MolNFT v1 · #30031 · protein
The crystal structure of an acremonium strictum glucooligosaccharide oxidase reveals a novel flavinylation
1ZR6: “The crystal structure of an acremonium strictum glucooligosaccharide oxidase reveals a novel flavinylation”. X-ray diffraction, 3 ligands (FAD, NAG, ZN), 1 pocket (best druggability 0.82). MolNFT v1 #30031 on GenesisL1: 3D…
- PDB
- 1ZR6
- Type
- protein
- Length
- 479 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glucooligosaccharide oxidase
- EC
- 1.1.3.-
- UniProt
- Q6PW77
- Ligands
- FAD, NAG, ZN
- Pockets
- 1 · best druggability 0.82
Structure
x-ray diffraction · 1 distinct chain · 33% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glucooligosaccharide oxidase (EC 1.1.3.-) | protein | 479 | 33% helix, 22% strand | Q6PW77 |
Ligands and binding sites
- FAD · Flavin-adenine dinucleotide · ligand · chains A
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 2 copies · chains A
- ZN · Zinc ion · metal · 4 copies · chains A
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 | 533 | 0.82 | 0.88 | 73 | FAD |
Modifications
Observed in the structure: 2 cofactor, 2 glycan, 1 disulfide (flavinylation, N-glycosylation, disulfide).
Compared structures
- 1ZR6 · The crystal structure of an Acremonium strictum glucooligosaccharide oxidase reveals a… · the same entry in another collection · chain A against A, TM-score 1.00
- Q6PW77 · AlphaFold monomer V2.0 prediction for glucooligosaccharide oxidase (Q6PW77) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 Q6PW77
- Elsewhere: RCSB PDB 1ZR6 · PDBe 1ZR6 · UniProt Q6PW77
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