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Crystal structure of the catalytic domain of the beta-1,4- glycanase cex from cellulomonas fimi

Analyse Crystal structure of the catalytic domain of the beta-1,4- glycanase cex from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2EXO
Type: protein
Length: 312 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Exo-1,4-beta-D-glycanase
EC: 3.2.1.91
UniProt: P07986
Pockets: 1 · best druggability 0.38

Structure

x-ray diffraction · 1 distinct chain · 45% helix, 21% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Exo-1,4-beta-D-glycanase (EC 3.2.1.91)	protein	312	45% helix, 21% strand	P07986

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	95	0.38	0.76	19	empty

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

2EXO · Crystal structure of the catalytic domain of the beta-1,4-glycanase cex from cellulomonas… · the same entry in another collection · chain A against A, TM-score 1.00
P07986 · AlphaFold monomer V2.0 prediction for EXOGLUCANASE/XYLANASE (P07986) · a predicted model of the same protein · 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 P07986
Elsewhere: RCSB PDB 2EXO · PDBe 2EXO · UniProt P07986

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