Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3FUC

Recombinant calf purine nucleoside phosphorylase in a binary complex with multisubstrate analogue inhibitor 9-(5',5'-difluoro-5'-phosphonopentyl)-9-deazaguanine structure in a new space group with one 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	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	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	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

Functional Information from PDB Data

site_id	AC1
Number of Residues	21
Details	BINDING SITE FOR RESIDUE 9D9 A 301

Chain	Residue
A	SER33
A	PHE200
A	GLU201
A	VAL217
A	GLY218
A	MET219
A	SER220
A	THR242
A	ASN243
A	VAL245
A	HOH428
A	ARG84
A	HOH440
A	HOH556
A	HIS86
A	TYR88
A	ASN115
A	ALA116
A	ALA117
A	GLY118
A	LEU195

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG A 302

Chain	Residue
A	GLU186
A	HOH425
A	HOH503
A	HOH549
B	GLU186
B	HOH626

site_id	AC3
Number of Residues	20
Details	BINDING SITE FOR RESIDUE 9D9 B 301

Chain	Residue
B	SER33
B	ARG84
B	HIS86
B	TYR88
B	ASN115
B	ALA116
B	ALA117
B	GLY118
B	LEU195
B	PHE200
B	GLU201
B	VAL217
B	GLY218
B	MET219
B	SER220
B	THR242
B	ASN243
B	HOH510
B	HOH533
B	HOH619

site_id	AC4
Number of Residues	21
Details	BINDING SITE FOR RESIDUE 9D9 C 301

Chain	Residue
C	SER33
C	ARG84
C	HIS86
C	TYR88
C	ASN115
C	ALA116
C	ALA117
C	GLY118
C	LEU195
C	PHE200
C	GLU201
C	VAL217
C	GLY218
C	MET219
C	SER220
C	THR242
C	ASN243
C	VAL245
C	HOH401
C	HOH486
C	HOH493

site_id	AC5
Number of Residues	8
Details	BINDING SITE FOR RESIDUE MG C 302

Chain	Residue
C	ASP9
C	ASP9
C	HOH407
C	HOH407
C	HOH511
C	HOH511
C	HOH530
C	HOH530

site_id	AC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG C 303

Chain	Residue
C	GLU186
C	GLU186
C	HOH504
C	HOH504
C	HOH505
C	HOH505

site_id	AC7
Number of Residues	2
Details	BINDING SITE FOR RESIDUE AZI C 304

Chain	Residue
C	PRO92
C	LYS95

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	3
Details	BINDING: BINDING => ECO:0000269\|PubMed:9585525, ECO:0007744\|PDB:1A9O, ECO:0007744\|PDB:1A9P, ECO:0007744\|PDB:1A9S, ECO:0007744\|PDB:1A9T, ECO:0007744\|PDB:3PNP, ECO:0007744\|PDB:4PNP

Chain	Residue	Details
A	SER33
B	SER33
C	SER33

site_id	SWS_FT_FI2
Number of Residues	3
Details	BINDING: BINDING => ECO:0000269\|PubMed:9585525, ECO:0007744\|PDB:1A9P, ECO:0007744\|PDB:1A9T, ECO:0007744\|PDB:3PNP, ECO:0007744\|PDB:4PNP

Chain	Residue	Details
A	HIS64
B	HIS64
C	HIS64

site_id	SWS_FT_FI3
Number of Residues	9
Details	BINDING: BINDING => ECO:0000269\|PubMed:9585525, ECO:0007744\|PDB:1A9O, ECO:0007744\|PDB:1A9P, ECO:0007744\|PDB:1A9Q, ECO:0007744\|PDB:1A9R, ECO:0007744\|PDB:1A9S, ECO:0007744\|PDB:1A9T, ECO:0007744\|PDB:3PNP, ECO:0007744\|PDB:4PNP

Chain	Residue	Details
A	ARG84
A	ALA116
A	SER220
B	ARG84
B	ALA116
B	SER220
C	ARG84
C	ALA116
C	SER220

site_id	SWS_FT_FI4
Number of Residues	9
Details	BINDING: BINDING => ECO:0000269\|PubMed:9585525, ECO:0007744\|PDB:1A9P, ECO:0007744\|PDB:1A9S, ECO:0007744\|PDB:1A9T

Chain	Residue	Details
A	TYR88
A	MET219
A	HIS257
B	TYR88
B	MET219
B	HIS257
C	TYR88
C	MET219
C	HIS257

site_id	SWS_FT_FI5
Number of Residues	6
Details	BINDING: BINDING => ECO:0000269\|PubMed:9585525, ECO:0000305\|PubMed:9020983, ECO:0007744\|PDB:1A9P, ECO:0007744\|PDB:1A9Q, ECO:0007744\|PDB:1A9R, ECO:0007744\|PDB:1VFN

Chain	Residue	Details
A	GLU201
A	ASN243
B	GLU201
B	ASN243
C	GLU201
C	ASN243

site_id	SWS_FT_FI6
Number of Residues	3
Details	SITE: Important for substrate specificity => ECO:0000250\|UniProtKB:P00491

Chain	Residue	Details
A	ASN243
B	ASN243
C	ASN243

site_id	SWS_FT_FI7
Number of Residues	3
Details	MOD_RES: N-acetylmethionine => ECO:0000250\|UniProtKB:P00491

Chain	Residue	Details
A	MET1
B	MET1
C	MET1

site_id	SWS_FT_FI8
Number of Residues	3
Details	MOD_RES: Phosphoserine => ECO:0000250\|UniProtKB:P00491

Chain	Residue	Details
A	SER251
B	SER251
C	SER251

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