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Structure of hyperthermophilic family 12 endocellulase from pyrococcus furiosus in complex with gluco-oligosaccharide

Analyse Structure of hyperthermophilic family 12 endocellulase from pyrococcus furiosus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3WQ0
Type: protein
Length: 270 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Endoglucanase a
EC: 3.2.1.4
UniProt: Q9V2T0
Ligands: BGC, CA
Pockets: 1 · best druggability 0.62

Structure

x-ray diffraction · 1 distinct chain · 6% helix, 55% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Endoglucanase a (EC 3.2.1.4)	protein	270	6% helix, 55% strand	Q9V2T0

Ligands and binding sites

BGC · beta-D-glucopyranose · sugar · 4 copies · chains A
CA · Calcium ion · metal · 2 copies · chains A
GOL · Glycerol · additive · 3 copies · chains A
NHE · 2-[N-cyclohexylamino]ethane sulfonic acid · additive · 2 copies · 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	289	0.62	0.79	37	BGC, GOL

Compared structures

3WQ0 · Structure of hyperthermophilic family 12 endocellulase from Pyrococcus furiosus in… · 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 Q9V2T0
Elsewhere: RCSB PDB 3WQ0 · PDBe 3WQ0 · UniProt Q9V2T0

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