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Crystal Structure of 2-hydroxybiphenyl 3-monooxygenase M321A from Pseudomonas azelaica
Analyse Crystal Structure of 2-hydroxybiphenyl 3-monooxygenase M321A from Pseudomonas… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6EM0
- Type
- protein
- Length
- 1,131 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.78
- Source
- Pseudomonas nitroreducens
- Molecule
- 2-hydroxybiphenyl-3-monooxygenase
- UniProt
- O06647
- Ligands
- FAD
- Pockets
- 15 · best druggability 0.81
Structure
x-ray diffraction · resolution 2.78 · 2 distinct chains · 35% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 2-hydroxybiphenyl-3-monooxygenase | protein | 566 | 36% helix, 24% strand | O06647 |
| B | 2-hydroxybiphenyl-3-monooxygenase | protein | 565 | 34% helix, 24% strand | O06647 |
Ligands and binding sites
- FAD · Flavin-adenine dinucleotide · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
15 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1041 | 0.81 | 0.82 | 92 | FAD |
| 2 | 940 | 0.80 | 0.82 | 100 | empty |
| 3 | 985 | 0.80 | 0.81 | 97 | FAD |
| 4 | 59 | 0.66 | 0.95 | 19 | empty |
| 5 | 59 | 0.62 | 0.92 | 19 | empty |
Interfaces
1 interface between chains.
- A–B · 482 Ų buried · 6 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 cofactor (flavinylation).
Compared structures
- 6EM0 · Crystal structure of 2-hydroxybiphenyl 3-monooxygenase M321A from pseudomonas azelaica · 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 O06647
- Elsewhere: RCSB PDB 6EM0 · PDBe 6EM0 · UniProt O06647
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