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How family 26 glycoside hydrolases orchestrate catalysis on different polysaccharides. structure and activity of a clostridium thermocellum lichenase, CTLIC26A

Analyse How family 26 glycoside hydrolases orchestrate catalysis on different… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2BV9
Type: protein
Length: 284 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
Pockets: 3 · best druggability 0.42

Structure

x-ray diffraction · 1 distinct chain · 36% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Endoglucanase H (EC 3.2.1.4)	protein	284	36% helix, 19% strand	P16218

Pockets

3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	162	0.42	0.73	22	empty
2	56	0.30	0.75	16	empty
3	51	0.28	0.75	13	empty

Compared structures

2BV9 · 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 0.97

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 2BV9 · PDBe 2BV9 · UniProt P16218

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