MolNFT v1 · #111846 · protein
Crystal structure of 2-hydroxybiphenyl 3-monooxygenase W225Y from pseudomonas azelaica
4Z2T · 2-hydroxybiphenyl-3-monooxygenase: “Crystal structure of 2-hydroxybiphenyl 3-monooxygenase W225Y from pseudomonas azelaica”. X-ray diffraction, 1 ligand (FAD), 10 pockets (best druggability 0.80). MolNFT v1 #111846 on GenesisL1: 3D…
- PDB
- 4Z2T
- Type
- protein
- Length
- 1,123 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 2-hydroxybiphenyl-3-monooxygenase
- EC
- 1.14.13.44
- UniProt
- O06647
- Ligands
- FAD
- Pockets
- 10 · best druggability 0.80
Structure
x-ray diffraction · 2 distinct chains · 36% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 2-hydroxybiphenyl-3-monooxygenase (EC 1.14.13.44) | protein | 559 | 36% helix, 24% strand | O06647 |
| B | 2-hydroxybiphenyl-3-monooxygenase (EC 1.14.13.44) | protein | 564 | 37% 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
10 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1039 | 0.80 | 0.82 | 106 | empty |
| 2 | 993 | 0.80 | 0.81 | 95 | FAD |
| 3 | 927 | 0.79 | 0.81 | 80 | FAD |
| 4 | 194 | 0.52 | 0.77 | 37 | empty |
| 5 | 85 | 0.44 | 0.79 | 18 | empty |
Interfaces
1 interface between chains.
- A–B · 457 Ų buried · 8 hydrogen bonds · protein-protein
Compared structures
- 4Z2T · Crystal Structure of 2-hydroxybiphenyl 3-monooxygenase W225Y 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 4Z2T · PDBe 4Z2T · UniProt O06647
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