Research workbench
Crystal structure of formate dehydrogenase FDH2 enzyme from Granulicella mallensis MP5ACTX8 in the apo form.
Analyse Crystal structure of formate dehydrogenase FDH2 enzyme from Granulicella… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6T8C
- Type
- protein
- Length
- 1,494 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.97
- Source
- Granulicella mallensis (strain ATCC BAA-1857 / DSM 23137 / MP5ACTX8)
- Molecule
- Formate dehydrogenase
- EC
- 1.17.1.9
- UniProt
- G8NTI5
- Pockets
- 15 · best druggability 0.78
Structure
x-ray diffraction · resolution 1.97 · 2 distinct chains · 36% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | Formate dehydrogenase (EC 1.17.1.9) | protein | 374 | 36% helix, 17% strand | G8NTI5 |
| B, D | Formate dehydrogenase (EC 1.17.1.9) | protein | 373 | 36% helix, 17% strand | G8NTI5 |
Pockets
15 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1193 | 0.78 | 0.80 | 90 | empty |
| 2 | 1099 | 0.76 | 0.78 | 79 | empty |
| 3 | 794 | 0.74 | 0.78 | 87 | empty |
| 4 | 476 | 0.71 | 0.81 | 50 | empty |
| 5 | 60 | 0.60 | 0.91 | 15 | empty |
Interfaces
3 interfaces between chains.
- B–C · 3863 Ų buried · 43 hydrogen bonds · protein-protein
- A–B · 794 Ų buried · 4 hydrogen bonds · protein-protein
- B–D · 175 Ų buried · 3 hydrogen bonds · protein-protein
Compared structures
- 6T8C · Crystal structure of formate dehydrogenase FDH2 enzyme from granulicella mallensis… · 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 G8NTI5
- Elsewhere: RCSB PDB 6T8C · PDBe 6T8C · UniProt G8NTI5
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