3L0G

Crystal structure of Nicotinate-nucleotide pyrophosphorylase from Ehrlichia chaffeensis at 2.05A resolution

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004514	molecular_function	nicotinate-nucleotide diphosphorylase (carboxylating) activity
A	0005737	cellular_component	cytoplasm
A	0009435	biological_process	NAD biosynthetic process
A	0016740	molecular_function	transferase activity
A	0016757	molecular_function	glycosyltransferase activity
A	0016763	molecular_function	pentosyltransferase activity
A	0019363	biological_process	pyridine nucleotide biosynthetic process
A	0034213	biological_process	quinolinate catabolic process
B	0004514	molecular_function	nicotinate-nucleotide diphosphorylase (carboxylating) activity
B	0005737	cellular_component	cytoplasm
B	0009435	biological_process	NAD biosynthetic process
B	0016740	molecular_function	transferase activity
B	0016757	molecular_function	glycosyltransferase activity
B	0016763	molecular_function	pentosyltransferase activity
B	0019363	biological_process	pyridine nucleotide biosynthetic process
B	0034213	biological_process	quinolinate catabolic process
C	0004514	molecular_function	nicotinate-nucleotide diphosphorylase (carboxylating) activity
C	0005737	cellular_component	cytoplasm
C	0009435	biological_process	NAD biosynthetic process
C	0016740	molecular_function	transferase activity
C	0016757	molecular_function	glycosyltransferase activity
C	0016763	molecular_function	pentosyltransferase activity
C	0019363	biological_process	pyridine nucleotide biosynthetic process
C	0034213	biological_process	quinolinate catabolic process
D	0004514	molecular_function	nicotinate-nucleotide diphosphorylase (carboxylating) activity
D	0005737	cellular_component	cytoplasm
D	0009435	biological_process	NAD biosynthetic process
D	0016740	molecular_function	transferase activity
D	0016757	molecular_function	glycosyltransferase activity
D	0016763	molecular_function	pentosyltransferase activity
D	0019363	biological_process	pyridine nucleotide biosynthetic process
D	0034213	biological_process	quinolinate catabolic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE EDO A 300

Chain	Residue
A	SER128
A	THR129
A	TYR152
A	LEU211
A	GLU234
A	HOH293
A	FMT301

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site_id	AC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE EDO B 300

Chain	Residue
B	TYR152
B	GLU234
B	SER256
B	FMT301
B	HOH323
B	SER128
B	THR129

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site_id	AC3
Number of Residues	9
Details	BINDING SITE FOR RESIDUE EDO C 300

Chain	Residue
C	ARG127
C	SER128
C	THR129
C	TYR152
C	LEU211
C	GLU234
C	SER256
C	HOH290
C	FMT301

---

site_id	AC4
Number of Residues	8
Details	BINDING SITE FOR RESIDUE EDO D 300

Chain	Residue
D	ARG127
D	SER128
D	THR129
D	TYR152
D	LEU211
D	GLU234
D	FMT301
D	HOH303

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site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE FMT A 301

Chain	Residue
A	ARG130
A	ARG153
A	LYS163
A	EDO300
A	HOH304

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site_id	AC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE FMT B 301

Chain	Residue
B	ARG130
B	ARG153
B	LEU161
B	LYS163
B	HOH293
B	EDO300

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site_id	AC7
Number of Residues	6
Details	BINDING SITE FOR RESIDUE FMT C 301

Chain	Residue
C	ARG130
C	ARG153
C	LEU161
C	LYS163
C	EDO300
C	HOH347

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site_id	AC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE FMT D 301

Chain	Residue
D	ARG130
D	ARG153
D	LYS163
D	EDO300
D	HOH862

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