Research workbench
Crystal structure of endo-beta-N-acetylglucosaminidase F3
Analyse Crystal structure of endo-beta-N-acetylglucosaminidase F3 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1EOK
- Type
- protein
- Length
- 282 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Endo-beta-N-acetylglucosaminidase F3
- EC
- 3.2.1.96
- UniProt
- P36913
- Ligands
- SO4
Structure
x-ray diffraction · 1 distinct chain · 38% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Endo-beta-N-acetylglucosaminidase F3 (EC 3.2.1.96) | protein | 282 | 38% helix, 15% strand | P36913 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 1EOK · Crystal structure of endo-beta-N-acetylglucosaminidase F3 · the same entry in another collection · chain A against A, TM-score 1.00
- P36913 · AlphaFold monomer V2.0 prediction for endo-beta-N- acetylglucosaminidase F3 (P36913) · 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 P36913
- Elsewhere: RCSB PDB 1EOK · PDBe 1EOK · UniProt P36913
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