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High resolution structures of holo and apo formate dehydrogenase
Analyse High resolution structures of holo and apo formate dehydrogenase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2NAC
- Type
- protein
- Length
- 748 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- NAD-dependent formate dehydrogenase
- EC
- 1.2.1.2
- UniProt
- P33160
- Ligands
- SO4
- Pockets
- 8 · best druggability 0.67
Structure
x-ray diffraction · 1 distinct chain · 34% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | NAD-dependent formate dehydrogenase (EC 1.2.1.2) | protein | 374 | 34% helix, 18% strand | P33160 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 430 | 0.67 | 0.79 | 49 | SO4 |
| 2 | 324 | 0.64 | 0.80 | 34 | SO4 |
| 3 | 352 | 0.61 | 0.78 | 60 | empty |
| 4 | 134 | 0.52 | 0.80 | 17 | empty |
| 5 | 113 | 0.44 | 0.77 | 14 | empty |
Interfaces
1 interface between chains.
- A–B · 3908 Ų buried · 54 hydrogen bonds · protein-protein
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 P33160
- Elsewhere: RCSB PDB 2NAC · PDBe 2NAC · UniProt P33160
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