Research workbench
The L-histidinol dehydrogenase (hisd) structure implicates domain swapping and gene duplication.
Analyse The L-histidinol dehydrogenase (hisd) structure implicates domain swapping and… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1K75
- Type
- protein
- Length
- 862 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- L-histidinol dehydrogenase
- EC
- 1.1.1.23
- UniProt
- P06988
- Ligands
- SO4
- Pockets
- 8 · best druggability 0.83
Structure
x-ray diffraction · 1 distinct chain · 49% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | L-histidinol dehydrogenase (EC 1.1.1.23) | protein | 431 | 49% helix, 17% strand | P06988 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 503 | 0.83 | 0.90 | 53 | empty |
| 2 | 200 | 0.76 | 0.91 | 40 | empty |
| 3 | 215 | 0.75 | 0.90 | 36 | empty |
| 4 | 104 | 0.47 | 0.80 | 27 | empty |
| 5 | 79 | 0.40 | 0.78 | 21 | empty |
Interfaces
1 interface between chains.
- A–B · 5329 Ų buried · 85 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 12 modified (engineered).
Compared structures
- 1K75 · The L-histidinol dehydrogenase (hisD) structure implicates domain swapping and gene… · the same entry in another collection · chain A against A, TM-score 1.00
- P06988 · AlphaFold monomer V2.0 prediction for histidinol dehydrogenase (P06988) · 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 P06988
- Elsewhere: RCSB PDB 1K75 · PDBe 1K75 · UniProt P06988
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