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Catalysis and specificity in enzymatic glycoside hydrolases: a 2,5B conformation for the glycosyl-enzyme intermidiate revealed by the structure of the bacillus agaradhaerens family 11 xylanase

Analyse Catalysis and specificity in enzymatic glycoside hydrolases: a 2,5B… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1QH7
Type: protein
Length: 414 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Xylanase
EC: 3.2.1.8
UniProt: Q7SIE3
Ligands: XYP
Pockets: 2 · best druggability 0.51

Structure

x-ray diffraction · 1 distinct chain · 7% helix, 63% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Xylanase (EC 3.2.1.8)	protein	207	7% helix, 63% strand	Q7SIE3

Ligands and binding sites

XYP · beta-D-xylopyranose · sugar · 2 copies · chains A, B

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	164	0.51	0.78	29	XYP
2	75	0.47	0.83	20	XYP

Modifications

Observed in the structure: 2 modified (cyclization).

Compared structures

1QH7 · Catalysis and specificity in enzymatic glycoside hydrolases: a 2,5B conformation for the… · 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 Q7SIE3
Elsewhere: RCSB PDB 1QH7 · PDBe 1QH7 · UniProt Q7SIE3

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