Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3UT6

Crystal structure of E. Coli PNP complexed with PO4 and formycin A

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0004731	molecular_function	purine-nucleoside phosphorylase activity
A	0005829	cellular_component	cytosol
A	0006139	biological_process	nucleobase-containing compound metabolic process
A	0006152	biological_process	purine nucleoside catabolic process
A	0006974	biological_process	DNA damage response
A	0009116	biological_process	nucleoside metabolic process
A	0009164	biological_process	nucleoside catabolic process
A	0016020	cellular_component	membrane
A	0016757	molecular_function	glycosyltransferase activity
A	0016763	molecular_function	pentosyltransferase activity
A	0019686	biological_process	purine nucleoside interconversion
A	0042278	biological_process	purine nucleoside metabolic process
A	0042802	molecular_function	identical protein binding
A	0047975	molecular_function	guanosine phosphorylase activity
B	0003824	molecular_function	catalytic activity
B	0004731	molecular_function	purine-nucleoside phosphorylase activity
B	0005829	cellular_component	cytosol
B	0006139	biological_process	nucleobase-containing compound metabolic process
B	0006152	biological_process	purine nucleoside catabolic process
B	0006974	biological_process	DNA damage response
B	0009116	biological_process	nucleoside metabolic process
B	0009164	biological_process	nucleoside catabolic process
B	0016020	cellular_component	membrane
B	0016757	molecular_function	glycosyltransferase activity
B	0016763	molecular_function	pentosyltransferase activity
B	0019686	biological_process	purine nucleoside interconversion
B	0042278	biological_process	purine nucleoside metabolic process
B	0042802	molecular_function	identical protein binding
B	0047975	molecular_function	guanosine phosphorylase activity
C	0003824	molecular_function	catalytic activity
C	0004731	molecular_function	purine-nucleoside phosphorylase activity
C	0005829	cellular_component	cytosol
C	0006139	biological_process	nucleobase-containing compound metabolic process
C	0006152	biological_process	purine nucleoside catabolic process
C	0006974	biological_process	DNA damage response
C	0009116	biological_process	nucleoside metabolic process
C	0009164	biological_process	nucleoside catabolic process
C	0016020	cellular_component	membrane
C	0016757	molecular_function	glycosyltransferase activity
C	0016763	molecular_function	pentosyltransferase activity
C	0019686	biological_process	purine nucleoside interconversion
C	0042278	biological_process	purine nucleoside metabolic process
C	0042802	molecular_function	identical protein binding
C	0047975	molecular_function	guanosine phosphorylase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	17
Details	BINDING SITE FOR RESIDUE FMC A 300

Chain	Residue
A	ARG87
A	SER203
A	ASP204
A	PO4301
A	HOH304
A	HOH325
A	HOH611
C	HIS4
C	ARG43
A	SER90
A	CYS91
A	GLY92
A	PHE159
A	VAL178
A	GLU179
A	MET180
A	GLU181

site_id	AC2
Number of Residues	8
Details	BINDING SITE FOR RESIDUE PO4 A 301

Chain	Residue
A	PRO19
A	GLY20
A	ARG24
A	ARG87
A	GLY89
A	SER90
A	FMC300
C	ARG43

site_id	AC3
Number of Residues	17
Details	BINDING SITE FOR RESIDUE FMC B 300

Chain	Residue
B	HIS4
B	MET64
B	ARG87
B	SER90
B	CYS91
B	GLY92
B	PHE159
B	VAL178
B	GLU179
B	MET180
B	GLU181
B	ASP204
B	ILE206
B	HOH244
B	HOH465
B	HOH466
B	HOH549

site_id	AC4
Number of Residues	9
Details	BINDING SITE FOR RESIDUE PO4 B 301

Chain	Residue
B	GLY20
B	ASP21
B	VAL88
B	GLY89
B	SER90
B	HOH244
B	HOH282
B	PO4302
B	HOH549

site_id	AC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PO4 B 302

Chain	Residue
B	ASP21
B	ARG24
B	ARG217
B	PO4301

site_id	AC6
Number of Residues	16
Details	BINDING SITE FOR RESIDUE FMC C 300

Chain	Residue
A	HIS4
C	ARG87
C	SER90
C	CYS91
C	GLY92
C	PHE159
C	VAL178
C	GLU179
C	MET180
C	GLU181
C	ASP204
C	ILE206
C	HOH286
C	HOH296
C	HOH318
C	HOH362

site_id	AC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PO4 C 301

Chain	Residue
C	ASP21
C	ARG24
C	PO4302
C	HOH341
C	HOH371

site_id	AC8
Number of Residues	13
Details	BINDING SITE FOR RESIDUE PO4 C 302

Chain	Residue
C	PRO19
C	GLY20
C	ASP21
C	ARG24
C	VAL88
C	GLY89
C	SER90
C	PHE221
C	HOH264
C	HOH286
C	HOH296
C	PO4301
C	HOH502

