6.3.3.1: phosphoribosylformylglycinamidine cyclo-ligase

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

Word Map on EC 6.3.3.1

6.3.3.1

purine

transformylase

glycinamide

trifunctional

phosphoribosylglycinamide

formyltransferase

monofunctional

amidotransferase

formylglycinamide

2.1.2.2

cowpea

purl

phosphoribosylamine

unguiculata

Reaction

2-(formamido)-N1-(5-phospho-D-ribosyl)acetamidine

5-amino-1-(5-phospho-D-ribosyl)imidazole

Synonyms

5'-Aminoimidazole ribonucleotide synthetase, 5'-Phosphoribosyl-5-aminoimidazole synthetase, AIR synthase, AIR synthetase, AIRS, aminoimidazole ribonucleotide synthetase, phosphoribosyl aminoimidazole synthetase, Phosphoribosyl-aminoimidazole synthetase, Phosphoribosylaminoimidazole synthetase, PurM, Synthetase, phosphoribosylaminoimidazole

ECTree

6 Ligases

6.3 Forming carbon-nitrogen bonds

6.3.3 Cyclo-ligases

6.3.3.1 phosphoribosylformylglycinamidine cyclo-ligase

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Results	in table
41398	AA Sequence
1	CAS Registry Number
9	Cloned(Commentary)
1	Crystallization (Commentary)
2	Disease/ Diagnostics
6	Inhibitors
1	Ki Value [mM]
13	KM Value [mM]
4	Localization
10	Metals/Ions
14	Molecular Weight [Da]
5	Natural Substrates/ Products (Substrates)
21	Organism
8	Pathway
34	PDB ID
2	pH Optimum
1	pH Range
5	Protein Variants
11	Purification (Commentary)
5	Reaction
1	Reaction Type
21	Reference
7	Source Tissue
3	Specific Activity [micromol/min/mg]
1	Storage Stability
27	Substrates and Products (Substrate)
7	Subunits
18	Synonyms
1	Systematic Name

Crystallization

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Crystallization on EC 6.3.3.1 - phosphoribosylformylglycinamidine cyclo-ligase

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molecular modeling based on Escherichia coli crystal structure, and molecular dynamics simulation. The binding pocket is composed of residues Lys13, Thr14, Ala17, Leu18, Ile21, Arg26, Lys35, Glu38, Pro39, Glu40, Asp103, Leu105, Ile133, Gly135, Gly136, Gln137 and Thr138

Pyrococcus horikoshii

O58054

745399