6.3.4.13: phosphoribosylamine-glycine ligase

This is an abbreviated version!
For detailed information about phosphoribosylamine-glycine ligase, go to the full flat file.

Word Map on EC 6.3.4.13

6.3.4.13

transformylase

aminoimidazole

formyltransferase

amidotransferase

phosphoribosylaminoimidazole

phosphoribosylpyrophosphate

medicine

Reaction

Synonyms

2-Amino-N-ribosylacetamide 5'-phosphate kinosynthase, 5'-Phosphoribosylglycinamide synthetase, ade5, EC 6.3.1.3, GAR synthetase, GAR-syn, GARS, GARSase, GART, Glycinamide ribonucleotide synthetase, glycinamide ribotide synthetase, Glycineamide ribonucleotide synthetase, Phosphoribosylglycinamide synthetase, Phosphoribosylglycineamide synthetase, PRG synthetase, PUR2,5, Synthetase, phosphoribosylglycinamide, trifunctional purine biosynthetic protein adenosine-3

ECTree

6 Ligases

6.3 Forming carbon-nitrogen bonds

6.3.4 Other carbon-nitrogen ligases

6.3.4.13 phosphoribosylamine-glycine ligase

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Results	in table
43746	AA Sequence
1	Application
1	CAS Registry Number
13	Cloned(Commentary)
1	Cofactor
5	Crystallization (Commentary)
10	Disease/ Diagnostics
4	General Information
1	General Stability
4	Inhibitors
19	KM Value [mM]
1	Localization
1	Metals/Ions
14	Molecular Weight [Da]
31	Natural Substrates/ Products (Substrates)
95	Organism
8	Pathway
32	PDB ID
2	pH Optimum
1	pH Range
2	Protein Variants
10	Purification (Commentary)
21	Reaction
1	Reaction Type
54	Reference
12	Source Tissue
8	Specific Activity [micromol/min/mg]
3	Storage Stability
105	Substrates and Products (Substrate)
11	Subunits
21	Synonyms
1	Systematic Name
2	Temperature Optimum [°C]
3	Temperature Range [°C]
1	Temperature Stability [°C]
8	Turnover Number [1/s]

Crystallization

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Crystallization on EC 6.3.4.13 - phosphoribosylamine-glycine ligase

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native enzyme and in complex with ATP, to 2.4 and 1.8 A resolution, respectively. Comparison of crystal structures of GAR-syn from Thermus thermophilus, Geobacillus kaustophilus and Aquifex aeolicus. The orientations of the B domains are varied among GAR-syns and the molecular dynamics simulation suggests the mobility of the B domain. The B loop in the B domain fixes the position of the beta- and gamma-phosphate groups of the bound ATP

Aquifex aeolicus

O66949

715404

selenomethionine incorporated enzyme, hanging drop vapor diffusion method

2 entries

native enzyme and in complex with phosphate, with AMP and phosphate, and with AMP and glycine, to 2.21, 2.20, 1.9 and 2.21 A resolution, respectively. Comparison of crystal structures of GAR-syn from Thermus thermophilus, Geobacillus kaustophilus and Aquifex aeolicus. The orientations of the B domains are varied among GAR-syn's and the molecular dynamics simulation suggests the mobility of the B domain. The B loop in the B domain fixes the position of the beta- and gamma-phosphate groups of the bound ATP

Geobacillus kaustophilus

Q5L3C7

715404

selenomethionine derivative, to 2.8 A resolution. Comparison of crystal structures of GAR-syn from Thermus thermophilus, Geobacillus kaustophilus and Aquifex aeolicus. The orientations of the B domains are varied among GAR-syns and the molecular dynamics simulation suggests the mobility of the B domain. The B loop in the B domain fixes the position of the beta- and gamma-phosphate groups of the bound ATP

Thermus thermophilus

Q5SK40

715404