Research workbench
Crystal structure of the branched-chain-amino-acid aminotransferase from haliangium ochraceum
Analyse Crystal structure of the branched-chain-amino-acid aminotransferase from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6H65
- Type
- protein
- Length
- 1,837 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Branched-chain-amino-acid aminotransferase
- EC
- 2.6.1.42
- UniProt
- D0LR31
- Ligands
- PLP
- Pockets
- 20 · best druggability 0.78
Structure
x-ray diffraction · 5 distinct chains · 31% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, D | Branched-chain-amino-acid aminotransferase (EC 2.6.1.42) | protein | 305 | 31% helix, 30% strand | D0LR31 |
| B | Branched-chain-amino-acid aminotransferase (EC 2.6.1.42) | protein | 306 | 31% helix, 28% strand | D0LR31 |
| C | Branched-chain-amino-acid aminotransferase (EC 2.6.1.42) | protein | 308 | 31% helix, 30% strand | D0LR31 |
| E | Branched-chain-amino-acid aminotransferase (EC 2.6.1.42) | protein | 307 | 31% helix, 28% strand | D0LR31 |
| F | Branched-chain-amino-acid aminotransferase (EC 2.6.1.42) | protein | 306 | 31% helix, 30% strand | D0LR31 |
Ligands and binding sites
- PLP · Pyridoxal-5'-phosphate · ligand · 6 copies · chains A, B, C, D, E, F
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 16 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1074 | 0.78 | 0.80 | 92 | empty |
| 2 | 1090 | 0.78 | 0.80 | 96 | empty |
| 3 | 654 | 0.71 | 0.78 | 80 | empty |
| 4 | 100 | 0.71 | 0.94 | 18 | empty |
| 5 | 97 | 0.70 | 0.93 | 18 | empty |
Interfaces
8 interfaces between chains.
- A–D · 775 Ų buried · 15 hydrogen bonds · protein-protein
- D–F · 771 Ų buried · 17 hydrogen bonds · protein-protein
- B–C · 770 Ų buried · 18 hydrogen bonds · protein-protein
- A–F · 768 Ų buried · 19 hydrogen bonds · protein-protein
- C–E · 766 Ų buried · 18 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 cofactor (pyridoxal phosphate Schiff base).
Compared structures
- 6H65 · Crystal structure of the branched-chain-amino-acid aminotransferase from Haliangium… · 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 D0LR31
- Elsewhere: RCSB PDB 6H65 · PDBe 6H65 · UniProt D0LR31
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