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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
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0000287molecular_functionmagnesium ion binding
A0001913biological_processT cell mediated cytotoxicity
A0001975biological_processresponse to amphetamine
A0004422molecular_functionhypoxanthine phosphoribosyltransferase activity
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006164biological_processpurine nucleotide biosynthetic process
A0006166biological_processpurine ribonucleoside salvage
A0006178biological_processguanine salvage
A0007625biological_processgrooming behavior
A0007626biological_processlocomotory behavior
A0016740molecular_functiontransferase activity
A0016757molecular_functionglycosyltransferase activity
A0021756biological_processstriatum development
A0021895biological_processcerebral cortex neuron differentiation
A0021954biological_processcentral nervous system neuron development
A0032263biological_processGMP salvage
A0032264biological_processIMP salvage
A0042417biological_processdopamine metabolic process
A0042802molecular_functionidentical protein binding
A0043103biological_processhypoxanthine salvage
A0044209biological_processAMP salvage
A0045964biological_processpositive regulation of dopamine metabolic process
A0046038biological_processGMP catabolic process
A0046040biological_processIMP metabolic process
A0046083biological_processadenine metabolic process
A0046100biological_processhypoxanthine metabolic process
A0046651biological_processlymphocyte proliferation
A0046872molecular_functionmetal ion binding
A0048813biological_processdendrite morphogenesis
A0051289biological_processprotein homotetramerization
A0052657molecular_functionguanine phosphoribosyltransferase activity
A0070062cellular_componentextracellular exosome
A0071542biological_processdopaminergic neuron differentiation
B0000166molecular_functionnucleotide binding
B0000287molecular_functionmagnesium ion binding
B0001913biological_processT cell mediated cytotoxicity
B0001975biological_processresponse to amphetamine
B0004422molecular_functionhypoxanthine phosphoribosyltransferase activity
B0005515molecular_functionprotein binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006164biological_processpurine nucleotide biosynthetic process
B0006166biological_processpurine ribonucleoside salvage
B0006178biological_processguanine salvage
B0007625biological_processgrooming behavior
B0007626biological_processlocomotory behavior
B0016740molecular_functiontransferase activity
B0016757molecular_functionglycosyltransferase activity
B0021756biological_processstriatum development
B0021895biological_processcerebral cortex neuron differentiation
B0021954biological_processcentral nervous system neuron development
B0032263biological_processGMP salvage
B0032264biological_processIMP salvage
B0042417biological_processdopamine metabolic process
B0042802molecular_functionidentical protein binding
B0043103biological_processhypoxanthine salvage
B0044209biological_processAMP salvage
B0045964biological_processpositive regulation of dopamine metabolic process
B0046038biological_processGMP catabolic process
B0046040biological_processIMP metabolic process
B0046083biological_processadenine metabolic process
B0046100biological_processhypoxanthine metabolic process
B0046651biological_processlymphocyte proliferation
B0046872molecular_functionmetal ion binding
B0048813biological_processdendrite morphogenesis
B0051289biological_processprotein homotetramerization
B0052657molecular_functionguanine phosphoribosyltransferase activity
B0070062cellular_componentextracellular exosome
B0071542biological_processdopaminergic neuron differentiation
Functional Information from PROSITE/UniProt
site_idPS00103
Number of Residues13
DetailsPUR_PYR_PR_TRANSFER Purine/pyrimidine phosphoribosyl transferases signature. VLIVEDIIDTGkT
ChainResidueDetails
AVAL129-THR141

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000305
ChainResidueDetails
ATHR138
BTHR138

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:8044844
ChainResidueDetails
AGLY69
AASP134
AARG166
APHE186
BGLY69
BASP134
BARG166
BPHE186

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING:
ChainResidueDetails
ATYR194
BTYR194

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P00493
ChainResidueDetails
ASER103
BSER103

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P27605
ChainResidueDetails
AMET142
BMET142

site_idSWS_FT_FI6
Number of Residues4
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0007744|PubMed:28112733
ChainResidueDetails
AVAL115
BVAL115

Catalytic Information from CSA
site_idMCSA1
Number of Residues5
DetailsM-CSA 48
ChainResidueDetails
AASP134attractive charge-charge interaction, electrostatic stabiliser
AILE135attractive charge-charge interaction, electrostatic stabiliser
ATHR138hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
AVAL187electrostatic stabiliser
AASP200electrostatic stabiliser

site_idMCSA2
Number of Residues5
DetailsM-CSA 48
ChainResidueDetails
BASP134attractive charge-charge interaction, electrostatic stabiliser
BILE135attractive charge-charge interaction, electrostatic stabiliser
BTHR138hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
BVAL187electrostatic stabiliser
BASP200electrostatic stabiliser

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PDB entries from 2024-04-24

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