Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1LVU

Crystal structure of calf spleen purine nucleoside phosphorylase in a new space group with full trimer in the asymmetric unit

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0004731	molecular_function	purine-nucleoside phosphorylase activity
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006139	biological_process	nucleobase-containing compound metabolic process
A	0006166	biological_process	purine ribonucleoside salvage
A	0009116	biological_process	nucleoside metabolic process
A	0016740	molecular_function	transferase activity
A	0016757	molecular_function	glycosyltransferase activity
A	0016763	molecular_function	pentosyltransferase activity
A	0047975	molecular_function	guanosine phosphorylase activity
B	0003824	molecular_function	catalytic activity
B	0004731	molecular_function	purine-nucleoside phosphorylase activity
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0006139	biological_process	nucleobase-containing compound metabolic process
B	0006166	biological_process	purine ribonucleoside salvage
B	0009116	biological_process	nucleoside metabolic process
B	0016740	molecular_function	transferase activity
B	0016757	molecular_function	glycosyltransferase activity
B	0016763	molecular_function	pentosyltransferase activity
B	0047975	molecular_function	guanosine phosphorylase activity
C	0003824	molecular_function	catalytic activity
C	0004731	molecular_function	purine-nucleoside phosphorylase activity
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
C	0006139	biological_process	nucleobase-containing compound metabolic process
C	0006166	biological_process	purine ribonucleoside salvage
C	0009116	biological_process	nucleoside metabolic process
C	0016740	molecular_function	transferase activity
C	0016757	molecular_function	glycosyltransferase activity
C	0016763	molecular_function	pentosyltransferase activity
C	0047975	molecular_function	guanosine phosphorylase activity
D	0003824	molecular_function	catalytic activity
D	0004731	molecular_function	purine-nucleoside phosphorylase activity
D	0005737	cellular_component	cytoplasm
D	0005829	cellular_component	cytosol
D	0006139	biological_process	nucleobase-containing compound metabolic process
D	0006166	biological_process	purine ribonucleoside salvage
D	0009116	biological_process	nucleoside metabolic process
D	0016740	molecular_function	transferase activity
D	0016757	molecular_function	glycosyltransferase activity
D	0016763	molecular_function	pentosyltransferase activity
D	0047975	molecular_function	guanosine phosphorylase activity
E	0003824	molecular_function	catalytic activity
E	0004731	molecular_function	purine-nucleoside phosphorylase activity
E	0005737	cellular_component	cytoplasm
E	0005829	cellular_component	cytosol
E	0006139	biological_process	nucleobase-containing compound metabolic process
E	0006166	biological_process	purine ribonucleoside salvage
E	0009116	biological_process	nucleoside metabolic process
E	0016740	molecular_function	transferase activity
E	0016757	molecular_function	glycosyltransferase activity
E	0016763	molecular_function	pentosyltransferase activity
E	0047975	molecular_function	guanosine phosphorylase activity
F	0003824	molecular_function	catalytic activity
F	0004731	molecular_function	purine-nucleoside phosphorylase activity
F	0005737	cellular_component	cytoplasm
F	0005829	cellular_component	cytosol
F	0006139	biological_process	nucleobase-containing compound metabolic process
F	0006166	biological_process	purine ribonucleoside salvage
F	0009116	biological_process	nucleoside metabolic process
F	0016740	molecular_function	transferase activity
F	0016757	molecular_function	glycosyltransferase activity
F	0016763	molecular_function	pentosyltransferase activity
F	0047975	molecular_function	guanosine phosphorylase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA A 8001

