Research workbench
Structure of endoglucanase V cellobiose complex
Analyse Structure of endoglucanase V cellobiose complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3ENG
- Type
- protein
- Length
- 213 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Endoglucanase V cellobiose complex
- EC
- 3.2.1.4
- UniProt
- P43316
- Ligands
- BGC
- Pockets
- 1 · best druggability 0.42
Structure
x-ray diffraction · 1 distinct chain · 18% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Endoglucanase V cellobiose complex (EC 3.2.1.4) | protein | 213 | 18% helix, 27% strand | P43316 |
Ligands and binding sites
- BGC · beta-D-glucopyranose · sugar · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 151 | 0.42 | 0.75 | 30 | BGC |
Modifications
Observed in the structure: 7 disulfide (disulfide).
Compared structures
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 P43316
- Elsewhere: RCSB PDB 3ENG · PDBe 3ENG · UniProt P43316
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