› 5ah3

X-ray diffraction
2.4Å resolution

Crystal structure of the Mep2 mutant R452D,S453D from Candida albicans

Released:
DOI: 10.2210/pdb5ah3/pdb
PDB entry 5ah3 coloured by chain, front view.
PDB entry 5ah3 coloured by chain, side view.
PDB entry 5ah3 coloured by chain, top view.
Source organism: Candida albicans
Primary publication:
Structural basis for Mep2 ammonium transceptor activation by phosphorylation.
van den Berg B, Chembath A, Jefferies D, Basle A, Khalid S, Rutherford JC
Nat Commun 7 11337 (2016)
PMID: 27088325

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-176854 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ammonium transporter Chain: A
Molecule details ›
Chain: A
Length: 486 amino acids
Theoretical weight: 52.78 KDa
Source organism: Candida albicans
Expression system: Saccharomyces cerevisiae W303
UniProt:
  • Canonical: Q59UP8 (Residues: 1-480; Coverage: 100%)
Gene names: CAALFM_C400430WA, MEP2, orf19.13117
Sequence domains: Ammonium Transporter Family
Structure domains: Ammonium transporter AmtB like domains

Ligands and Environments

1 bound ligand:
Ligand DMU 5 x DMU
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04-1
Spacegroup: P6322
Unit cell:
a: 112.678Å b: 112.678Å c: 251.146Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.175 0.174 0.2
Expression system: Saccharomyces cerevisiae W303

Quick links

Citations

11 review citations

Update on amino acid transporter functions and on possible amino acid sensing mechanisms in plants.
Dinkeloo et al. (2018)
10 more

1 mention without citation

Structural basis for Mep2 ammonium transceptor activation by phosphorylation.
van den Berg et al. (2016)