Chain	Residue
A	SER51
A	GLU58
A	HOH8018
A	HOH8022
A	HOH8094
D	GLU58

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA D 8002

Chain	Residue
D	HOH8044
D	HOH8058
D	HOH8154
A	GLU58
D	SER51
D	GLU58

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA F 8003

Chain	Residue
B	GLU1058
B	HOH8073
F	HOH204
F	HOH306
F	SER2051
F	GLU2058

site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA B 8004

Chain	Residue
B	SER1051
B	GLU1058
B	HOH8022
B	HOH8052
B	HOH8071
F	GLU2058

site_id	AC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA C 8005

Chain	Residue
C	HOH117
C	HOH355
C	SER2051
C	GLU2058
E	GLU1058
E	HOH8072

site_id	AC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA E 8006

Chain	Residue
C	GLU2058
E	SER1051
E	GLU1058
E	HOH8042
E	HOH8059
E	HOH8090

site_id	AC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA B 8007

Chain	Residue
B	ASP1215
B	HOH8043
B	HOH8244
B	HOH8337
D	GLU250

site_id	AC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA F 8008

Chain	Residue
C	GLU2250
F	HOH76
F	HOH582
F	ASN2121
F	ASP2215

site_id	AC9
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA A 8009

Chain	Residue
A	GLU8
A	HOH8082
A	HOH8091
E	GLU1008
E	HOH8032
E	HOH8274

site_id	BC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA B 8010

Chain	Residue
B	GLU1008
B	HOH8037
B	HOH8131
D	GLU8
D	HOH8033
D	HOH8131

site_id	BC2
Number of Residues	20
Details	BINDING SITE FOR RESIDUE 9PP A 6100

Chain	Residue
A	GLY32
A	SER33
A	HIS86
A	ASN115
A	ALA116
A	GLY118
A	LEU195
A	PHE200
A	GLU201
A	VAL217
A	GLY218
A	MET219
A	SER220
A	ASN243
A	HOH8034
A	HOH8048
A	HOH8070
A	HOH8092
A	HOH8131
A	HOH8162

site_id	BC3
Number of Residues	21
Details	BINDING SITE FOR RESIDUE 9PP B 6200

Chain	Residue
B	GLY1032
B	SER1033
B	ARG1084
B	HIS1086
B	ASN1115
B	ALA1116
B	ALA1117
B	GLY1118
B	LEU1195
B	PHE1200
B	GLU1201
B	VAL1217
B	GLY1218
B	MET1219
B	SER1220
B	ASN1243
B	HOH8012
B	HOH8057
B	HOH8092
B	HOH8105
B	HOH8119

site_id	BC4
Number of Residues	20
Details	BINDING SITE FOR RESIDUE 9PP C 6300

Chain	Residue
C	HOH134
C	HOH326
C	HOH483
C	HOH707
C	HOH1653
C	GLY2032
C	SER2033
C	ARG2084
C	HIS2086
C	ASN2115
C	ALA2116
C	ALA2117
C	GLY2118
C	PHE2200
C	GLU2201
C	VAL2217
C	GLY2218
C	MET2219
C	SER2220
C	ASN2243

site_id	BC5
Number of Residues	20
Details	BINDING SITE FOR RESIDUE 9PP D 6400

Chain	Residue
D	GLY32
D	SER33
D	HIS86
D	ASN115
D	ALA116
D	ALA117
D	GLY118
D	LEU195
D	PHE200
D	GLU201
D	VAL217
D	GLY218
D	MET219
D	SER220
D	ASN243
D	HOH8019
D	HOH8024
D	HOH8056
D	HOH8083
D	HOH8123

site_id	BC6
Number of Residues	22
Details	BINDING SITE FOR RESIDUE 9PP E 6500

Chain	Residue
E	GLY1032
E	SER1033
E	ARG1084
E	HIS1086
E	ASN1115
E	ALA1116
E	ALA1117
E	GLY1118
E	LEU1195
E	PHE1200
E	GLU1201
E	VAL1217
E	GLY1218
E	MET1219
E	SER1220
E	ASN1243
E	HOH8016
E	HOH8022
E	HOH8030
E	HOH8051
E	HOH8056
F	PHE2159

site_id	BC7
Number of Residues	19
Details	BINDING SITE FOR RESIDUE 9PP F 6600

Chain	Residue
F	HOH157
F	HOH276
F	HOH279
F	HOH860
F	GLY2032
F	SER2033
F	HIS2086
F	ASN2115
F	ALA2116
F	ALA2117
F	GLY2118
F	LEU2195
F	PHE2200
F	GLU2201
F	VAL2217
F	GLY2218
F	MET2219
F	SER2220
F	ASN2243

