Research workbench
High resolution crystal structure of CBM32 from a N-acetyl-beta- hexosaminidase in complex with lacnac
Analyse High resolution crystal structure of CBM32 from a N-acetyl-beta- hexosaminidase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2J1E
- Type
- protein
- Length
- 142 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hyaluronidase
- UniProt
- Q8XL08
- Ligands
- NDG, GAL, CA
Structure
x-ray diffraction · 1 distinct chain · 4% helix, 51% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Hyaluronidase | protein | 142 | 4% helix, 51% strand | Q8XL08 |
Ligands and binding sites
- NDG · 2-acetamido-2-deoxy-alpha-D-glucopyranose · sugar · chains A
- GAL · beta-D-galactopyranose · sugar · chains A
- CA · Calcium ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 2J1E · High Resolution Crystal Structure of CBM32 from a N-acetyl-beta- hexosaminidase in… · the same entry in another collection · chain A against A, TM-score 1.00
- Q8XL08 · AlphaFold monomer V2.0 prediction for O-glcnacase nagj (Q8XL08) · a predicted model of the same protein · chain A against A, TM-score 0.96
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 Q8XL08
- Elsewhere: RCSB PDB 2J1E · PDBe 2J1E · UniProt Q8XL08
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