Research workbench
Crystal structure of a putative aminotransferase (BPSL1724) from burkholderia pseudomallei K96243 at 2.60 a resolution
Analyse Crystal structure of a putative aminotransferase (BPSL1724) from burkholderia… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3P1T
- Type
- protein
- Length
- 1,279 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Putative histidinol-phosphate aminotransferase
- UniProt
- Q63U92
- Ligands
- SO4
- Pockets
- 20 · best druggability 0.68
Structure
x-ray diffraction · 4 distinct chains · 43% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Putative histidinol-phosphate aminotransferase | protein | 322 | 42% helix, 17% strand | Q63U92 |
| B | Putative histidinol-phosphate aminotransferase | protein | 319 | 43% helix, 18% strand | Q63U92 |
| C | Putative histidinol-phosphate aminotransferase | protein | 321 | 43% helix, 17% strand | Q63U92 |
| D | Putative histidinol-phosphate aminotransferase | protein | 317 | 44% helix, 18% strand | Q63U92 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 4 copies · chains A, B, D
- EDO · 1,2-ethanediol · additive · 13 copies · chains A, B, C, D
- TLA · L(+)-tartaric acid · additive · 5 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, 12 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 348 | 0.68 | 0.81 | 45 | EDO |
| 2 | 324 | 0.67 | 0.82 | 47 | TLA |
| 3 | 53 | 0.67 | 0.96 | 20 | empty |
| 4 | 340 | 0.66 | 0.81 | 26 | empty |
| 5 | 363 | 0.66 | 0.80 | 26 | empty |
Interfaces
3 interfaces between chains.
- C–D · 2112 Ų buried · 29 hydrogen bonds · protein-protein
- A–B · 2106 Ų buried · 29 hydrogen bonds · protein-protein
- B–D · 466 Ų buried · 8 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 16 modified (engineered).
Compared structures
- 3P1T · Crystal structure of a putative aminotransferase (BPSL1724) from Burkholderia… · the same entry in another collection · chain A 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 Q63U92
- Elsewhere: RCSB PDB 3P1T · PDBe 3P1T · UniProt Q63U92
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.