Research workbench
Molecular analysis of the interaction between the prostacyclin receptor and the first PDZ domain of PDZK1
Analyse Molecular analysis of the interaction between the prostacyclin receptor and the… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4F8K
- Type
- protein
- Length
- 218 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- NA(+)/H(+) exchange regulatory cofactor nhe-RF3, prostacyclin receptor
- UniProt
- Q9JIL4, P43252
- Pockets
- 2 · best druggability 0.64
Structure
x-ray diffraction · 1 distinct chain · 24% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | NA(+)/H(+) exchange regulatory cofactor nhe-RF3, prostacyclin receptor | protein | 109 | 24% helix, 28% strand | Q9JIL4, P43252 |
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 388 | 0.64 | 0.79 | 40 | empty |
| 2 | 73 | 0.36 | 0.76 | 13 | empty |
Interfaces
1 interface between chains.
- A–B · 686 Ų buried · 18 hydrogen bonds · protein-protein
Compared structures
- 4F8K · Molecular analysis of the interaction between the prostacyclin receptor and the first PDZ… · the same entry in another collection · chain A against A, TM-score 1.00
- Q9JIL4 · AlphaFold monomer V2.0 prediction for NA(+)/H(+) exchange regulatory cofactor nhe-RF3… · a predicted model of the same protein · chain A against A, TM-score 0.96
- P43252 · AlphaFold monomer V2.0 prediction for prostacyclin receptor (P43252) · a predicted model of the same protein · chain A against A, TM-score 0.30
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 Q9JIL4
- Every structure of UniProt P43252
- Elsewhere: RCSB PDB 4F8K · PDBe 4F8K · UniProt Q9JIL4 · UniProt P43252
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