› 4pmx

X-ray diffraction
1.3Å resolution

Crystal structure of GH10 endo-b-1,4-xylanase (XynB) from Xanthomonas axonopodis pv citri in the native form

Released:
DOI: 10.2210/pdb4pmx/pdb
PDB entry 4pmx coloured by chain, front view.
PDB entry 4pmx coloured by chain, side view.
PDB entry 4pmx coloured by chain, top view.
Source organism: Xanthomonas citri pv. citri str. 306
Primary publication:
Molecular mechanisms associated with xylan degradation by Xanthomonas plant pathogens.
Santos CR, Hoffmam ZB, de Matos Martins VP, Zanphorlin LM, de Paula Assis LH, Honorato RV, Lopes de Oliveira PS, Ruller R, Murakami MT
J Biol Chem 289 32186-32200 (2014)
PMID: 25266726

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-241392 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Xylanase Chain: A
Molecule details ›
Chain: A
Length: 306 amino acids
Theoretical weight: 34.43 KDa
Source organism: Xanthomonas citri pv. citri str. 306
Expression system: Escherichia coli BL21(DE3)
Structure domains: Glycosidases

Ligands and Environments

1 bound ligand:
Ligand CA 1 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: LNLS BEAMLINE W01B-MX2
Spacegroup: P212121
Unit cell:
a: 49.463Å b: 71.834Å c: 83.839Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.133 0.132 0.174
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

2 review citations

A mini review of xylanolytic enzymes with regards to their synergistic interactions during hetero-xylan degradation.
Malgas et al. (2019)
1 more

3 mentions without citation

Molecular mechanisms associated with xylan degradation by Xanthomonas plant pathogens.
Santos et al. (2014)
2 more