Research workbench
Glycan labelling using engineered variants of galactose oxidase obtained by directed evolution
Analyse Glycan labelling using engineered variants of galactose oxidase obtained by… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2WQ8
- Type
- protein
- Length
- 639 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Galactose oxidase
- EC
- 1.1.3.9
- UniProt
- Q01745
- Ligands
- CU, CA
- Pockets
- 4 · best druggability 0.53
Structure
x-ray diffraction · 1 distinct chain · 4% helix, 42% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Galactose oxidase (EC 1.1.3.9) | protein | 639 | 4% helix, 42% strand | Q01745 |
Ligands and binding sites
- CU · Copper (II) ion · metal · chains A
- CA · Calcium ion · metal · chains A
- EDO · 1,2-ethanediol · additive · 9 copies · chains A
- GOL · Glycerol · additive · 3 copies · chains A
- ACY · Acetic acid · additive · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 59 | 0.53 | 0.88 | 22 | empty |
| 2 | 256 | 0.53 | 0.76 | 35 | empty |
| 3 | 187 | 0.46 | 0.74 | 34 | EDO, GOL |
| 4 | 57 | 0.29 | 0.74 | 21 | empty |
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 2WQ8 · Glycan labelling using engineered variants of galactose oxidase obtained by directed… · 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 Q01745
- Elsewhere: RCSB PDB 2WQ8 · PDBe 2WQ8 · UniProt Q01745
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