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Cellulomonas fimi XYLANASE/CELLULASE cex (cf XYN10A) in complex with cellotetraose-like isofagomine

Analyse Cellulomonas fimi XYLANASE/CELLULASE cex (cf XYN10A) in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3CUG
Type: protein
Length: 314 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Exo-beta-1,4-glucanase
EC: 3.2.1.91
UniProt: Q59277
Ligands: G3I
Pockets: 1 · best druggability 0.41

Structure

x-ray diffraction · 1 distinct chain · 44% helix, 20% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Exo-beta-1,4-glucanase (EC 3.2.1.91)	protein	314	44% helix, 20% strand	Q59277

Ligands and binding sites

G3I · (3R,4R,5R)-3-hydroxy-5-(hydroxymethyl)piperidin-4-yl beta-D-glucopyranosyl-(1->4)-beta-D-glucopyranosyl-(1->4)-beta-D-glucopyranoside · ligand · 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, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	129	0.41	0.75	19	G3I

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

3CUG · Cellulomonas fimi Xylanase/Cellulase Cex (Cf Xyn10A) in complex with cellotetraose-like… · 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 Q59277
Elsewhere: RCSB PDB 3CUG · PDBe 3CUG · UniProt Q59277

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