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Structural basis for the exocellulase activity of the cellobiohydrolase cbha from C. thermocellum

Analyse Structural basis for the exocellulase activity of the cellobiohydrolase cbha… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1RQ5
Type: protein
Length: 602 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cellobiohydrolase
EC: 3.2.1.91
UniProt: Q59325
Ligands: BGC, CA
Pockets: 3 · best druggability 0.72

Structure

x-ray diffraction · 1 distinct chain · 35% helix, 10% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cellobiohydrolase (EC 3.2.1.91)	protein	602	35% helix, 10% strand	Q59325

Ligands and binding sites

BGC · beta-D-glucopyranose · sugar · 4 copies · chains A
CA · Calcium ion · metal · 2 copies · chains A

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

Pockets

3 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	425	0.72	0.83	43	BGC
2	82	0.44	0.80	21	empty
3	60	0.35	0.78	19	empty

Compared structures

1RQ5 · Structural Basis for the Exocellulase Activity of the Cellobiohydrolase CbhA from C.… · 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 Q59325
Elsewhere: RCSB PDB 1RQ5 · PDBe 1RQ5 · UniProt Q59325

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