MolNFT v1 · #60531 · protein

Cellulomonas fimi XYLANASE/CELLULASE cex (cf XYN10A) in complex with sulfur substituted beta-1,4 xylopentaose.

3CUJ · Exo-beta-1,4-glucanase: “Cellulomonas fimi XYLANASE/CELLULASE cex (cf XYN10A) in complex with sulfur substituted beta-1,4 xylopentaose.”. X-ray diffraction, 2 ligands (TWY, XYP), 1 pocket (best druggability 0.39). MolNFT v1 #60531…

PDB: 3CUJ
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: TWY, XYP
Pockets: 1 · best druggability 0.39

Structure

x-ray diffraction · 1 distinct chain · 44% helix, 21% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Exo-beta-1,4-glucanase (EC 3.2.1.91)	protein	314	44% helix, 21% strand	Q59277

Ligands and binding sites

TWY · 4-thio-beta-D-xylopyranose · ligand · 4 copies · chains A
XYP · beta-D-xylopyranose · sugar · 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	98	0.39	0.76	19	TWY

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

3CUJ · Cellulomonas fimi Xylanase/Cellulase Cex (Cf Xyn10A) in complex with sulfur substituted… · 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 3CUJ · PDBe 3CUJ · UniProt Q59277

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