1YRY

Crystal structure of human PNP complexed with MESG

Functional Information from GO Data

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 E 291

Chain	Residue
E	PRO92
E	GLN144
E	ARG148
E	HOH399

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site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 E 292

Chain	Residue
E	GLY34
E	LEU35
E	GLY36
E	GLN82
E	HOH317

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site_id	AC3
Number of Residues	8
Details	BINDING SITE FOR RESIDUE SO4 E 293

Chain	Residue
E	GLY32
E	SER33
E	ARG84
E	HIS86
E	ASN115
E	ALA116
E	SER220
E	MSG290

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site_id	AC4
Number of Residues	18
Details	BINDING SITE FOR RESIDUE MSG E 290

Chain	Residue
E	SER33
E	HIS86
E	TYR88
E	ALA116
E	ALA117
E	GLY118
E	PHE159
E	PHE200
E	GLU201
E	VAL217
E	GLY218
E	MET219
E	THR242
E	ASN243
E	VAL245
E	HIS257
E	SO4293
E	HOH370

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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
E	VAL79-LEU120

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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
E	SER33

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

Chain	Residue	Details
E	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
E	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
E	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
E	ALA116
E	GLU201
E	SER220
E	ASN243

---

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

Chain	Residue	Details
E	MET219
E	HIS257

---

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

Chain	Residue	Details
E	ASN243

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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
E	MET1

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

Chain	Residue	Details
E	SER251

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Catalytic Information from CSA

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

Chain	Residue	Details
E	ASN243
E	HIS86
E	GLU89

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site_id	MCSA1
Number of Residues	10
Details	M-CSA 17

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

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