1YTE

Crystal structure of a nicotinate phosphoribosyltransferase from Thermoplasma acidophilum, phosphoribosylpyrophosphate bound structure

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0004514	molecular_function	nicotinate-nucleotide diphosphorylase (carboxylating) activity
A	0004516	molecular_function	nicotinate phosphoribosyltransferase activity
A	0009435	biological_process	NAD biosynthetic process
A	0016740	molecular_function	transferase activity
A	0016763	molecular_function	pentosyltransferase activity
A	0016874	molecular_function	ligase activity
A	0019363	biological_process	pyridine nucleotide biosynthetic process
A	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	13
Details	BINDING SITE FOR RESIDUE PCP A 401

Chain	Residue
A	SER45
A	HOH512
A	HOH515
A	HOH527
A	HOH573
A	ARG142
A	PRO239
A	SER240
A	GLY272
A	GLY292
A	THR293
A	ASP302
A	HOH502

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	3
Details	BINDING: BINDING => ECO:0000305|PubMed:15753098

Chain	Residue	Details
A	TYR21
A	PHE138
A	SER240

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site_id	SWS_FT_FI2
Number of Residues	4
Details	BINDING: BINDING => ECO:0000305|PubMed:15753098, ECO:0007744|PDB:1YTK

Chain	Residue	Details
A	ARG235
A	GLY272
A	THR293
A	THR179

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site_id	SWS_FT_FI3
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269|Ref.3

Chain	Residue	Details
A	CYS348
A	CYS350
A	CYS330
A	CYS333

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site_id	SWS_FT_FI4
Number of Residues	1
Details	MOD_RES: Phosphohistidine => ECO:0000250|UniProtKB:P22253

Chain	Residue	Details
A	HIS182

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