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3GGJ

Human hypoxanthine-guanine phosphoribosyltransferase in complex with 9-(2-phosphonoethoxyethyl)guanine

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 PDB Data
site_idAC1
Number of Residues14
DetailsBINDING SITE FOR RESIDUE 25H A 218
ChainResidue
AASP107
APHE186
AVAL187
ALEU192
AHOH227
AHOH267
ATHR110
AASP137
ATHR138
AGLY139
ALYS140
ATHR141
ALYS165
ALYS185

site_idAC2
Number of Residues13
DetailsBINDING SITE FOR RESIDUE 25H B 218
ChainResidue
BILE135
BASP137
BTHR138
BGLY139
BTHR141
BLYS165
BLYS185
BPHE186
BVAL187
BLEU192
BASP193
BHOH219
BHOH221

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
AASP137
BASP137

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:8044844
ChainResidueDetails
ALYS68
AGLU133
ALYS165
ALYS185
BLYS68
BGLU133
BLYS165
BLYS185

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING:
ChainResidueDetails
AASP193
BASP193

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: N-acetylalanine => ECO:0000269|PubMed:7107641
ChainResidueDetails
AALA1
BALA1

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P00493
ChainResidueDetails
ALYS102
BLYS102

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P27605
ChainResidueDetails
ATHR141
BTHR141

site_idSWS_FT_FI7
Number of Residues4
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0007744|PubMed:28112733
ChainResidueDetails
ALYS114
BLYS114

Catalytic Information from CSA
site_idMCSA1
Number of Residues5
DetailsM-CSA 48
ChainResidueDetails
AGLU133attractive charge-charge interaction, electrostatic stabiliser
AASP134attractive charge-charge interaction, electrostatic stabiliser
AASP137hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
APHE186electrostatic stabiliser
AARG199electrostatic stabiliser

site_idMCSA2
Number of Residues5
DetailsM-CSA 48
ChainResidueDetails
BGLU133attractive charge-charge interaction, electrostatic stabiliser
BASP134attractive charge-charge interaction, electrostatic stabiliser
BASP137hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
BPHE186electrostatic stabiliser
BARG199electrostatic stabiliser

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PDB entries from 2024-04-10

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