Research workbench
Crystal structure of a putative rossmann-like dehydrogenase (CGL2689) from corynebacterium glutamicum at 2.07 a resolution
Analyse Crystal structure of a putative rossmann-like dehydrogenase (CGL2689) from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3DFU
- Type
- protein
- Length
- 456 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Uncharacterized protein from 6-phosphogluconate dehydrogenase-like family
- UniProt
- Q8NM90
- Pockets
- 2 · best druggability 0.72
Structure
x-ray diffraction · 2 distinct chains · 55% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Uncharacterized protein from 6-phosphogluconate dehydrogenase-like family | protein | 228 | 55% helix, 15% strand | Q8NM90 |
| B | Uncharacterized protein from 6-phosphogluconate dehydrogenase-like family | protein | 228 | 55% helix, 16% strand | Q8NM90 |
Ligands and binding sites
- GOL · Glycerol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 402 | 0.72 | 0.83 | 43 | empty |
| 2 | 440 | 0.65 | 0.78 | 39 | empty |
Interfaces
1 interface between chains.
- A–B · 3128 Ų buried · 37 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 11 modified (engineered).
Compared structures
- 3DFU · Crystal structure of a putative rossmann-like dehydrogenase (CGL2689) from… · the same entry in another collection · chain A against A, TM-score 1.00
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 Q8NM90
- Elsewhere: RCSB PDB 3DFU · PDBe 3DFU · UniProt Q8NM90
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