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Xylanase XYN10B mutant (E262S) from cellvibrio mixtus in complex with arabinofuranose alpha 1,3 linked to xylotriose

Analyse Xylanase XYN10B mutant (E262S) from cellvibrio mixtus 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: 1UR2
Type: protein
Length: 351 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Endoxylanase
EC: 3.2.1.8
UniProt: O68541
Ligands: XYP, XYS, AHR, MG, CL
Pockets: 1 · best druggability 0.60

Structure

x-ray diffraction · 1 distinct chain · 43% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Endoxylanase (EC 3.2.1.8)	protein	351	43% helix, 18% strand	O68541

Ligands and binding sites

XYP · beta-D-xylopyranose · sugar · 5 copies · chains A
XYS · alpha-D-xylopyranose · sugar · chains A
AHR · alpha-L-arabinofuranose · sugar · chains A
MG · Magnesium ion · metal · chains A
CL · Chloride ion · ion · 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	301	0.60	0.78	37	XYP, XYS

Compared structures

1UR2 · Xylanase Xyn10B mutant (E262S) from Cellvibrio mixtus in complex with arabinofuranose… · 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 O68541
Elsewhere: RCSB PDB 1UR2 · PDBe 1UR2 · UniProt O68541

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