› 3b5l

X-ray diffraction
1.8Å resolution

Crystal Structure of a Novel Engineered Retroaldolase: RA-61

Released:
DOI: 10.2210/pdb3b5l/pdb
PDB entry 3b5l coloured by chain, front view.
PDB entry 3b5l coloured by chain, side view.
PDB entry 3b5l coloured by chain, top view.
Source organism: synthetic construct
Primary publication:
De novo computational design of retro-aldol enzymes.
Jiang L, Althoff EA, Clemente FR, Doyle L, Röthlisberger D, Zanghellini A, Gallaher JL, Betker JL, Tanaka F, Barbas CF, Hilvert D, Houk KN, Stoddard BL, Baker D
Science 319 1387-91 (2008)
PMID: 18323453

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-184541 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Endo-1,4-beta-xylanase Chain: B
Molecule details ›
Chain: B
Length: 198 amino acids
Theoretical weight: 21.92 KDa
Source organism: synthetic construct
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8GMV7 (Residues: 41-237; Coverage: 65%)
Gene names: FHX40_0105, xyn11A
Sequence domains: Glycosyl hydrolases family 11
Structure domains: Jelly Rolls

Ligands and Environments

2 bound ligands:
Ligand SO4 2 x SO4
Ligand NH4 2 x NH4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007
Spacegroup: P212121
Unit cell:
a: 39.19Å b: 66.06Å c: 66.07Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.206 0.203 0.248
Expression system: Escherichia coli

Quick links

Citations

179 review citations

The role of dynamic conformational ensembles in biomolecular recognition.
Boehr et al. (2009)
178 more

2 mentions without citation

De novo computational design of retro-aldol enzymes.
Jiang et al. (2008)
1 more