MolNFT v1 · #60529 · protein

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

3CUH · Exo-beta-1,4-glucanase: “Cellulomonas fimi XYLANASE/CELLULASE cex (cf XYN10A) in complex with cellotriose-like isofagomine”. X-ray diffraction, 1 ligand (G2I), 1 pocket (best druggability 0.43). MolNFT v1 #60529 on GenesisL1: 3D…

PDB: 3CUH
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: G2I
Pockets: 1 · best druggability 0.43

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

G2I · (3R,4R,5R)-3-hydroxy-5-(hydroxymethyl)piperidin-4-yl 4-O-beta-D-glucopyranosyl-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	150	0.43	0.75	21	G2I

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

3CUH · Cellulomonas fimi Xylanase/Cellulase Cex (Cf Xyn10A) in complex with cellotriose-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 3CUH · PDBe 3CUH · UniProt Q59277

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