MolNFT v1 · #124208 · protein
Xylooligosaccharide oxidase from myceliophthora thermophila C1
5K8E · FAD linked oxidase-like protein: “Xylooligosaccharide oxidase from myceliophthora thermophila C1”. X-ray diffraction, 2 ligands (FAD, NAG), 1 pocket (best druggability 0.82). MolNFT v1 #124208 on GenesisL1: 3D structure, binding…
- PDB
- 5K8E
- Type
- protein
- Length
- 473 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- FAD linked oxidase-like protein
- EC
- 1.1.3.-
- UniProt
- G2QG48
- Ligands
- FAD, NAG
- Pockets
- 1 · best druggability 0.82
Structure
x-ray diffraction · 1 distinct chain · 35% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | FAD linked oxidase-like protein (EC 1.1.3.-) | protein | 473 | 35% helix, 22% strand | G2QG48 |
Ligands and binding sites
- FAD · Flavin-adenine dinucleotide · ligand · chains A
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 7 copies · chains A
- GOL · Glycerol · additive · 3 copies · chains A
- MES · 2-(N-morpholino)-ethanesulfonic acid · additive · 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 | 565 | 0.82 | 0.87 | 75 | FAD, MES |
Modifications
Observed in the structure: 5 glycan, 2 cofactor, 1 disulfide (N-glycosylation, flavinylation, disulfide).
Compared structures
- 5K8E · Xylooligosaccharide oxidase from Myceliophthora thermophila C1 · the same entry in another collection · chain A against A, TM-score 1.00
- G2QG48 · AlphaFold monomer V2.0 prediction for xylooligosaccharide oxidase (G2QG48) · a predicted model of the same protein · 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 G2QG48
- Elsewhere: RCSB PDB 5K8E · PDBe 5K8E · UniProt G2QG48
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