› 3hoj

X-ray diffraction
2.2Å resolution

Crystal Structure of a Novel Engineered Retroaldolase: RA-22

Released:
DOI: 10.2210/pdb3hoj/pdb
PDB entry 3hoj coloured by chain, front view.
PDB entry 3hoj coloured by chain, side view.
PDB entry 3hoj 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

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-163638 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
RETROALDOLASE-22 Chain: A
Molecule details ›
Chain: A
Length: 248 amino acids
Theoretical weight: 28.46 KDa
Source organism: synthetic construct
Expression system: Escherichia coli
Structure domains: Aldolase class I

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007
Spacegroup: P21212
Unit cell:
a: 72.047Å b: 73.583Å c: 47.399Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.238 0.236 0.293
Expression system: Escherichia coli

Quick links

Citations

178 review citations

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

1 mention without citation

A score of the ability of a three-dimensional protein model to retrieve its own sequence as a quantitative measure of its quality and appropriateness.
Martínez-Castilla et al. (2010)