2PBZ

Crystal structure of an IMP biosynthesis protein PurP from Thermococcus kodakaraensis

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
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	0016879	molecular_function	ligase activity, forming carbon-nitrogen bonds
B	0000166	molecular_function	nucleotide binding
B	0000287	molecular_function	magnesium ion binding
B	0005524	molecular_function	ATP binding
B	0006164	biological_process	purine nucleotide biosynthetic process
B	0006188	biological_process	IMP biosynthetic process
B	0016879	molecular_function	ligase activity, forming carbon-nitrogen bonds
C	0000166	molecular_function	nucleotide binding
C	0000287	molecular_function	magnesium ion binding
C	0005524	molecular_function	ATP binding
C	0006164	biological_process	purine nucleotide biosynthetic process
C	0006188	biological_process	IMP biosynthetic process
C	0016879	molecular_function	ligase activity, forming carbon-nitrogen bonds

Functional Information from PDB Data

site_id	AC1
Number of Residues	15
Details	BINDING SITE FOR RESIDUE ATP A 400

Chain	Residue
A	PHE129
A	ILE263
A	HOH409
A	HOH436
A	HOH438
A	HOH454
C	ARG201
A	GLU145
A	ARG164
A	PHE165
A	ILE166
A	TYR170
A	TYR172
A	LEU194
A	TYR209

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site_id	AC2
Number of Residues	17
Details	BINDING SITE FOR RESIDUE ATP B 400

Chain	Residue
A	ARG201
B	PHE129
B	GLU145
B	ARG164
B	PHE165
B	ILE166
B	TYR170
B	TYR172
B	LEU194
B	TYR209
B	ILE263
B	HOH405
B	HOH427
B	HOH439
B	HOH441
B	HOH458
B	HOH470

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site_id	AC3
Number of Residues	18
Details	BINDING SITE FOR RESIDUE ATP C 400

Chain	Residue
B	ARG201
C	PHE129
C	GLU145
C	ARG164
C	PHE165
C	ILE166
C	TYR170
C	TYR172
C	LEU194
C	TYR209
C	ILE263
C	HOH404
C	HOH414
C	HOH415
C	HOH428
C	HOH433
C	HOH438
C	HOH457

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