MolNFT v2 · #181199 · protein
Crystal Structure of human cyclic GMP-AMP synthase in complex with 6-(2-chloro-4-methylphenyl)-3-(2-phenylethyl)benzimidazole-4-carboxylic acid
7FUK: “Crystal Structure of human cyclic GMP-AMP synthase in complex with…”. X-ray diffraction at 1.606, 2 ligands (YQU, ZN). MolNFT v2 #181199 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 7FUK
- Type
- protein
- Length
- 353 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.606
- Source
- Homo sapiens
- UniProt
- Q8N884
- Ligands
- YQU, ZN
Structure
x-ray diffraction · resolution 1.606 · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 353 | — | Q8N884 |
Ligands and binding sites
- YQU · (5M)-5-(2-chloro-4-methylphenyl)-1-(2-phenylethyl)-1H-benzimidazole-7-carboxylic acid · ligand · chains A
- ZN · Zinc ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- Q8N884 · AlphaFold monomer V2.0 prediction for cyclic gmp-AMP synthase (Q8N884) · a predicted model of the same protein · chain A against A, TM-score 0.94
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 Q8N884
- Elsewhere: RCSB PDB 7FUK · PDBe 7FUK · UniProt Q8N884
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