2R7L

Crystal structure of FAICAR synthetase (PurP) from M. jannaschii complexed with ATP and AICAR

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000287	molecular_function	magnesium ion binding
A	0005524	molecular_function	ATP binding
A	0006164	biological_process	purine nucleotide biosynthetic process
A	0006188	biological_process	IMP biosynthetic process
A	0006189	biological_process	'de novo' IMP biosynthetic process
A	0016874	molecular_function	ligase activity
A	0016879	molecular_function	ligase activity, forming carbon-nitrogen bonds
A	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	2
Details	BINDING SITE FOR RESIDUE SO4 A 500

Chain	Residue
A	LYS56
A	ARG57

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site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CL A 601

Chain	Residue
A	HIS27
A	ARG314
A	ASP316
A	GLY317

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site_id	AC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE CL A 602

Chain	Residue
A	HIS210
A	ASP316
A	THR319

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site_id	AC4
Number of Residues	22
Details	BINDING SITE FOR RESIDUE ATP A 400

Chain	Residue
A	PRO140
A	ILE154
A	LYS156
A	TYR166
A	GLU199
A	GLU200
A	TYR201
A	ARG228
A	GLU230
A	ARG238
A	TYR253
A	ILE255
A	GLN297
A	LEU299
A	PHE309
A	GLU310
A	HOH608
A	HOH611
A	HOH612
A	HOH613
A	HOH689
A	HOH726

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site_id	AC5
Number of Residues	14
Details	BINDING SITE FOR RESIDUE AMZ A 401

Chain	Residue
A	HIS27
A	SER94
A	ARG228
A	ILE255
A	ASN258
A	ARG264
A	SER266
A	GLY317
A	GLY318
A	HOH603
A	HOH604
A	HOH605
A	HOH645
A	HOH724

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	6
Details	BINDING:

Chain	Residue	Details
A	HIS27
A	SER94
A	LYS156
A	GLU199
A	GLU230
A	ASN258

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site_id	SWS_FT_FI2
Number of Residues	2
Details	BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01163

Chain	Residue	Details
A	GLN297
A	GLU310

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