1D6N

TERNARY COMPLEX STRUCTURE OF HUMAN HGPRTASE, PRPP, MG2+, AND THE INHIBITOR HPP REVEALS THE INVOLVEMENT OF THE FLEXIBLE LOOP IN SUBSTRATE BINDING

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0000287	molecular_function	magnesium ion binding
A	0004422	molecular_function	hypoxanthine phosphoribosyltransferase activity
A	0005515	molecular_function	protein binding
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006164	biological_process	purine nucleotide biosynthetic process
A	0006166	biological_process	purine ribonucleoside salvage
A	0006178	biological_process	guanine salvage
A	0016740	molecular_function	transferase activity
A	0016757	molecular_function	glycosyltransferase activity
A	0032263	biological_process	GMP salvage
A	0032264	biological_process	IMP salvage
A	0042802	molecular_function	identical protein binding
A	0043103	biological_process	hypoxanthine salvage
A	0044209	biological_process	AMP salvage
A	0045964	biological_process	positive regulation of dopamine metabolic process
A	0046038	biological_process	GMP catabolic process
A	0046040	biological_process	IMP metabolic process
A	0046100	biological_process	hypoxanthine metabolic process
A	0046872	molecular_function	metal ion binding
A	0051289	biological_process	protein homotetramerization
A	0052657	molecular_function	guanine phosphoribosyltransferase activity
A	0070062	cellular_component	extracellular exosome
B	0000166	molecular_function	nucleotide binding
B	0000287	molecular_function	magnesium ion binding
B	0004422	molecular_function	hypoxanthine phosphoribosyltransferase activity
B	0005515	molecular_function	protein binding
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0006164	biological_process	purine nucleotide biosynthetic process
B	0006166	biological_process	purine ribonucleoside salvage
B	0006178	biological_process	guanine salvage
B	0016740	molecular_function	transferase activity
B	0016757	molecular_function	glycosyltransferase activity
B	0032263	biological_process	GMP salvage
B	0032264	biological_process	IMP salvage
B	0042802	molecular_function	identical protein binding
B	0043103	biological_process	hypoxanthine salvage
B	0044209	biological_process	AMP salvage
B	0045964	biological_process	positive regulation of dopamine metabolic process
B	0046038	biological_process	GMP catabolic process
B	0046040	biological_process	IMP metabolic process
B	0046100	biological_process	hypoxanthine metabolic process
B	0046872	molecular_function	metal ion binding
B	0051289	biological_process	protein homotetramerization
B	0052657	molecular_function	guanine phosphoribosyltransferase activity
B	0070062	cellular_component	extracellular exosome

Functional Information from PROSITE/UniProt

site_id	PS00103
Number of Residues	13
Details	PUR_PYR_PR_TRANSFER Purine/pyrimidine phosphoribosyl transferases signature. VLIVEDIIDTGkT

Chain	Residue	Details
A	VAL129-THR141

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	Active site: {"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	24
Details	Binding site: {"evidences":[{"source":"PubMed","id":"8044844","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	2
Details	Binding site: {}

Chain

Residue

Details

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site_id	SWS_FT_FI4
Number of Residues	2
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P00493","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI5
Number of Residues	2
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P27605","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI6
Number of Residues	4
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate","evidences":[{"source":"PubMed","id":"28112733","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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Catalytic Information from CSA

site_id	CSA1
Number of Residues	4
Details	Annotated By Reference To The Literature 1a95

Chain	Residue	Details
A	GLU133
A	ASP134
A	ASP137
A	LYS165

---

site_id	CSA2
Number of Residues	4
Details	Annotated By Reference To The Literature 1a95

Chain	Residue	Details
B	GLU133
B	ASP134
B	ASP137
B	LYS165

---

site_id	CSA3
Number of Residues	5
Details	Annotated By Reference To The Literature 1a95

Chain	Residue	Details
A	GLU133
A	ASP134
A	ARG169
A	ASP137
A	LYS165

---

site_id	CSA4
Number of Residues	5
Details	Annotated By Reference To The Literature 1a95

Chain	Residue	Details
B	GLU133
B	ASP134
B	ARG169
B	ASP137
B	LYS165

---

site_id	MCSA1
Number of Residues	5
Details	M-CSA 48

Chain	Residue	Details
A	GLU133	attractive charge-charge interaction, electrostatic stabiliser
A	ASP134	attractive charge-charge interaction, electrostatic stabiliser
A	ASP137	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
A	PHE186	electrostatic stabiliser
A	ARG199	electrostatic stabiliser

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site_id	MCSA2
Number of Residues	5
Details	M-CSA 48

Chain	Residue	Details
B	GLU133	attractive charge-charge interaction, electrostatic stabiliser
B	ASP134	attractive charge-charge interaction, electrostatic stabiliser
B	ASP137	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
B	PHE186	electrostatic stabiliser
B	ARG199	electrostatic stabiliser

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