Research workbench
Crystal structure of putative histidinol-phosphate aminotransferase (NP_281508.1) from campylobacter jejuni at 2.01 a resolution
Analyse Crystal structure of putative histidinol-phosphate aminotransferase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3GET
- Type
- protein
- Length
- 726 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
- Q9PII2
- Pockets
- 8 · best druggability 0.76
Structure
x-ray diffraction · 2 distinct chains · 47% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Histidinol-phosphate aminotransferase (EC 2.6.1.9) | protein | 365 | 46% helix, 15% strand | Q9PII2 |
| B | Histidinol-phosphate aminotransferase (EC 2.6.1.9) | protein | 361 | 48% helix, 15% strand | Q9PII2 |
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 | 442 | 0.76 | 0.85 | 44 | empty |
| 2 | 787 | 0.73 | 0.79 | 64 | empty |
| 3 | 684 | 0.70 | 0.77 | 61 | empty |
| 4 | 105 | 0.39 | 0.76 | 18 | empty |
| 5 | 91 | 0.37 | 0.76 | 18 | empty |
Interfaces
1 interface between chains.
- A–B · 2899 Ų buried · 51 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 12 modified (engineered, cofactor).
Compared structures
- 3GET · Crystal structure of putative histidinol-phosphate aminotransferase (NP_281508.1) from… · the same entry in another collection · chain B against B, TM-score 1.00
- Q9PII2 · AlphaFold monomer V2.0 prediction for histidinol-phosphate aminotransferase (Q9PII2) · a predicted model of the same protein · chain B 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 Q9PII2
- Elsewhere: RCSB PDB 3GET · PDBe 3GET · UniProt Q9PII2
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