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Crystal structure of endo-beta-N-acetylglucosaminidase F1, an ALPHA(SLASH)BETA-barrel enzyme adapted for a complex substrate
Analyse Crystal structure of endo-beta-N-acetylglucosaminidase F1, an… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2EBN
- Type
- protein
- Length
- 285 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Endo-beta-N-acetylglucosaminidase F1
- EC
- 3.2.1.96
- UniProt
- P36911
- Ligands
- ZN
Structure
x-ray diffraction · 1 distinct chain · 32% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Endo-beta-N-acetylglucosaminidase F1 (EC 3.2.1.96) | protein | 285 | 32% helix, 25% strand | P36911 |
Ligands and binding sites
- ZN · Zinc ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 2EBN · Crystal structure of endo-beta-N-acetylglucosaminidase F1, an ALPHA(SLASH)BETA-barrel… · the same entry in another collection · chain A against A, TM-score 1.00
- P36911 · AlphaFold monomer V2.0 prediction for endo-beta-N- acetylglucosaminidase F1 (P36911) · 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 P36911
- Elsewhere: RCSB PDB 2EBN · PDBe 2EBN · UniProt P36911
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