Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3BGS

Structure of human purine nucleoside phosphorylase with L-DADMe-ImmH and phosphate

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000255	biological_process	allantoin metabolic process
A	0001882	molecular_function	nucleoside binding
A	0002060	molecular_function	purine nucleobase binding
A	0003824	molecular_function	catalytic activity
A	0004731	molecular_function	purine-nucleoside phosphorylase activity
A	0005515	molecular_function	protein binding
A	0005576	cellular_component	extracellular region
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006139	biological_process	nucleobase-containing compound metabolic process
A	0006148	biological_process	inosine catabolic process
A	0006149	biological_process	deoxyinosine catabolic process
A	0006157	biological_process	deoxyadenosine catabolic process
A	0006166	biological_process	purine ribonucleoside salvage
A	0006204	biological_process	IMP catabolic process
A	0006738	biological_process	nicotinamide riboside catabolic process
A	0006955	biological_process	immune response
A	0009116	biological_process	nucleoside metabolic process
A	0009165	biological_process	nucleotide biosynthetic process
A	0009410	biological_process	response to xenobiotic stimulus
A	0016757	molecular_function	glycosyltransferase activity
A	0016763	molecular_function	pentosyltransferase activity
A	0032743	biological_process	positive regulation of interleukin-2 production
A	0034418	biological_process	urate biosynthetic process
A	0034774	cellular_component	secretory granule lumen
A	0042102	biological_process	positive regulation of T cell proliferation
A	0042301	molecular_function	phosphate ion binding
A	0042802	molecular_function	identical protein binding
A	0043101	biological_process	purine-containing compound salvage
A	0046059	biological_process	dAMP catabolic process
A	0046638	biological_process	positive regulation of alpha-beta T cell differentiation
A	0047975	molecular_function	guanosine phosphorylase activity
A	0070062	cellular_component	extracellular exosome
A	1904813	cellular_component	ficolin-1-rich granule lumen

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PO4 A 302

Chain	Residue
A	GLU153
A	ASP157
A	ARG158
A	HIS257
A	HOH318

site_id	AC2
Number of Residues	10
Details	BINDING SITE FOR RESIDUE PO4 A 303

Chain	Residue
A	ASN115
A	ALA116
A	SER220
A	DIH301
A	HOH346
A	HOH376
A	GLY32
A	SER33
A	ARG84
A	HIS86

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PO4 A 304

Chain	Residue
A	PRO92
A	GLN144
A	ARG148
A	HOH317
A	HOH373

site_id	AC4
Number of Residues	16
Details	BINDING SITE FOR RESIDUE DIH A 301

Chain	Residue
A	TYR88
A	ALA116
A	ALA117
A	GLY118
A	PHE159
A	PHE200
A	GLU201
A	VAL217
A	GLY218
A	MET219
A	THR242
A	ASN243
A	HIS257
A	VAL260
A	PO4303
A	HOH335

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	VAL79-LEU120

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	BINDING: BINDING => ECO:0000269\|PubMed:23438750, ECO:0000305\|PubMed:14706628, ECO:0000305\|PubMed:1763067, ECO:0007744\|PDB:1RCT, ECO:0007744\|PDB:1ULA, ECO:0007744\|PDB:1ULB, ECO:0007744\|PDB:4EAR, ECO:0007744\|PDB:4EB8, ECO:0007744\|PDB:4GKA

Chain	Residue	Details
A	SER33

site_id	SWS_FT_FI2
Number of Residues	1
Details	BINDING: BINDING => ECO:0000250\|UniProtKB:P55859

Chain	Residue	Details
A	HIS64

site_id	SWS_FT_FI3
Number of Residues	1
Details	BINDING: BINDING => ECO:0000269\|PubMed:23438750, ECO:0000305\|PubMed:14706628, ECO:0000305\|PubMed:1763067, ECO:0007744\|PDB:1RCT, ECO:0007744\|PDB:1ULA, ECO:0007744\|PDB:1ULB, ECO:0007744\|PDB:1V3Q, ECO:0007744\|PDB:4EAR, ECO:0007744\|PDB:4EB8, ECO:0007744\|PDB:4GKA

Chain	Residue	Details
A	ARG84

site_id	SWS_FT_FI4
Number of Residues	1
Details	BINDING: BINDING => ECO:0000269\|PubMed:14706628, ECO:0000269\|PubMed:23438750, ECO:0007744\|PDB:1RCT, ECO:0007744\|PDB:4EAR, ECO:0007744\|PDB:4EB8

Chain	Residue	Details
A	TYR88

site_id	SWS_FT_FI5
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269\|PubMed:14706628, ECO:0000269\|PubMed:23438750, ECO:0000305\|PubMed:1763067, ECO:0007744\|PDB:1RCT, ECO:0007744\|PDB:1ULB, ECO:0007744\|PDB:4EAR, ECO:0007744\|PDB:4EB8, ECO:0007744\|PDB:4GKA

Chain	Residue	Details
A	SER220
A	ASN243
A	ALA116
A	GLU201

site_id	SWS_FT_FI6
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269\|PubMed:14706628, ECO:0007744\|PDB:1RCT

Chain	Residue	Details
A	MET219
A	HIS257

site_id	SWS_FT_FI7
Number of Residues	1
Details	SITE: Important for substrate specificity => ECO:0000269\|PubMed:9305964

Chain	Residue	Details
A	ASN243

site_id	SWS_FT_FI8
Number of Residues	1
Details	MOD_RES: N-acetylmethionine => ECO:0000269\|Ref.8, ECO:0007744\|PubMed:19413330, ECO:0007744\|PubMed:22223895

Chain	Residue	Details
A	MET1

site_id	SWS_FT_FI9
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0007744\|PubMed:23186163

Chain	Residue	Details
A	SER251

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	10
Details	M-CSA 17

Chain	Residue	Details
A	SER33	hydrogen bond donor
A	HIS64	electrostatic stabiliser
A	HIS86	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
A	TYR88	electrostatic stabiliser, hydrogen bond donor
A	GLU89	activator, electrostatic stabiliser, hydrogen bond acceptor
A	ALA116	electrostatic stabiliser, hydrogen bond donor
A	MET219	electrostatic stabiliser, hydrogen bond donor
A	SER220	electrostatic stabiliser, hydrogen bond donor
A	ASN243	electrostatic stabiliser, hydrogen bond donor, polar interaction
A	HIS257	electrostatic stabiliser, hydrogen bond acceptor

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