MolNFT v2 · #105195 · protein
Neutron diffraction reveals hydrogen bonds critical for cGMP-selective activation: Insights for PKG agonist design
4QX5: “Neutron diffraction reveals hydrogen bonds critical for cGMP-selective activation: Insights for PKG agonist…”. X-ray diffraction at 1.318. MolNFT v2 #105195 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 4QX5
- Type
- protein
- Length
- 127 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.318
- Source
- Homo sapiens
- UniProt
- Q13976
Structure
x-ray diffraction · resolution 1.318 · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 127 | — | Q13976 |
Compared structures
- 4QX5 · Neutron diffraction reveals hydrogen bonds critical for cgmp-selective activation… · the same entry in another collection · chain A against A, TM-score 1.00
- Q13976 · AlphaFold monomer V2.0 prediction for cgmp-dependent protein kinase 1 (Q13976) · a predicted model of the same protein · chain A against A, TM-score 0.91
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 Q13976
- Elsewhere: RCSB PDB 4QX5 · PDBe 4QX5 · UniProt Q13976
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