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2VFA

Crystal structure of a chimera of Plasmodium falciparum and human hypoxanthine-guanine phosphoribosyl transferases

Functional Information from GO Data
ChainGOidnamespacecontents
A0004422molecular_functionhypoxanthine phosphoribosyltransferase activity
A0006166biological_processpurine ribonucleoside salvage
B0004422molecular_functionhypoxanthine phosphoribosyltransferase activity
B0006166biological_processpurine ribonucleoside salvage
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE 5GP A 1224
ChainResidue
AASP146
ALYS174
APHE195
AVAL196
ALEU201
AASP202
ATYR203

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 1225
ChainResidue
AASP146
ATHR147
AGLY148
ATHR150
ALYS77
AGLU142

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE 5GP B 1227
ChainResidue
BLYS77
BLYS174
BPHE195
BVAL196
BLEU201
BASP202

site_idAC4
Number of Residues9
DetailsBINDING SITE FOR RESIDUE SO4 B 1228
ChainResidue
BLYS77
BGLU142
BILE145
BASP146
BTHR147
BGLY148
BLYS149
BTHR150
BMET151

Functional Information from PROSITE/UniProt
site_idPS00103
Number of Residues13
DetailsPUR_PYR_PR_TRANSFER Purine/pyrimidine phosphoribosyl transferases signature. VLIVEDIIDTGkT
ChainResidueDetails
AVAL138-THR150

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING:
ChainResidueDetails
ALYS174
BLYS174

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:10433693
ChainResidueDetails
AASP202
BASP202

site_idSWS_FT_FI3
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000305
ChainResidueDetails
AASP146
BASP146

site_idSWS_FT_FI4
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:8044844
ChainResidueDetails
ALYS77
AGLU142
BLYS77
BGLU142

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P00493
ChainResidueDetails
ALYS111
BLYS111

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P27605
ChainResidueDetails
ATHR150
BTHR150

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
ALYS123
BLYS123

Catalytic Information from CSA
site_idMCSA1
Number of Residues3
DetailsM-CSA 48
ChainResidueDetails
AGLU142attractive charge-charge interaction, electrostatic stabiliser
AASP143attractive charge-charge interaction, electrostatic stabiliser
AASP146hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor

site_idMCSA2
Number of Residues3
DetailsM-CSA 48
ChainResidueDetails
BGLU142attractive charge-charge interaction, electrostatic stabiliser
BASP143attractive charge-charge interaction, electrostatic stabiliser
BASP146hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor

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PDB entries from 2024-05-22

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