Research workbench
AlphaFold monomer V2.0 prediction for nucleoside diphosphate kinase (B4RMG0)
Analyse AlphaFold monomer V2.0 prediction for nucleoside diphosphate kinase (B4RMG0) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- B4RMG0
- Type
- protein
- Length
- 141 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x82Bbe1E2D8b1352DDE783388f32DC9513683f83C
- Molecule
- Nucleoside diphosphate kinase
- UniProt
- B4RMG0
- Pockets
- 1 · best druggability 0.47
Structure
1 distinct chain · 46% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Nucleoside diphosphate kinase | protein | 141 | 46% helix, 21% strand | B4RMG0 |
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 162 | 0.47 | 0.76 | 27 | empty |
Compared structures
- 5V6D · Crystal structure of nucleoside diphosphate kinase from Neisseria gonorrhoeae in complex… · an experimental structure of the same protein · chain A against N, TM-score 0.99
- 5V6D · Crystal structure of nucleoside diphosphate kinase from neisseria gonorrhoeae in complex… · an experimental structure of the same protein · chain A against F, TM-score 0.99
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 B4RMG0
- Elsewhere: UniProt B4RMG0 · AlphaFold DB B4RMG0
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