› 2d23

X-ray diffraction
1.95Å resolution

Crystal structure of EP complex of catalytic-site mutant xylanase from Streptomyces olivaceoviridis E-86

Released:
DOI: 10.2210/pdb2d23/pdb
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PDB entry 2d23 coloured by chain, front view.
PDB entry 2d23 coloured by chain, side view.
PDB entry 2d23 coloured by chain, top view.
Source organism: Streptomyces olivaceoviridis
Primary publication:
Crystallographic snapshots of an entire reaction cycle for a retaining xylanase from Streptomyces olivaceoviridis E-86.
Suzuki R, Fujimoto Z, Ito S, Kawahara S, Kaneko S, Taira K, Hasegawa T, Kuno A
J Biochem 146 61-70 (2009)
PMID: 19279191

Function and Biology Details

Reaction catalysed: 
Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-181928 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Beta-xylanase Chains: A, B
Molecule details ›
Chains: A, B
Length: 436 amino acids
Theoretical weight: 46.77 KDa
Source organism: Streptomyces olivaceoviridis
Expression system: Escherichia coli
UniProt:
  • Canonical: Q7SI98 (Residues: 1-436; Coverage: 100%)
Sequence domains:
Structure domains:

Ligands and Environments

Carbohydrate polymer : NEW Components: XYS
Carbohydrate polymer
2 bound ligands:
Ligand AZI 2 x AZI
Ligand GOL 8 x GOL
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: PHOTON FACTORY BEAMLINE AR-NW12A
Spacegroup: P212121
Unit cell:
a: 78.929Å b: 94.092Å c: 139.466Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.183 0.183 0.211
Expression system: Escherichia coli

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Citations

1 review citation

Structure and function of carbohydrate-binding module families 13 and 42 of glycoside hydrolases, comprising a β-trefoil fold.
Fujimoto Z. (2013)
10 other articles

2 mentions without citation

Structural determinants of growth factor binding and specificity by VEGF receptor 2.
Leppänen et al. (2010)
1 more

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