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Crystal structure of a thermophilic xylanase a from bacillus subtilis 1A1 quadruple mutant Q7H/G13R/S22P/S179C

Analyse Crystal structure of a thermophilic xylanase a from bacillus subtilis 1A1… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5K9Y
Type: protein
Length: 370 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Endo-1,4-beta-xylanase a
EC: 3.2.1.8
UniProt: P18429
Pockets: 1 · best druggability 0.76

Structure

x-ray diffraction · 1 distinct chain · 5% helix, 59% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Endo-1,4-beta-xylanase a (EC 3.2.1.8)	protein	185	5% helix, 59% strand	P18429

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	547	0.76	0.83	60	empty

Interfaces

1 interface between chains.

A–B · 816 Å² buried · 13 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 modified (oxidation).

Compared structures

5K9Y · Crystal structure of a thermophilic xylanase A from Bacillus subtilis 1A1 quadruple… · the same entry in another collection · chain A against A, TM-score 1.00
P18429 · AlphaFold monomer V2.0 prediction for endo-1,4-beta-xylanase a (P18429) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 P18429
Elsewhere: RCSB PDB 5K9Y · PDBe 5K9Y · UniProt P18429

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