1VKZ

Crystal structure of Phosphoribosylamine--glycine ligase (TM1250) from Thermotoga maritima at 2.30 A resolution

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0004637	molecular_function	phosphoribosylamine-glycine ligase activity
A	0005524	molecular_function	ATP binding
A	0006164	biological_process	purine nucleotide biosynthetic process
A	0006189	biological_process	'de novo' IMP biosynthetic process
A	0009113	biological_process	purine nucleobase biosynthetic process
A	0016874	molecular_function	ligase activity
A	0046872	molecular_function	metal ion binding
B	0003824	molecular_function	catalytic activity
B	0004637	molecular_function	phosphoribosylamine-glycine ligase activity
B	0005524	molecular_function	ATP binding
B	0006164	biological_process	purine nucleotide biosynthetic process
B	0006189	biological_process	'de novo' IMP biosynthetic process
B	0009113	biological_process	purine nucleobase biosynthetic process
B	0016874	molecular_function	ligase activity
B	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	1
Details	BINDING SITE FOR RESIDUE EDO B 401

Chain	Residue
B	LEU180

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Functional Information from PROSITE/UniProt

site_id	PS00184
Number of Residues	8
Details	GARS Phosphoribosylglycinamide synthetase signature. RLGDPEtE

Chain	Residue	Details
A	ARG277-GLU284

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	6
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00138

Chain	Residue	Details
A	ILE125
A	GLU273
A	ASN275
B	ILE125
B	GLU273
B	ASN275

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