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X-ray diffraction
2.33Å resolution

Crystal Structure of MCR-1, a phosphoethanolamine transferase, extracellular domain

Released:
DOI: 10.2210/pdb5gov/pdb
PDB entry 5gov coloured by chain, front view.
PDB entry 5gov coloured by chain, side view.
PDB entry 5gov coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Crystal Structure of Escherichia coli originated MCR-1, a phosphoethanolamine transferase for Colistin Resistance.
Hu M, Guo J, Cheng Q, Yang Z, Chan EWC, Chen S, Hao Q
Sci Rep 6 38793 (2016)
PMID: 27958270

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-102666 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Probable phosphatidylethanolamine transferase Mcr-1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 365 amino acids
Theoretical weight: 40.7 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: A0A0R6L508 (Residues: 200-541; Coverage: 63%)
Gene names: APZ14_31440, mcr-1, mcr1
Sequence domains: Sulfatase
Structure domains: Alkaline Phosphatase, subunit A

Ligands and Environments

1 bound ligand:
Ligand ZN 11 x ZN
1 modified residue:
Ligand TPO 2 x TPO

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL17U
Spacegroup: P212121
Unit cell:
a: 54.439Å b: 55.833Å c: 219.388Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.188 0.186 0.236
Expression system: Escherichia coli

Quick links

Citations

9 review citations

Development of New Tools to Detect Colistin-Resistance among Enterobacteriaceae Strains.
Bardet et al. (2018)
8 more

3 mentions without citation

Crystal Structure of Escherichia coli originated MCR-1, a phosphoethanolamine transferase for Colistin Resistance.
Hu et al. (2016)
2 more