Research workbench
Crystal structure of GH20 exo beta-N-acetylglucosaminidase from vibrio harveyi in complex with N-acetylglucosamine
Analyse Crystal structure of GH20 exo beta-N-acetylglucosaminidase from vibrio harveyi… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6EZS
- Type
- protein
- Length
- 1,278 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- D9ISE0
- Ligands
- NAG
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | — | protein | 639 | — | D9ISE0 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 2 copies · chains A, B
- MLI · Malonate ion · additive · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6EZS · Crystal structure of GH20 Exo beta-N-Acetylglucosaminidase from Vibrio harveyi in complex… · 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 D9ISE0
- Elsewhere: RCSB PDB 6EZS · PDBe 6EZS · UniProt D9ISE0
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