MolNFT v1 · #24400 · protein
Histidinol-phosphate aminotransferase (hisc) from thermotoga maritima (apo-form)
1UU0: “Histidinol-phosphate aminotransferase (hisc) from thermotoga maritima (apo-form)”. X-ray diffraction, 1 ligand (PO4), 16 pockets (best druggability 0.83). MolNFT v1 #24400 on GenesisL1: 3D structure, binding sites and pockets in…
- PDB
- 1UU0
- Type
- protein
- Length
- 1,283 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
- PO4
- Pockets
- 16 · best druggability 0.83
Structure
x-ray diffraction · 4 distinct chains · 40% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Histidinol-phosphate aminotransferase (EC 2.6.1.9) | protein | 328 | 40% helix, 16% strand | Q9X0D0 |
| B | Histidinol-phosphate aminotransferase (EC 2.6.1.9) | protein | 315 | 44% helix, 17% strand | Q9X0D0 |
| C | Histidinol-phosphate aminotransferase (EC 2.6.1.9) | protein | 311 | 33% helix, 12% strand | Q9X0D0 |
| D | Histidinol-phosphate aminotransferase (EC 2.6.1.9) | protein | 329 | 43% helix, 17% strand | Q9X0D0 |
Ligands and binding sites
- PO4 · Phosphate ion · ion · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
16 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 799 | 0.83 | 0.85 | 85 | empty |
| 2 | 818 | 0.77 | 0.81 | 64 | empty |
| 3 | 256 | 0.70 | 0.85 | 33 | empty |
| 4 | 126 | 0.55 | 0.82 | 31 | PO4 |
| 5 | 82 | 0.54 | 0.85 | 25 | empty |
Interfaces
6 interfaces between chains.
- C–D · 2575 Ų buried · 37 hydrogen bonds · protein-protein
- A–B · 2563 Ų buried · 38 hydrogen bonds · protein-protein
- A–C · 662 Ų buried · 9 hydrogen bonds · protein-protein
- A–D · 333 Ų buried · 8 hydrogen bonds · protein-protein
- B–D · 198 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 1UU0 · Histidinol-phosphate aminotransferase (HisC) from Thermotoga maritima (Apo-form) · 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 1UU0 · PDBe 1UU0 · UniProt Q9X0D0
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