› 5od1

X-ray diffraction
1.34Å resolution

Structure of the engineered metalloesterase MID1sc10 complexed with a phosphonate transition state analogue

Released:
DOI: 10.2210/pdb5od1/pdb
PDB entry 5od1 coloured by chain, front view.
PDB entry 5od1 coloured by chain, side view.
PDB entry 5od1 coloured by chain, top view.
Source organism: synthetic construct
Primary publication:
Evolution of a highly active and enantiospecific metalloenzyme from short peptides.
Studer S, Hansen DA, Pianowski ZL, Mittl PRE, Debon A, Guffy SL, Der BS, Kuhlman B, Hilvert D
Science 362 1285-1288 (2018)
PMID: 30545884

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-166052 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
MID1sc10 Chain: A
Molecule details ›
Chain: A
Length: 97 amino acids
Theoretical weight: 10.87 KDa
Source organism: synthetic construct
Expression system: Escherichia coli

Ligands and Environments

3 bound ligands:
Ligand ZN 1 x ZN
Ligand 9RQ 1 x 9RQ
Ligand GOL 1 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06SA
Spacegroup: I222
Unit cell:
a: 32.349Å b: 46.877Å c: 112.621Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.129 0.126 0.171
Expression system: Escherichia coli

Quick links

Citations

8 review citations

The road to fully programmable protein catalysis.
Lovelock et al. (2022)
7 more

3 mentions without citation

De novo protein design, a retrospective.
Korendovych et al. (2020)
2 more