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CCCEL6A catalytic domain complexed with P-nitrophenyl beta-D- cellotrioside

Analyse CCCEL6A catalytic domain complexed with P-nitrophenyl beta-D- cellotrioside in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3VOI
Type: protein
Length: 360 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cellobiohydrolase
EC: 3.2.1.91
UniProt: B7X9Z0
Ligands: RCB, MG
Pockets: 1 · best druggability 0.74

Structure

x-ray diffraction · 1 distinct chain · 41% helix, 12% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cellobiohydrolase (EC 3.2.1.91)	protein	360	41% helix, 12% strand	B7X9Z0

Ligands and binding sites

RCB · 4-nitrophenyl beta-D-glucopyranosyl-(1->4)-beta-D-glucopyranosyl-(1->4)-beta-D-glucopyranoside · ligand · chains A
MG · Magnesium ion · metal · 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	305	0.74	0.86	50	MG, RCB

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

3VOI · CcCel6A catalytic domain complexed with p-nitrophenyl beta-D-cellotrioside · 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 B7X9Z0
Elsewhere: RCSB PDB 3VOI · PDBe 3VOI · UniProt B7X9Z0

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