Research workbench
Complex of histidinol-phosphate aminotransferase (hisc) from thermotoga maritima (apo-form)
Analyse Complex of histidinol-phosphate aminotransferase (hisc) from thermotoga… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1UU1
- Type
- protein
- Length
- 1,332 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
- PMP, HSA
- Pockets
- 20 · best druggability 0.85
Structure
x-ray diffraction · 3 distinct chains · 43% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Histidinol-phosphate aminotransferase (EC 2.6.1.9) | protein | 329 | 43% helix, 16% strand | Q9X0D0 |
| B, D | Histidinol-phosphate aminotransferase (EC 2.6.1.9) | protein | 334 | 43% helix, 16% strand | Q9X0D0 |
| C | Histidinol-phosphate aminotransferase (EC 2.6.1.9) | protein | 335 | 42% helix, 16% strand | Q9X0D0 |
Ligands and binding sites
- PMP · 4'-deoxy-4'-aminopyridoxal-5'-phosphate · ligand · 4 copies · chains A, B, C, D
- HSA · Phosphoric acid mono-[2-amino-3-(3H-imidazol-4-yl)-propyl]ester · ligand · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 968 | 0.85 | 0.86 | 87 | PMP, HSA |
| 2 | 809 | 0.76 | 0.80 | 77 | empty |
| 3 | 280 | 0.75 | 0.88 | 48 | PMP, HSA |
| 4 | 429 | 0.73 | 0.83 | 57 | PMP, HSA |
| 5 | 447 | 0.73 | 0.82 | 56 | PMP, HSA |
Interfaces
6 interfaces between chains.
- C–D · 3382 Ų buried · 40 hydrogen bonds · protein-protein
- A–B · 3284 Ų buried · 40 hydrogen bonds · protein-protein
- B–D · 762 Ų buried · 23 hydrogen bonds · protein-protein
- B–C · 259 Ų buried · 12 hydrogen bonds · protein-protein
- A–C · 179 Ų buried · 4 hydrogen bonds · protein-protein
Compared structures
- 1UU1 · Complex of Histidinol-phosphate aminotransferase (HisC) from Thermotoga maritima… · the same entry in another collection · chain A against A, TM-score 1.00
- Q9X0D0 · AlphaFold monomer V2.0 prediction for histidinol-phosphate aminotransferase (Q9X0D0) · a predicted model of the same protein · chain A 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 1UU1 · PDBe 1UU1 · UniProt Q9X0D0
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.