MolNFT v1 · #85043 · protein

Structure of the catalytic core domain of the cellobiohydrolase, CEL6A, from chaetomium thermophilum

4A05 · Cellobiohydrolase family 6: “Structure of the catalytic core domain of the cellobiohydrolase, CEL6A, from chaetomium thermophilum”. X-ray diffraction, 3 ligands (BGC, NAG, LI), 1 pocket (best druggability 0.72). MolNFT v1 #85043 on…

PDB: 4A05
Type: protein
Length: 360 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cellobiohydrolase family 6
EC: 3.2.1.91
UniProt: Q4JQF8
Ligands: BGC, NAG, LI
Pockets: 1 · best druggability 0.72

Structure

x-ray diffraction · 1 distinct chain · 38% helix, 13% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cellobiohydrolase family 6 (EC 3.2.1.91)	protein	360	38% helix, 13% strand	Q4JQF8

Ligands and binding sites

BGC · beta-D-glucopyranose · sugar · 6 copies · chains A
NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 2 copies · chains A
LI · Lithium ion · metal · 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	414	0.72	0.83	56	BGC, LI

Modifications

Observed in the structure: 2 disulfide, 1 glycan (disulfide, N-glycosylation).

Compared structures

4A05 · Structure of the catalytic core domain of the cellobiohydrolase, Cel6A, from Chaetomium… · 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 Q4JQF8
Elsewhere: RCSB PDB 4A05 · PDBe 4A05 · UniProt Q4JQF8

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