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The wild type crystal structure of B-1,4-xylanase (XYNAS9) from streptomyces sp. 9

Analyse The wild type crystal structure of B-1,4-xylanase (XYNAS9) from streptomyces… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3WUB
Type: protein
Length: 313 residues
Chains: 1
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: B4XVN1
Ligands: ZN
Pockets: 1 · best druggability 0.45

Structure

x-ray diffraction · 1 distinct chain · 44% helix, 20% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Endo-1,4-beta-xylanase a (EC 3.2.1.8)	protein	313	44% helix, 20% strand	B4XVN1

Ligands and binding sites

ZN · Zinc ion · metal · 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	132	0.45	0.77	25	empty

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

3WUB · The wild type crystal structure of b-1,4-Xylanase (XynAS9) from Streptomyces sp. 9 · the same entry in another collection · chain A against A, TM-score 1.00
B4XVN1 · AlphaFold monomer V2.0 prediction for endo-1,4-beta-xylanase a (B4XVN1) · a predicted model of the same protein · chain A against A, TM-score 1.00

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Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt B4XVN1
Elsewhere: RCSB PDB 3WUB · PDBe 3WUB · UniProt B4XVN1

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