MolNFT v2 · #151818 · protein
Crystal structure of the branched-chain-amino-acid aminotransferase from Haliangium ochraceum
6H65: “Crystal structure of the branched-chain-amino-acid aminotransferase from Haliangium ochraceum”. X-ray diffraction at 2.35, 1 ligand (PLP). MolNFT v2 #151818 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6H65
- Type
- protein
- Length
- 1,837 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.35
- UniProt
- D0LR31
- Ligands
- PLP
Structure
x-ray diffraction · resolution 2.35 · 5 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, D | — | protein | 305 | — | D0LR31 |
| B | — | protein | 306 | — | D0LR31 |
| C | — | protein | 308 | — | D0LR31 |
| E | — | protein | 307 | — | D0LR31 |
| F | — | protein | 306 | — | 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.
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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