Functional Information from PROSITE/UniProt

site_id	PS01240
Number of Residues	42
Details	PNP_MTAP_2 Purine and other phosphorylases family 2 signature. VmmqGrfHmYegypFwkvTfpVrVfrllGvet.LVvtNAaGGL

Chain	Residue	Details
A	VAL79-LEU120

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	6
Details	Binding site: {"evidences":[{"source":"PubMed","id":"9585525","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1A9O","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1A9P","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1A9S","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1A9T","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3PNP","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4PNP","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	6
Details	Binding site: {"evidences":[{"source":"PubMed","id":"9585525","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1A9P","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1A9T","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3PNP","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4PNP","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	24
Details	Binding site: {"evidences":[{"source":"PubMed","id":"9585525","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1A9O","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1A9P","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1A9Q","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1A9R","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1A9S","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1A9T","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3PNP","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4PNP","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	14
Details	Binding site: {"evidences":[{"source":"PubMed","id":"9585525","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1A9P","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1A9S","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1A9T","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	12
Details	Binding site: {"evidences":[{"source":"PubMed","id":"9585525","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9020983","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"1A9P","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1A9Q","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1A9R","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1VFN","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	6
Details	Site: {"description":"Important for substrate specificity","evidences":[{"source":"UniProtKB","id":"P00491","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	2
Details	Modified residue: {"description":"N-acetylmethionine","evidences":[{"source":"UniProtKB","id":"P00491","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P00491","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	CSA1
Number of Residues	3
Details	Annotated By Reference To The Literature 1cg6

Chain	Residue	Details
A	ASN243
A	HIS86
A	GLU89

site_id	CSA2
Number of Residues	3
Details	Annotated By Reference To The Literature 1cg6

Chain	Residue	Details
B	ASN1243
B	GLU1089
B	HIS1086

site_id	CSA3
Number of Residues	3
Details	Annotated By Reference To The Literature 1cg6

Chain	Residue	Details
C	HIS2086
C	ASN2243
C	GLU2089

site_id	CSA4
Number of Residues	3
Details	Annotated By Reference To The Literature 1cg6

Chain	Residue	Details
D	ASN243
D	HIS86
D	GLU89

site_id	CSA5
Number of Residues	3
Details	Annotated By Reference To The Literature 1cg6

Chain	Residue	Details
E	ASN1243
E	GLU1089
E	HIS1086

site_id	CSA6
Number of Residues	3
Details	Annotated By Reference To The Literature 1cg6

Chain	Residue	Details
F	HIS2086
F	ASN2243
F	GLU2089

site_id	CSA7
Number of Residues	2
Details	Annotated By Reference To The Literature 1cg6

Chain	Residue	Details
A	ASN243
A	ASP248

site_id	CSA8
Number of Residues	2
Details	Annotated By Reference To The Literature 1cg6

Chain	Residue	Details
B	ASP1248
B	ASN1243

site_id	CSA9
Number of Residues	2
Details	Annotated By Reference To The Literature 1cg6

Chain	Residue	Details
C	ASN2243
C	ASP2248

site_id	CSA10
Number of Residues	2
Details	Annotated By Reference To The Literature 1cg6

Chain	Residue	Details
D	ASN243
D	ASP248

site_id	CSA11
Number of Residues	2
Details	Annotated By Reference To The Literature 1cg6

Chain	Residue	Details
E	ASP1248
E	ASN1243

site_id	CSA12
Number of Residues	2
Details	Annotated By Reference To The Literature 1cg6

Chain	Residue	Details
F	ASN2243
F	ASP2248

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)