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3D structure of a thermophilic family GH11 xylanase from thermobifida fusca

Analyse 3D structure of a thermophilic family GH11 xylanase from thermobifida fusca in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3ZSE
Type: protein
Length: 187 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Endo-1,4-beta-xylanase
EC: 3.2.1.8
UniProt: Q5RZ98
Ligands: X2F, XYP
Pockets: 1 · best druggability 0.49

Structure

x-ray diffraction · 1 distinct chain · 5% helix, 61% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Endo-1,4-beta-xylanase (EC 3.2.1.8)	protein	187	5% helix, 61% strand	Q5RZ98

Ligands and binding sites

X2F · 2-deoxy-2-fluoro-alpha-D-xylopyranose · ligand · chains A
XYP · beta-D-xylopyranose · sugar · chains A
EDO · 1,2-ethanediol · additive · 5 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, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	121	0.49	0.80	28	X2F, XYP, EDO

Modifications

Observed in the structure: 1 covalent (covalent ligand).

Compared structures

3ZSE · 3D Structure of a thermophilic family GH11 xylanase from Thermobifida fusca · 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 Q5RZ98
Elsewhere: RCSB PDB 3ZSE · PDBe 3ZSE · UniProt Q5RZ98

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