MolNFT v1 · #129667 · protein
Crystal structure of aspergillus oryzae catechol oxidase in deoxy-form
5OR4: “Crystal structure of aspergillus oryzae catechol oxidase in deoxy-form”. X-ray diffraction, 4 ligands (NAG, BMA, MAN). MolNFT v1 #129667 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5OR4
- Type
- protein
- Length
- 1,483 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q2UNF9
- Ligands
- NAG, BMA, MAN, CU
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, D | — | protein | 371 | — | Q2UNF9 |
| C | — | protein | 370 | — | Q2UNF9 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 19 copies · chains A, B, C, D
- BMA · beta-D-mannopyranose · sugar · 3 copies · chains D, C, B
- MAN · alpha-D-mannopyranose · sugar · 3 copies · chains A, B, D
- CU · Copper (II) ion · metal · 8 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5OR4 · Crystal structure of Aspergillus oryzae catechol oxidase in deoxy-form · 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 5OR4 · PDBe 5OR4 · UniProt Q2UNF9
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