› 5cml

X-ray diffraction
1.56Å resolution

Crystal structure of the Esterase domain from Rhodothermus marinus Rmar_1206 protein

Released:
DOI: 10.2210/pdb5cml/pdb
PDB entry 5cml coloured by chain, front view.
PDB entry 5cml coloured by chain, side view.
PDB entry 5cml coloured by chain, top view.
Source organism: Rhodothermus marinus
Primary publication:
Characterisation of a New Family of Carboxyl Esterases with an OsmC Domain.
Jensen MV, Horsfall LE, Wardrope C, Togneri PD, Marles-Wright J, Rosser SJ
PLoS One 11 e0166128 (2016)
PMID: 27851780

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)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Serine aminopeptidase S33 domain-containing protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 263 amino acids
Theoretical weight: 29.02 KDa
Source organism: Rhodothermus marinus
Expression system: Escherichia coli
UniProt:
  • Canonical: D0MHY8 (Residues: 1-255; Coverage: 62%)
Gene name: Rmar_1206
Sequence domains: Serine aminopeptidase, S33
Structure domains: alpha/beta hydrolase

Ligands and Environments

1 bound ligand:
Ligand PGE 2 x PGE
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I02
Spacegroup: P21
Unit cell:
a: 60.325Å b: 74.069Å c: 60.953Å
α: 90° β: 113.47° γ: 90°
R-values:
R R work R free
0.146 0.144 0.176
Expression system: Escherichia coli

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Citations

3 mentions without citation

Recent developments in MrBUMP: better search-model preparation, graphical interaction with search models, and solution improvement and assessment.
Keegan et al. (2018)
2 more