4RJ2

Crystal structure of E.coli purine nucleoside phosphorylase at 0.99 A resolution

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0004731	molecular_function	purine-nucleoside phosphorylase activity
A	0006139	biological_process	nucleobase-containing compound metabolic process
A	0009116	biological_process	nucleoside metabolic process
A	0016763	molecular_function	pentosyltransferase activity
B	0003824	molecular_function	catalytic activity
B	0004731	molecular_function	purine-nucleoside phosphorylase activity
B	0006139	biological_process	nucleobase-containing compound metabolic process
B	0009116	biological_process	nucleoside metabolic process
B	0016763	molecular_function	pentosyltransferase activity
C	0003824	molecular_function	catalytic activity
C	0004731	molecular_function	purine-nucleoside phosphorylase activity
C	0006139	biological_process	nucleobase-containing compound metabolic process
C	0009116	biological_process	nucleoside metabolic process
C	0016763	molecular_function	pentosyltransferase activity
D	0003824	molecular_function	catalytic activity
D	0004731	molecular_function	purine-nucleoside phosphorylase activity
D	0006139	biological_process	nucleobase-containing compound metabolic process
D	0009116	biological_process	nucleoside metabolic process
D	0016763	molecular_function	pentosyltransferase activity
E	0003824	molecular_function	catalytic activity
E	0004731	molecular_function	purine-nucleoside phosphorylase activity
E	0006139	biological_process	nucleobase-containing compound metabolic process
E	0009116	biological_process	nucleoside metabolic process
E	0016763	molecular_function	pentosyltransferase activity
F	0003824	molecular_function	catalytic activity
F	0004731	molecular_function	purine-nucleoside phosphorylase activity
F	0006139	biological_process	nucleobase-containing compound metabolic process
F	0009116	biological_process	nucleoside metabolic process
F	0016763	molecular_function	pentosyltransferase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	13
Details	BINDING SITE FOR RESIDUE GOL A 301

Chain	Residue
A	GLY20
A	HOH535
A	HOH558
D	ARG43
D	HOH460
A	GLY63
A	MET64
A	ARG87
A	GLY89
A	SER90
A	GLU179
A	MET180
A	GLU181

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site_id	AC2
Number of Residues	9
Details	BINDING SITE FOR RESIDUE GOL C 301

Chain	Residue
C	GLY20
C	ASP21
C	ARG87
C	GLY89
C	SER90
C	HOH434
C	HOH461
C	HOH554
E	ARG43

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site_id	AC3
Number of Residues	11
Details	BINDING SITE FOR RESIDUE GOL D 301

Chain	Residue
A	ARG43
D	PRO19
D	GLY20
D	ASP21
D	ARG87
D	GLY89
D	SER90
D	GOL303
D	HOH453
D	HOH470
D	HOH576

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site_id	AC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE GOL D 302

Chain	Residue
D	ARG101
D	THR220
D	ASP223

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site_id	AC5
Number of Residues	12
Details	BINDING SITE FOR RESIDUE GOL D 303

Chain	Residue
A	ARG43
D	GLY20
D	HIS62
D	GLY63
D	MET64
D	ARG87
D	GLU179
D	MET180
D	GLU181
D	GOL301
D	HOH564
D	HOH573

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site_id	AC6
Number of Residues	10
Details	BINDING SITE FOR RESIDUE GOL F 301

Chain	Residue
B	ARG43
F	GLY20
F	ARG24
F	HIS62
F	ARG87
F	VAL88
F	GLY89
F	SER90
F	GLU181
F	HOH493

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Functional Information from PROSITE/UniProt

site_id	PS01232
Number of Residues	16
Details	PNP_UDP_1 Purine and other phosphorylases family 1 signature. GhGMGiPScSIytkEL

Chain	Residue	Details
A	GLY61-LEU76

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