eF-site ID 1g9s-A PDB Code 1g9s Chain A click to enlarge Title CRYSTAL STRUCTURE OF A COMPLEX BETWEEN E.COLI HPRT AND IMP Classification TRANSFERASE Compound HYPOXANTHINE PHOSPHORIBOSYLTRANSFERASE Source null (HPRT_ECOLI) Sequence A:  MKHTVEVMIPEAEIKARIAELGRQITERYKDSGSDMVLVG LLRGSFMFMADLCREVQVSHEVDFMTASSRDLKILKDLDE DIRGKDVLIVEDIIDSGNTLSKVREILSLREPKSLAICTL LDKPSRREVNVPVEFIGFSIPDEFVVGYGIDYAQRYRHLP YIGKVILLD Description Functional site 1) chain A residue 103 type sequence E description BINDING SITE FOR RESIDUE IMP A 190 source : AC1 2) chain A residue 104 type sequence D description BINDING SITE FOR RESIDUE IMP A 190 source : AC1 3) chain A residue 105 type sequence I description BINDING SITE FOR RESIDUE IMP A 190 source : AC1 4) chain A residue 106 type sequence I description BINDING SITE FOR RESIDUE IMP A 190 source : AC1 5) chain A residue 107 type sequence D description BINDING SITE FOR RESIDUE IMP A 190 source : AC1 6) chain A residue 108 type sequence S description BINDING SITE FOR RESIDUE IMP A 190 source : AC1 7) chain A residue 109 type sequence G description BINDING SITE FOR RESIDUE IMP A 190 source : AC1 8) chain A residue 110 type sequence N description BINDING SITE FOR RESIDUE IMP A 190 source : AC1 9) chain A residue 111 type sequence T description BINDING SITE FOR RESIDUE IMP A 190 source : AC1 10) chain A residue 112 type sequence L description BINDING SITE FOR RESIDUE IMP A 190 source : AC1 11) chain A residue 135 type sequence K description BINDING SITE FOR RESIDUE IMP A 190 source : AC1 12) chain A residue 156 type sequence F description BINDING SITE FOR RESIDUE IMP A 190 source : AC1 13) chain A residue 157 type sequence V description BINDING SITE FOR RESIDUE IMP A 190 source : AC1 14) chain A residue 99-111 type prosite sequence VLIVEDIIDSGNT description PUR_PYR_PR_TRANSFER Purine/pyrimidine phosphoribosyl transferases signature. VLIVEDIIDSGnT source prosite : PS00103 15) chain A residue 103 type ACT_SITE sequence E description Proton acceptor => ECO:0000305|PubMed:12070315 source Swiss-Prot : SWS_FT_FI1 16) chain A residue 44 type BINDING sequence G description BINDING => ECO:0000250|UniProtKB:P9WHQ9 source Swiss-Prot : SWS_FT_FI2 17) chain A residue 43 type BINDING sequence V description BINDING => ECO:0000250|UniProtKB:P9WHQ9 source Swiss-Prot : SWS_FT_FI2 18) chain A residue 165 type BINDING sequence A description BINDING => ECO:0000250|UniProtKB:P9WHQ9 source Swiss-Prot : SWS_FT_FI2 19) chain A residue 99 type BINDING sequence V description BINDING => ECO:0000269|PubMed:12070315, ECO:0007744|PDB:1GRV source Swiss-Prot : SWS_FT_FI3 20) chain A residue 100 type BINDING sequence L description BINDING => ECO:0000269|PubMed:12070315, ECO:0007744|PDB:1GRV source Swiss-Prot : SWS_FT_FI3 21) chain A residue 103 type BINDING sequence E description BINDING => ECO:0000269|PubMed:12070315, ECO:0007744|PDB:1G9S source Swiss-Prot : SWS_FT_FI4 22) chain A residue 131 type BINDING sequence T description BINDING => ECO:0000269|PubMed:12070315, ECO:0007744|PDB:1G9S source Swiss-Prot : SWS_FT_FI4 23) chain A residue 159 type BINDING sequence G description BINDING => ECO:0000269|PubMed:12070315, ECO:0007744|PDB:1G9T source Swiss-Prot : SWS_FT_FI5

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