eF-site ID 1g9t-AB PDB Code 1g9t Chain A, B click to enlarge Title CRYSTAL STRUCTURE OF E.COLI HPRT-GMP COMPLEX Classification TRANSFERASE Compound HYPOXANTHINE PHOSPHORIBOSYLTRANSFERASE Source null (HPRT_ECOLI) Sequence A:  MKHTVEVMIPEAEIKARIAELGRQITERYKDSGSDMVLVG LLRGSFMFMADLCREVQVSHEVDFMTASRDLKILKDLDED IRGKDVLIVEDIIDSGNTLSKVREILSLREPKSLAICTLL DKPSRREVNVPVEFIGFSIPDEFVVGYGIDYAQRYRHLPY IGKVILL B:  MKHTVEVMIPEAEIKARIAELGRQITERYKDSGSDMVLVG LLRGSFMFMADLCREVQVSHEVDFMTASSRDLKILKDLDE DIRGKDVLIVEDIIDSGNTLSKVREILSLREPKSLAICTL LDKPSRREVNVPVEFIGFSIPDEFVVGYGIDYAQRYRHLP YIGKVILLD Description Functional site 1) chain A residue 103 type sequence E description BINDING SITE FOR RESIDUE 5GP A 190 source : AC1 2) chain A residue 105 type sequence I description BINDING SITE FOR RESIDUE 5GP A 190 source : AC1 3) chain A residue 107 type sequence D description BINDING SITE FOR RESIDUE 5GP A 190 source : AC1 4) chain A residue 108 type sequence S description BINDING SITE FOR RESIDUE 5GP A 190 source : AC1 5) chain A residue 109 type sequence G description BINDING SITE FOR RESIDUE 5GP A 190 source : AC1 6) chain A residue 110 type sequence N description BINDING SITE FOR RESIDUE 5GP A 190 source : AC1 7) chain A residue 111 type sequence T description BINDING SITE FOR RESIDUE 5GP A 190 source : AC1 8) chain A residue 112 type sequence L description BINDING SITE FOR RESIDUE 5GP A 190 source : AC1 9) chain A residue 135 type sequence K description BINDING SITE FOR RESIDUE 5GP A 190 source : AC1 10) chain A residue 156 type sequence F description BINDING SITE FOR RESIDUE 5GP A 190 source : AC1 11) chain A residue 157 type sequence V description BINDING SITE FOR RESIDUE 5GP A 190 source : AC1 12) chain A residue 162 type sequence I description BINDING SITE FOR RESIDUE 5GP A 190 source : AC1 13) chain A residue 163 type sequence D description BINDING SITE FOR RESIDUE 5GP A 190 source : AC1 14) chain B residue 407 type BINDING sequence D description BINDING => ECO:0000269|PubMed:12070315, ECO:0007744|PDB:1G9S source Swiss-Prot : SWS_FT_FI4 15) chain B residue 435 type BINDING sequence K description BINDING => ECO:0000269|PubMed:12070315, ECO:0007744|PDB:1G9S source Swiss-Prot : SWS_FT_FI4 16) chain A residue 107 type BINDING sequence D description BINDING => ECO:0000269|PubMed:12070315, ECO:0007744|PDB:1G9S source Swiss-Prot : SWS_FT_FI4 17) chain A residue 135 type BINDING sequence K description BINDING => ECO:0000269|PubMed:12070315, ECO:0007744|PDB:1G9S source Swiss-Prot : SWS_FT_FI4 18) chain B residue 463 type BINDING sequence D description BINDING => ECO:0000269|PubMed:12070315, ECO:0007744|PDB:1G9T source Swiss-Prot : SWS_FT_FI5 19) chain A residue 163 type BINDING sequence D description BINDING => ECO:0000269|PubMed:12070315, ECO:0007744|PDB:1G9T source Swiss-Prot : SWS_FT_FI5 20) chain A residue 99-111 type prosite sequence VLIVEDIIDSGNT description PUR_PYR_PR_TRANSFER Purine/pyrimidine phosphoribosyl transferases signature. VLIVEDIIDSGnT source prosite : PS00103 21) chain B residue 407 type ACT_SITE sequence D description Proton acceptor => ECO:0000305|PubMed:12070315 source Swiss-Prot : SWS_FT_FI1 22) chain A residue 107 type ACT_SITE sequence D description Proton acceptor => ECO:0000305|PubMed:12070315 source Swiss-Prot : SWS_FT_FI1 23) chain B residue 348 type BINDING sequence G description BINDING => ECO:0000250|UniProtKB:P9WHQ9 source Swiss-Prot : SWS_FT_FI2 24) chain B residue 469 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P9WHQ9 source Swiss-Prot : SWS_FT_FI2 25) chain B residue 347 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P9WHQ9 source Swiss-Prot : SWS_FT_FI2 26) chain A residue 169 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P9WHQ9 source Swiss-Prot : SWS_FT_FI2 27) chain A residue 48 type BINDING sequence G description BINDING => ECO:0000250|UniProtKB:P9WHQ9 source Swiss-Prot : SWS_FT_FI2 28) chain A residue 47 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P9WHQ9 source Swiss-Prot : SWS_FT_FI2 29) chain B residue 403 type BINDING sequence E description BINDING => ECO:0000269|PubMed:12070315, ECO:0007744|PDB:1GRV source Swiss-Prot : SWS_FT_FI3 30) chain B residue 404 type BINDING sequence D description BINDING => ECO:0000269|PubMed:12070315, ECO:0007744|PDB:1GRV source Swiss-Prot : SWS_FT_FI3 31) chain A residue 103 type BINDING sequence E description BINDING => ECO:0000269|PubMed:12070315, ECO:0007744|PDB:1GRV source Swiss-Prot : SWS_FT_FI3 32) chain A residue 104 type BINDING sequence D description BINDING => ECO:0000269|PubMed:12070315, ECO:0007744|PDB:1GRV source Swiss-Prot : SWS_FT_FI3

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