MolNFT v1 · #32603 · protein
How family 26 glycoside hydrolases orchestrate catalysis on different polysaccharides. structure and activity of a clostridium thermocellum lichenase, CTLIC26A
2BVD · Endoglucanase H: “How family 26 glycoside hydrolases orchestrate catalysis on different polysaccharides. structure and activity…”. X-ray diffraction, 1 ligand (ISX), 1 pocket (best druggability 0.48). MolNFT v1 #32603 on GenesisL1…
- PDB
- 2BVD
- Type
- protein
- Length
- 276 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Endoglucanase H
- EC
- 3.2.1.4
- UniProt
- P16218
- Ligands
- ISX
- Pockets
- 1 · best druggability 0.48
Structure
x-ray diffraction · 1 distinct chain · 37% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Endoglucanase H (EC 3.2.1.4) | protein | 276 | 37% helix, 20% strand | P16218 |
Ligands and binding sites
- ISX · (3R,4R,5R)-4-hydroxy-5-(hydroxymethyl)piperidin-3-yl beta-D-glucopyranoside · ligand · 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 | 162 | 0.48 | 0.76 | 29 | ISX |
Compared structures
- 2BVD · HOW FAMILY 26 GLYCOSIDE HYDROLASES ORCHESTRATE CATALYSIS ON DIFFERENT POLYSACCHARIDES.… · the same entry in another collection · chain A against A, TM-score 1.00
- P16218 · AlphaFold monomer V2.0 prediction for endoglucanase H (P16218) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 P16218
- Elsewhere: RCSB PDB 2BVD · PDBe 2BVD · UniProt P16218
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