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

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	3
Details	ACT_SITE: Proton donor => ECO:0000255\|HAMAP-Rule:MF_01627, ECO:0000269\|PubMed:30337572

Chain	Residue	Details
A	ASP204
B	ASP204
C	ASP204

site_id	SWS_FT_FI2
Number of Residues	3
Details	BINDING: BINDING => ECO:0000305\|PubMed:30337572, ECO:0007744\|PDB:4TS3, ECO:0007744\|PDB:4TS9, ECO:0007744\|PDB:4TTA, ECO:0007744\|PDB:4TTI, ECO:0007744\|PDB:4TTJ

Chain	Residue	Details
A	HIS4
B	HIS4
C	HIS4

site_id	SWS_FT_FI3
Number of Residues	9
Details	BINDING: in other chain => ECO:0000269\|PubMed:11786017, ECO:0000269\|PubMed:21672603, ECO:0000269\|PubMed:30337572, ECO:0007744\|PDB:1K9S, ECO:0007744\|PDB:3ONV, ECO:0007744\|PDB:3OOE, ECO:0007744\|PDB:3OOH, ECO:0007744\|PDB:3OPV, ECO:0007744\|PDB:4TS3, ECO:0007744\|PDB:4TS9, ECO:0007744\|PDB:4TTA, ECO:0007744\|PDB:4TTI, ECO:0007744\|PDB:4TTJ

Chain	Residue	Details
B	GLY20
B	ARG24
B	ARG87
C	GLY20
C	ARG24
C	ARG87
A	GLY20
A	ARG24
A	ARG87

site_id	SWS_FT_FI4
Number of Residues	3
Details	BINDING: BINDING => ECO:0000269\|PubMed:11786017, ECO:0000269\|PubMed:21672603, ECO:0000269\|PubMed:30337572, ECO:0007744\|PDB:1K9S, ECO:0007744\|PDB:3ONV, ECO:0007744\|PDB:3OOE, ECO:0007744\|PDB:3OOH, ECO:0007744\|PDB:3OPV, ECO:0007744\|PDB:4TS3, ECO:0007744\|PDB:4TS9, ECO:0007744\|PDB:4TTA, ECO:0007744\|PDB:4TTI, ECO:0007744\|PDB:4TTJ

Chain	Residue	Details
C	ARG43
A	ARG43
B	ARG43

site_id	SWS_FT_FI5
Number of Residues	6
Details	BINDING: in other chain => ECO:0000305\|PubMed:30337572, ECO:0007744\|PDB:4TS3, ECO:0007744\|PDB:4TS9, ECO:0007744\|PDB:4TTA, ECO:0007744\|PDB:4TTI, ECO:0007744\|PDB:4TTJ

Chain	Residue	Details
B	SER203
C	GLU179
C	SER203
B	GLU179
A	GLU179
A	SER203

site_id	SWS_FT_FI6
Number of Residues	3
Details	SITE: Important for catalytic activity => ECO:0000255\|HAMAP-Rule:MF_01627, ECO:0000269\|PubMed:21672603, ECO:0000269\|PubMed:30337572

Chain	Residue	Details
A	ARG217
B	ARG217
C	ARG217

site_id	SWS_FT_FI7
Number of Residues	3
Details	MOD_RES: N6-acetyllysine => ECO:0000269\|PubMed:18723842

Chain	Residue	Details
A	LYS26
B	LYS26
C	LYS26

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	7
Details	M-CSA 375

Chain	Residue	Details
A	GLY20	electrostatic stabiliser
A	ARG24	electrostatic stabiliser
A	ARG43	electrostatic stabiliser
A	ARG87	electrostatic stabiliser
A	SER90	electrostatic stabiliser
A	ASP204	proton shuttle (general acid/base)
A	ARG217	enhance reactivity

site_id	MCSA2
Number of Residues	7
Details	M-CSA 375

Chain	Residue	Details
B	GLY20	electrostatic stabiliser
B	ARG24	electrostatic stabiliser
B	ARG43	electrostatic stabiliser
B	ARG87	electrostatic stabiliser
B	SER90	electrostatic stabiliser
B	ASP204	proton shuttle (general acid/base)
B	ARG217	enhance reactivity

site_id	MCSA3
Number of Residues	7
Details	M-CSA 375

Chain	Residue	Details
C	GLY20	electrostatic stabiliser
C	ARG24	electrostatic stabiliser
C	ARG43	electrostatic stabiliser
C	ARG87	electrostatic stabiliser
C	SER90	electrostatic stabiliser
C	ASP204	proton shuttle (general acid/base)
C	ARG217	enhance reactivity

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)