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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: 1UT9
Type: protein
Length: 605 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cellulose 1,4-beta-cellobiosidase
EC: 3.2.1.4
Pockets: 2 · best druggability 0.71

Structure

x-ray diffraction · 1 distinct chain · 36% helix, 14% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cellulose 1,4-beta-cellobiosidase (EC 3.2.1.4)	protein	605	36% helix, 14% strand	—

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	389	0.71	0.83	43	empty
2	78	0.47	0.82	22	empty

Compared structures

1UT9 · 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

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Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Elsewhere: RCSB PDB 1UT9 · PDBe 1UT9

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