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Crystal structure of recombinant alkali thermostable GH10 xylanase from bacillus sp. ng-27

Analyse Crystal structure of recombinant alkali thermostable GH10 xylanase from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4QCE
Type: protein
Length: 708 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Alkaline thermostable endoxylanase
EC: 3.2.1.8
UniProt: O30700
Ligands: MG, NA
Pockets: 2 · best druggability 0.73

Structure

x-ray diffraction · 1 distinct chain · 44% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Alkaline thermostable endoxylanase (EC 3.2.1.8)	protein	354	44% helix, 16% strand	O30700

Ligands and binding sites

MG · Magnesium ion · metal · 2 copies · chains A, B
NA · Sodium ion · metal · 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, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	859	0.73	0.78	82	empty
2	353	0.58	0.76	39	empty

Interfaces

1 interface between chains.

A–B · 362 Å² buried · 7 hydrogen bonds · protein-protein

Compared structures

4QCE · Crystal structure of recombinant alkali thermostable GH10 xylanase from Bacillus sp. NG-27 · 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 O30700
Elsewhere: RCSB PDB 4QCE · PDBe 4QCE · UniProt O30700

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