Research workbench
Crystal structure of full-length catechol oxidase from aspergillus oryzae
Analyse Crystal structure of full-length catechol oxidase from aspergillus oryzae in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4J3P
- Type
- protein
- Length
- 371 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Catechol oxidase
- EC
- 1.10.3.1
- UniProt
- Q2UNF9
- Ligands
- NAG, BMA, MAN, CU, OXY, SO4
- Pockets
- 2 · best druggability 0.67
Structure
x-ray diffraction · 1 distinct chain · 38% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Catechol oxidase (EC 1.10.3.1) | protein | 371 | 38% helix, 12% strand | Q2UNF9 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 5 copies · chains A
- BMA · beta-D-mannopyranose · sugar
- MAN · alpha-D-mannopyranose · sugar · chains A
- CU · Copper (II) ion · metal · 2 copies · chains A
- OXY · Oxygen molecule · ion · chains A
- SO4 · Sulfate ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 222 | 0.67 | 0.84 | 38 | OXY |
| 2 | 60 | 0.38 | 0.80 | 17 | empty |
Modifications
Observed in the structure: 5 glycan, 3 disulfide (N-glycosylation, disulfide, O-glycosylation).
Compared structures
- 4J3P · Crystal structure of full-length catechol oxidase from Aspergillus oryzae · 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 Q2UNF9
- Elsewhere: RCSB PDB 4J3P · PDBe 4J3P · UniProt Q2UNF9
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