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Thermobifida fusca cellobiohydrolase CEL6B catalytic mutant D226A- S232A cocrystallized with cellobiose

Analyse Thermobifida fusca cellobiohydrolase CEL6B catalytic mutant D226A- S232A… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4AVN
Type: protein
Length: 420 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cellobiohydrolase. glycosyl hydrolase family 6
EC: 3.2.1.91
UniProt: Q47SA9
Ligands: BGC, CA
Pockets: 2 · best druggability 0.78

Structure

x-ray diffraction · 1 distinct chain · 32% helix, 13% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cellobiohydrolase. glycosyl hydrolase family 6 (EC 3.2.1.91)	protein	420	32% helix, 13% strand	Q47SA9

Ligands and binding sites

BGC · beta-D-glucopyranose · sugar · 5 copies · chains A
CA · Calcium ion · metal · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	461	0.78	0.86	55	BGC
2	66	0.37	0.78	14	empty

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

4AVN · Thermobifida fusca cellobiohydrolase Cel6B catalytic mutant D226A- S232A cocrystallized… · 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 Q47SA9
Elsewhere: RCSB PDB 4AVN · PDBe 4AVN · UniProt Q47SA9

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