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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
DetailsActive site: {"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues20
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"8044844","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"10433693","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P27605","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues4
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate","evidences":[{"source":"PubMed","id":"28112733","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P00493","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1a95
ChainResidueDetails
AGLU142
AASP143
ALYS174
AASP146

site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 1a95
ChainResidueDetails
BGLU142
BASP143
BLYS174
BASP146

site_idCSA3
Number of Residues5
DetailsAnnotated By Reference To The Literature 1a95
ChainResidueDetails
AGLU142
AASP143
ALYS174
AASP146
ALEU178

site_idCSA4
Number of Residues5
DetailsAnnotated By Reference To The Literature 1a95
ChainResidueDetails
BGLU142
BASP143
BLYS174
BASP146
BLEU178

site_idMCSA1
Number of Residues5
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
APHE195electrostatic stabiliser
AARG208electrostatic stabiliser

site_idMCSA2
Number of Residues5
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
BPHE195electrostatic stabiliser
BARG208electrostatic stabiliser

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PDB entries from 2025-10-15

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