MolNFT v1 · #14020 · protein
Crystal structure of mouse guanylate kinase in complex with gmp and ADP
1LVG: “Crystal structure of mouse guanylate kinase in complex with gmp and ADP”. X-ray diffraction, 3 ligands (ADP, 5GP, K), 1 pocket (best druggability 0.72). MolNFT v1 #14020 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1LVG
- Type
- protein
- Length
- 190 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Guanylate kinase
- EC
- 2.7.4.8
- UniProt
- Q64520
- Ligands
- ADP, 5GP, K
- Pockets
- 1 · best druggability 0.72
Structure
x-ray diffraction · 1 distinct chain · 44% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Guanylate kinase (EC 2.7.4.8) | protein | 190 | 44% helix, 22% strand | Q64520 |
Ligands and binding sites
- ADP · Adenosine-5'-diphosphate · ligand · chains A
- 5GP · Guanosine-5'-monophosphate · ligand · chains A
- K · Potassium ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 344 | 0.72 | 0.84 | 48 | K, ADP, 5GP |
Compared structures
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 Q64520
- Elsewhere: RCSB PDB 1LVG · PDBe 1LVG · UniProt Q64520
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