MolNFT v2 · #171281 · protein
Biuret Hydrolase (BiuH) from Rhodococcus sp. Mel C169S bound with biuret
6XJM: “Biuret Hydrolase (BiuH) from Rhodococcus sp. Mel C169S bound with biuret”. X-ray diffraction at 2.05, 1 ligand (C5J). MolNFT v2 #171281 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6XJM
- Type
- protein
- Length
- 911 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.05
- Source
- Rhodococcus sp. Mel
- UniProt
- H8ZKV9
- Ligands
- C5J
Structure
x-ray diffraction · resolution 2.05 · 4 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 226 | — | H8ZKV9 |
| B | — | protein | 227 | — | H8ZKV9 |
| C | — | protein | 228 | — | H8ZKV9 |
| D | — | protein | 230 | — | H8ZKV9 |
Ligands and binding sites
- C5J · dicarbonimidic diamide · ligand · 4 copies · chains A, D, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6XJM · Biuret hydrolase (biuh) from rhodococcus sp. mel C169S bound with biuret · 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 H8ZKV9
- Elsewhere: RCSB PDB 6XJM · PDBe 6XJM · UniProt H8ZKV9
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