Research workbench
4-hydroxyisoleucine dehydrogenase complexed with NADH
Analyse 4-hydroxyisoleucine dehydrogenase complexed with NADH in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5GWR
- Type
- protein
- Length
- 924 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.2
- Source
- Bacillus thuringiensis
- Molecule
- 4-hydroxyisolecuine dehydrogenase
- UniProt
- A0A0K0Q8K4
- Ligands
- NAD
- Pockets
- 14 · best druggability 0.85
Structure
x-ray diffraction · resolution 2.2 · 2 distinct chains · 49% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 4-hydroxyisolecuine dehydrogenase | protein | 243 | 49% helix, 16% strand | A0A0K0Q8K4 |
| B, C, D | 4-hydroxyisolecuine dehydrogenase | protein | 227 | 48% helix, 18% strand | A0A0K0Q8K4 |
Ligands and binding sites
- NAD · Nicotinamide-adenine-dinucleotide · ligand · 4 copies · chains A, B, C, D
- EDO · 1,2-ethanediol · additive · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
14 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1091 | 0.85 | 0.86 | 56 | empty |
| 2 | 477 | 0.76 | 0.84 | 50 | NAD |
| 3 | 468 | 0.68 | 0.79 | 47 | NAD |
| 4 | 513 | 0.67 | 0.78 | 47 | NAD |
| 5 | 484 | 0.66 | 0.78 | 43 | NAD |
Interfaces
6 interfaces between chains.
- A–B · 1657 Ų buried · 22 hydrogen bonds · protein-protein
- C–D · 1643 Ų buried · 23 hydrogen bonds · protein-protein
- B–C · 1589 Ų buried · 17 hydrogen bonds · protein-protein
- A–D · 1586 Ų buried · 17 hydrogen bonds · protein-protein
- B–D · 445 Ų buried · 10 hydrogen bonds · protein-protein
Compared structures
- 5GWR · 4-hydroxyisoleucine dehydrogenase complexed with NADH · 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 A0A0K0Q8K4
- Elsewhere: RCSB PDB 5GWR · PDBe 5GWR · UniProt A0A0K0Q8K4
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