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Crystal structure of the catalytic nucleophile mutant of VVEG16 in complex with cellotetraose

Analyse Crystal structure of the catalytic nucleophile mutant of VVEG16 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: 5DZE
Type: protein
Length: 199 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Endo-glucanase
UniProt: F6I323
Ligands: BGC, GLC
Pockets: 1 · best druggability 0.44

Structure

x-ray diffraction · 1 distinct chain · 5% helix, 52% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Endo-glucanase	protein	199	5% helix, 52% strand	F6I323

Ligands and binding sites

BGC · beta-D-glucopyranose · sugar · 4 copies · chains A
GLC · alpha-D-glucopyranose · 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	113	0.44	0.78	22	GLC, BGC

Compared structures

5DZE · Crystal Structure of the catalytic nucleophile mutant of VvEG16 in complex with… · 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 F6I323
Elsewhere: RCSB PDB 5DZE · PDBe 5DZE · UniProt F6I323

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