Research workbench
Histidinol-phosphate aminotransferase (hisc) from thermotoga maritima
Analyse Histidinol-phosphate aminotransferase (hisc) from thermotoga maritima in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1H1C
- Type
- protein
- Length
- 1,282 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Histidinol-phosphate aminotransferase
- EC
- 2.6.1.9
- UniProt
- Q9X0D0
- Ligands
- PLP
- Pockets
- 18 · best druggability 0.81
Structure
x-ray diffraction · 4 distinct chains · 41% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Histidinol-phosphate aminotransferase (EC 2.6.1.9) | protein | 329 | 40% helix, 16% strand | Q9X0D0 |
| B | Histidinol-phosphate aminotransferase (EC 2.6.1.9) | protein | 315 | 43% helix, 15% strand | Q9X0D0 |
| C | Histidinol-phosphate aminotransferase (EC 2.6.1.9) | protein | 309 | 41% helix, 11% strand | Q9X0D0 |
| D | Histidinol-phosphate aminotransferase (EC 2.6.1.9) | protein | 329 | 40% helix, 16% strand | Q9X0D0 |
Ligands and binding sites
- PLP · Pyridoxal-5'-phosphate · ligand · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
18 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 861 | 0.81 | 0.83 | 76 | empty |
| 2 | 335 | 0.69 | 0.82 | 40 | empty |
| 3 | 136 | 0.68 | 0.89 | 35 | empty |
| 4 | 314 | 0.65 | 0.81 | 31 | empty |
| 5 | 217 | 0.60 | 0.81 | 30 | empty |
Interfaces
6 interfaces between chains.
- A–B · 2586 Ų buried · 37 hydrogen bonds · protein-protein
- C–D · 2578 Ų buried · 38 hydrogen bonds · protein-protein
- A–C · 515 Ų buried · 6 hydrogen bonds · protein-protein
- A–D · 299 Ų buried · 3 hydrogen bonds · protein-protein
- B–D · 215 Ų buried · 1 hydrogen bond · protein-protein
Modifications
Observed in the structure: 32 modified, 4 cofactor (engineered, pyridoxal phosphate Schiff base).
Compared structures
- 1H1C · Histidinol-phosphate aminotransferase (HisC) from Thermotoga maritima · the same entry in another collection · chain D against D, TM-score 1.00
- Q9X0D0 · AlphaFold monomer V2.0 prediction for histidinol-phosphate aminotransferase (Q9X0D0) · a predicted model of the same protein · chain B against A, TM-score 0.99
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 Q9X0D0
- Elsewhere: RCSB PDB 1H1C · PDBe 1H1C · UniProt Q9X0D0
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