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Crystal structure of an endo-beta-1,4-xylanase (glycoside hydrolase family 10/GH10) enzyme from trichoderma reesei

Analyse Crystal structure of an endo-beta-1,4-xylanase (glycoside hydrolase family… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4XV0
Type: protein
Length: 302 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Beta-xylanase
EC: 3.2.1.8
UniProt: G0RA32
Ligands: SO4, CL

Structure

x-ray diffraction · 1 distinct chain · 45% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Beta-xylanase (EC 3.2.1.8)	protein	302	45% helix, 19% strand	G0RA32

Ligands and binding sites

SO4 · Sulfate ion · ion · 5 copies · chains A
CL · Chloride ion · ion · 4 copies · chains A
GOL · Glycerol · additive · 2 copies · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Modifications

Observed in the structure: 1 disulfide, 1 modified (disulfide, cyclization).

Compared structures

4XV0 · Crystal structure of an endo-beta-1,4-xylanase (glycoside hydrolase family 10/GH10)… · the same entry in another collection · chain A against A, TM-score 1.00
G0RA32 · AlphaFold monomer V2.0 prediction for endo-1,4-beta-xylanase 3 (G0RA32) · 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 G0RA32
Elsewhere: RCSB PDB 4XV0 · PDBe 4XV0 · UniProt G0RA32

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