5.1.1.18: serine racemase
This is an abbreviated version!
For detailed information about serine racemase, go to the full flat file.
Word Map on EC 5.1.1.18
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5.1.1.18
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d-serine
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n-methyl-d-aspartate
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co-agonist
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nmdars
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astrocyte
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d-amino
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schizophrenia
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neurotransmission
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pyridoxal
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hypofunction
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d-aspartate
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glutamatergic
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5'-phosphate-dependent
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nmda-type
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d-ser
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plp-dependent
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nmdar-mediated
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pharmacology
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medicine
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alanine-serine-cysteine
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drug development
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glycine-binding
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n-methyl-d
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vante
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brain-enriched
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gliotransmitter
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nmdar-dependent
- 5.1.1.18
- d-serine
- n-methyl-d-aspartate
-
co-agonist
-
nmdars
- astrocyte
-
d-amino
-
schizophrenia
-
neurotransmission
- pyridoxal
-
hypofunction
- d-aspartate
-
glutamatergic
-
5'-phosphate-dependent
-
nmda-type
- d-ser
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plp-dependent
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nmdar-mediated
- pharmacology
- medicine
-
alanine-serine-cysteine
- drug development
-
glycine-binding
-
n-methyl-d
-
vante
-
brain-enriched
-
gliotransmitter
-
nmdar-dependent
Reaction
Synonyms
hSR, More, RiSR, RLO149_c015450, Ser racemase, SerR, SRace, SRR, T01H8.2, Zm-SR, ZmSR
ECTree
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Crystallization
Crystallization on EC 5.1.1.18 - serine racemase
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purified recombinant mutant C2D/C6D by sitting drop vapor diffusion, 10 mg/ml protein in 20 mM Tris-HCl, pH 8.0, 100 mM NaCl, 10% glycerol, 0.05 mM PLP, 2 mM MgCl2, 5 mM dithiothreitol, mixed with 25% PEG 3350, 200 mM sodium malonate, and 50 mM MnCl2 as the reservoir solution, 4 days, the selenomethionine-labeled enzyme crystals grow under similar conditions, X-ray diffraction structure determination and analysis at 1.5-1.7 A resolution
purified recombinant mutant C2D/C6D by sitting drop vapor diffusion, 35 mg/ml protein, from 55% v/v Tacsimate, i.e. 1.8305 M malonic acid, 0.25 M ammonium citrate tribasic, 0.12 M succinic acid, 0.3 M DL-malic acid, 0.4 M sodium acetate trihydrate, 0.5 M sodium formate, and 0.16 M ammonium tartrate dibasic, pH 8.0, and 100 mM Bis-Tris propane, pH 7.8, 10 days, X-ray diffraction structure determination and analysis at 1.8-1.95 A resolution
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free wild-type enzyme, wild-type enzyme in complex with the ATP analogue AMP-PCP, and the modified enzyme in complex with serine, vapor diffusion method at 20°C, 0.003 ml of protein solution with 2.2 mg/ml protein and 10 mM Tris-HCl buffer, pH 8.0, are mixed with an equal volume of reservoir solution containing 28% w/v PEG 4000, 200 mM sodium acetate, and 100 mM Tris-HCl, pH 8.5, and equilibrated against 450 ml of the reservoir solution, for the ligand complexed enzyme, 10 mM AMP-PCP and 0.2 M MgCl2 are added, X-ray diffraction structure determination and analysis at at 1.7 A, 1.9 A, and 2.2 A resolution, respectively
native and modified enzyme, X-ray diffraction structure determination and analysis at 1.7 A resolution
purified recombinant His6-tagged enzyme, hanging drop vapour diffusion method, mixing of 0.001 ml of 10 mg/ml protein in 20 mM Tris-HCl, 100 mM NaCl, 10% glycerol, pH 8.0, with 0.001 ml of reservoir solution containing 0.2 M calcium acetate, 0.1 M sodium cacodylate, pH 6.5, 18% PEG 8000, equilibration agains 0.2 ml of reservoir solution, at 4°C, X-ray diffraction structure determination and analysis at 2.1 A resolution, molecular replacement based on the Rattus norvegicus serine racemase, PDB ID 3hmk