Research workbench
Structural and biochemical characterization of a non-canonical biuret hydrolase (biuh) from the cyanuric acid catabolism pathway of rhizobium leguminasorum bv. viciae 3841
Analyse Structural and biochemical characterization of a non-canonical biuret hydrolase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6AZO
- Type
- protein
- Length
- 921 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Putative amidase
- UniProt
- Q1M7F4
- Ligands
- CL
- Pockets
- 6 · best druggability 0.86
Structure
x-ray diffraction · 2 distinct chains · 38% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, D | Putative amidase | protein | 230 | 37% helix, 22% strand | Q1M7F4 |
| C | Putative amidase | protein | 231 | 38% helix, 22% strand | Q1M7F4 |
Ligands and binding sites
- CL · Chloride ion · ion · 2 copies · chains C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 498 | 0.86 | 0.93 | 45 | empty |
| 2 | 324 | 0.70 | 0.84 | 38 | empty |
| 3 | 129 | 0.61 | 0.86 | 24 | empty |
| 4 | 345 | 0.60 | 0.77 | 37 | empty |
| 5 | 362 | 0.59 | 0.76 | 36 | empty |
Interfaces
6 interfaces between chains.
- B–C · 2063 Ų buried · 33 hydrogen bonds · protein-protein
- A–D · 2059 Ų buried · 37 hydrogen bonds · protein-protein
- B–D · 774 Ų buried · 10 hydrogen bonds · protein-protein
- A–C · 772 Ų buried · 10 hydrogen bonds · protein-protein
- A–B · 298 Ų buried · 2 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 24 modified (engineered).
Compared structures
- 6AZO · 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 6AZO · PDBe 6AZO · UniProt Q1M7F4
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