5grr

X-ray diffraction
1.45Å resolution

Crystal structure of MCR-1

Released:
Source organism: Escherichia coli
Primary publication:
High resolution crystal structure of the catalytic domain of MCR-1.
OpenAccess logo Sci Rep 6 39540 (2016)
PMID: 28000749

Function and Biology Details

Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-102665 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Probable phosphatidylethanolamine transferase Mcr-1 Chain: A
Molecule details ›
Chain: A
Length: 325 amino acids
Theoretical weight: 36.18 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: A0A0R6L508 (Residues: 219-541; Coverage: 60%)
Gene names: APZ14_31440, mcr-1, mcr1
Sequence domains: Sulfatase
Structure domains: Alkaline Phosphatase, subunit A

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL17U
Spacegroup: P212121
Unit cell:
a: 47.314Å b: 62.696Å c: 104.831Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.153 0.152 0.177
Expression system: Escherichia coli