Research workbench
Crystal structure of formate dehydrogenase mutant C256I/E261P/S381I from pseudomonas sp. 101
Analyse Crystal structure of formate dehydrogenase mutant C256I/E261P/S381I from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6JWG
- Type
- protein
- Length
- 743 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Formate dehydrogenase
- EC
- 1.17.1.9
- UniProt
- P33160
- Pockets
- 9 · best druggability 0.72
Structure
x-ray diffraction · 2 distinct chains · 35% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Formate dehydrogenase (EC 1.17.1.9) | protein | 374 | 35% helix, 17% strand | P33160 |
| B | Formate dehydrogenase (EC 1.17.1.9) | protein | 369 | 35% helix, 17% strand | P33160 |
Ligands and binding sites
- GOL · Glycerol · additive · 2 copies · chains A, B
- TRS · 2-amino-2-hydroxymethyl-propane-1,3-diol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
9 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 493 | 0.72 | 0.81 | 56 | GOL |
| 2 | 481 | 0.69 | 0.80 | 50 | TRS |
| 3 | 257 | 0.53 | 0.76 | 40 | empty |
| 4 | 120 | 0.47 | 0.78 | 14 | empty |
| 5 | 118 | 0.46 | 0.78 | 25 | empty |
Interfaces
1 interface between chains.
- A–B · 3927 Ų buried · 56 hydrogen bonds · protein-protein
Compared structures
- 6JWG · Crystal structure of Formate dehydrogenase mutant C256I/E261P/S381I from Pseudomonas sp.… · the same entry in another collection · chain A against A, TM-score 1.00
- P33160 · AlphaFold monomer V2.0 prediction for formate dehydrogenase (P33160) · a predicted model of the same protein · chain A against A, TM-score 0.96
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 6JWG · PDBe 6JWG · UniProt P33160
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.