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A common protein fold and similar active site in two distinct families of beta-glycanases

Analyse A common protein fold and similar active site in two distinct families of… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1XYZ
Type: protein
Length: 640 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: 1,4-beta-D-xylan-xylanohydrolase
EC: 3.2.1.8
UniProt: P10478
Pockets: 3 · best druggability 0.73

Structure

x-ray diffraction · 1 distinct chain · 45% helix, 20% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	1,4-beta-D-xylan-xylanohydrolase (EC 3.2.1.8)	protein	320	45% helix, 20% strand	P10478

Pockets

3 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	1048	0.73	0.76	89	empty
2	74	0.36	0.77	19	empty
3	61	0.29	0.74	13	empty

Interfaces

1 interface between chains.

A–B · 443 Å² buried · 4 hydrogen bonds · protein-protein

Compared structures

1XYZ · A common protein fold and similar active site in two distinct families of beta-glycanases · the same entry in another collection · chain A against A, TM-score 1.00
P10478 · AlphaFold monomer V2.0 prediction for endo-1,4-beta-xylanase Z (P10478) · 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 P10478
Elsewhere: RCSB PDB 1XYZ · PDBe 1XYZ · UniProt P10478

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