MolNFT v2 · #144321 · protein
Structural and biochemical characterization of a non-canonical biuret hydrolase (BiuH) from the cyanuric acid catabolism pathway of Rhizobium leguminasorum bv. viciae 3841
6AZN: “Structural and biochemical characterization of a non-canonical biuret hydrolase (BiuH) from the cyanuric acid…”. X-ray diffraction at 1.75, 1 ligand (PO4). MolNFT v2 #144321 on GenesisL1: 3D structure, binding sites and pockets in…
- PDB
- 6AZN
- Type
- protein
- Length
- 1,809 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.75
- Source
- Rhizobium leguminosarum bv. viciae (strain 3841)
- UniProt
- Q1M7F4
- Ligands
- PO4
Structure
x-ray diffraction · resolution 1.75 · 4 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C, D, F, G | — | protein | 226 | — | Q1M7F4 |
| B | — | protein | 223 | — | Q1M7F4 |
| H | — | protein | 229 | — | Q1M7F4 |
| I | — | protein | 227 | — | Q1M7F4 |
Ligands and binding sites
- PO4 · Phosphate ion · ion · 3 copies · chains A, B, F, G, H, I
- EDO · 1,2-ethanediol · additive · 4 copies · chains A, B, C, D, I, H
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6AZN · Structural and biochemical characterization of a non-canonical biuret hydrolase (biuh)… · 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 Q1M7F4
- Elsewhere: RCSB PDB 6AZN · PDBe 6AZN · UniProt Q1M7F4
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