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The high-resolution crystal structure of tsxyla, intracellular xylanase from /thermoanaerobacterium saccharolyticum JW/SL-YS485/: the complex of the E251A mutant with xylobiose

Analyse The high-resolution crystal structure of tsxyla, intracellular xylanase from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3W27
Type: protein
Length: 324 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Glycoside hydrolase family 10
EC: 3.2.1.8
UniProt: I3VVC1
Ligands: XYS, XYP
Pockets: 1 · best druggability 0.41

Structure

x-ray diffraction · 1 distinct chain · 42% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Glycoside hydrolase family 10 (EC 3.2.1.8)	protein	324	42% helix, 18% strand	I3VVC1

Ligands and binding sites

XYS · alpha-D-xylopyranose · sugar · chains A
XYP · beta-D-xylopyranose · 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	63	0.41	0.80	18	XYS, XYP

Compared structures

3W27 · The high-resolution crystal structure of TsXylA, intracellular xylanase from… · 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 I3VVC1
Elsewhere: RCSB PDB 3W27 · PDBe 3W27 · UniProt I3VVC1

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