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Crystal structure of E. COLI guanosine kinase
Analyse Crystal structure of E. COLI guanosine kinase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6VWO
- Type
- protein
- Length
- 383 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Inosine-guanosine kinase
- EC
- 2.7.1.73
- UniProt
- P0AEW6
- Ligands
- GMP, ADP, K, MG
- Pockets
- 3 · best druggability 0.76
Structure
x-ray diffraction · 1 distinct chain · 37% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Inosine-guanosine kinase (EC 2.7.1.73) | protein | 383 | 37% helix, 21% strand | P0AEW6 |
Ligands and binding sites
- GMP · Guanosine · ligand · 2 copies · chains A
- ADP · Adenosine-5'-diphosphate · ligand · chains A
- K · Potassium ion · metal · 3 copies · chains A
- MG · Magnesium ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 561 | 0.76 | 0.83 | 57 | ADP, GMP, K, MG |
| 2 | 91 | 0.43 | 0.80 | 22 | empty |
| 3 | 72 | 0.31 | 0.74 | 21 | empty |
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 P0AEW6
- Elsewhere: RCSB PDB 6VWO · PDBe 6VWO · UniProt P0AEW6
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