Research workbench
1.78 ångström resolution crystal structure of quercetin 2,3- dioxygenase from acinetobacter baumannii
Analyse 1.78 ångström resolution crystal structure of quercetin 2,3- dioxygenase from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6D0G
- Type
- protein
- Length
- 299 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Pirin family protein
- EC
- 1.13.11.24
- UniProt
- V5VHS3
- Ligands
- MN, BR
- Pockets
- 1 · best druggability 0.66
Structure
x-ray diffraction · 1 distinct chain · 7% helix, 50% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Pirin family protein (EC 1.13.11.24) | protein | 299 | 7% helix, 50% strand | V5VHS3 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 279 | 0.66 | 0.82 | 42 | MN |
Modifications
Observed in the structure: 11 modified (engineered).
Compared structures
- 6D0G · 1.78 Angstrom Resolution Crystal Structure of Quercetin 2,3-dioxygenase from… · 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 V5VHS3
- Elsewhere: RCSB PDB 6D0G · PDBe 6D0G · UniProt V5VHS3
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