 | 0.77 | 23 | empty |
Interfaces
1 interface between chains.
- A–B · 639 Ų buried · 22 hydrogen bonds · protein-protein
Compared structures
- 6RQR · Extended NHERF1 PDZ2 domain in complex with the PDZ-binding motif of CFTR · the same entry in another collection · chain A against A, TM-score 1.00
- O14745 · AlphaFold monomer V2.0 prediction for NA(+)/H(+) exchange regulatory cofactor nhe-RF1… · a predicted model of the same protein · chain A against A, TM-score 0.85
- P13569 · AlphaFold monomer V2.0 prediction for cystic fibrosis transmembrane conductance regulator… · a predicted model of the same protein · chain A against A, TM-score 0.33
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 O14745
- Every structure of UniProt P13569
- Elsewhere: RCSB PDB 6RQR · PDBe 6RQR · UniProt O14745 · UniProt P13569
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