› 5elm

X-ray diffraction
2Å resolution

Crystal structure of L-aspartate/glutamate specific racemase in complex with L-glutamate

Released:
DOI: 10.2210/pdb5elm/pdb
PDB entry 5elm coloured by chain, front view.
PDB entry 5elm coloured by chain, side view.
PDB entry 5elm coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Structural basis for an atypical active site of an L-aspartate/glutamate-specific racemase from Escherichia coli.
Ahn JW, Chang JH, Kim KJ
FEBS Lett 589 3842-7 (2015)
PMID: 26555188

Function and Biology Details

Reactions catalysed: 
An L-amino acid = a D-amino acid
L-aspartate = D-aspartate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-111207 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Aspartate/glutamate racemase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 238 amino acids
Theoretical weight: 26.39 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: C3SWD2 (Residues: 1-230; Coverage: 100%)
Gene names: ACN81_20060, ACU57_24110, BANRA_01362, BGM66_001442, BGZ_03603, BJI68_00725, BK292_22760, C1Q91_001304, C3F40_22375, CF22_001457, CG704_06135, CG831_002248, CIG67_09740, CTR35_002224, D4M65_07960, DIV22_30085, DS732_21010, DTL43_07930, E5H86_25045, EAI46_05580, EAN77_05830, ECs3697, EHD79_07070, EIZ93_12150, EN85_002110, EPS97_08920, FJQ40_12345, FORC44_0983, FPS11_11130, FVB16_08895, GAI89_12030, GAJ12_01165, GNW61_06625, GP954_11505, GP965_08955, GQE86_07465, GQM04_06965, GQM21_15610, GRW05_08465, GRW24_15355, GRW56_24285, GRW57_12805, GUC01_19940, HHH44_000146, HV209_17145, HVY77_05425, I6H00_23525, J0541_001380, J5U05_001123, JNP96_21800, NCTC8960_03712, NCTC9045_01146, NEP60_11815, RZR61_11780, SAMEA3752557_03104, ygeA
Sequence domains: Asp/Glu/Hydantoin racemase
Structure domains: Rossmann fold

Ligands and Environments

3 bound ligands:
Ligand GOL 2 x GOL
Ligand GLU 3 x GLU
Ligand NO3 1 x NO3
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PAL/PLS BEAMLINE 7A (6B, 6C1)
Spacegroup: P21
Unit cell:
a: 67.53Å b: 81.25Å c: 83.96Å
α: 90° β: 111.39° γ: 90°
R-values:
R R work R free
0.176 0.173 0.236
Expression system: Escherichia coli

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Citations

1 review citation

Racemases and epimerases operating through a 1,1-proton transfer mechanism: reactivity, mechanism and inhibition.
Lloyd et al. (2021)
8 other articles