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E292Q mutant of exo-B-(1,3)-glucanase from candida albicans in complex with two separately bound glucopyranoside units at 1.8 a

Analyse E292Q mutant of exo-B-(1,3)-glucanase from candida albicans in complex with two… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2PC8
Type: protein
Length: 394 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Hypothetical protein XOG1
EC: 3.2.1.58
UniProt: Q5AIZ3
Ligands: BGC
Pockets: 2 · best druggability 0.64

Structure

x-ray diffraction · 1 distinct chain · 39% helix, 13% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Hypothetical protein XOG1 (EC 3.2.1.58)	protein	394	39% helix, 13% strand	Q5AIZ3

Ligands and binding sites

BGC · beta-D-glucopyranose · sugar · 2 copies · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	337	0.64	0.79	41	BGC
2	85	0.40	0.78	23	empty

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

2PC8 · E292Q mutant of EXO-B-(1,3)-Glucanase from Candida Albicans in complex with two… · 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 Q5AIZ3
Elsewhere: RCSB PDB 2PC8 · PDBe 2PC8 · UniProt Q5AIZ3

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