Research workbench
Histidinol-phosphate aminotransferase from corynebacterium glutamicum
Analyse Histidinol-phosphate aminotransferase from corynebacterium glutamicum in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3CQ4
- Type
- protein
- Length
- 704 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Histidinol-phosphate aminotransferase
- EC
- 2.6.1.9
- UniProt
- Q9KJU4
- Pockets
- 7 · best druggability 0.69
Structure
x-ray diffraction · 2 distinct chains · 43% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Histidinol-phosphate aminotransferase (EC 2.6.1.9) | protein | 357 | 43% helix, 15% strand | Q9KJU4 |
| B | Histidinol-phosphate aminotransferase (EC 2.6.1.9) | protein | 347 | 44% helix, 16% strand | Q9KJU4 |
Ligands and binding sites
- ACT · Acetate ion · additive · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 347 | 0.69 | 0.82 | 34 | ACT |
| 2 | 305 | 0.68 | 0.83 | 33 | ACT |
| 3 | 339 | 0.59 | 0.77 | 48 | empty |
| 4 | 67 | 0.48 | 0.84 | 23 | empty |
| 5 | 60 | 0.46 | 0.84 | 20 | empty |
Interfaces
1 interface between chains.
- A–B · 2858 Ų buried · 27 hydrogen bonds · protein-protein
Compared structures
- 3CQ4 · Histidinol-phosphate aminotransferase from Corynebacterium glutamicum · the same entry in another collection · chain A against A, TM-score 1.00
- Q9KJU4 · AlphaFold monomer V2.0 prediction for histidinol-phosphate aminotransferase (Q9KJU4) · a predicted model of the same protein · chain B 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 Q9KJU4
- Elsewhere: RCSB PDB 3CQ4 · PDBe 3CQ4 · UniProt Q9KJU4
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