eF-site ID 3ggj-AB PDB Code 3ggj Chain A, B click to enlarge Title Human hypoxanthine-guanine phosphoribosyltransferase in complex with 9-(2-phosphonoethoxyethyl)guanine Classification TRANSFERASE Compound Hypoxanthine-guanine phosphoribosyltransferase Source Homo sapiens (Human) (HPRT_HUMAN) Sequence A:  SPGVVISDDEPGYDLDLFCIPNHYAEDLERVFIPHGLIMD RTERLARDVMKEMGGHHIVALCVLKGGYKFFADLLDYIKA LNRNSDRSIPMTVDFIRLKSYCNDQSTGDIKVIGGDDLST LTGKNVLIVEDIIDTGKTMQTLLSLVRQYNPKMVKVASLL VKRTPRSVGYKPDFVGFEIPDKFVVGYALDYNEYFRDLNH VCVISETGKAKYKA B:  RSPGVVISDDEPGYDLDLFCIPNHYAEDLERVFIPHGLIM DRTERLARDVMKEMGGHIVALCVLKGGYKFFADLLDYIKA LNRNSDRSIPMTVDFIRLKSYCNQSGDIKVIGDDLSTLTG KNVLIVEDIIDTGKTMQTLLSLVRQYNPKMVKVASLLVKR TPRSVGYKPDFVGFEIPDKFVVGYALDYNEYFRDLNHVCV ISETGKAKYKA Description Functional site 1) chain A residue 107 type sequence D description BINDING SITE FOR RESIDUE 25H A 218 source : AC1 2) chain A residue 110 type sequence T description BINDING SITE FOR RESIDUE 25H A 218 source : AC1 3) chain A residue 137 type sequence D description BINDING SITE FOR RESIDUE 25H A 218 source : AC1 4) chain A residue 138 type sequence T description BINDING SITE FOR RESIDUE 25H A 218 source : AC1 5) chain A residue 139 type sequence G description BINDING SITE FOR RESIDUE 25H A 218 source : AC1 6) chain A residue 140 type sequence K description BINDING SITE FOR RESIDUE 25H A 218 source : AC1 7) chain A residue 141 type sequence T description BINDING SITE FOR RESIDUE 25H A 218 source : AC1 8) chain A residue 165 type sequence K description BINDING SITE FOR RESIDUE 25H A 218 source : AC1 9) chain A residue 185 type sequence K description BINDING SITE FOR RESIDUE 25H A 218 source : AC1 10) chain A residue 186 type sequence F description BINDING SITE FOR RESIDUE 25H A 218 source : AC1 11) chain A residue 187 type sequence V description BINDING SITE FOR RESIDUE 25H A 218 source : AC1 12) chain A residue 192 type sequence L description BINDING SITE FOR RESIDUE 25H A 218 source : AC1 13) chain B residue 135 type sequence I description BINDING SITE FOR RESIDUE 25H B 218 source : AC2 14) chain B residue 137 type sequence D description BINDING SITE FOR RESIDUE 25H B 218 source : AC2 15) chain B residue 138 type sequence T description BINDING SITE FOR RESIDUE 25H B 218 source : AC2 16) chain B residue 139 type sequence G description BINDING SITE FOR RESIDUE 25H B 218 source : AC2 17) chain B residue 141 type sequence T description BINDING SITE FOR RESIDUE 25H B 218 source : AC2 18) chain B residue 165 type sequence K description BINDING SITE FOR RESIDUE 25H B 218 source : AC2 19) chain B residue 185 type sequence K description BINDING SITE FOR RESIDUE 25H B 218 source : AC2 20) chain B residue 186 type sequence F description BINDING SITE FOR RESIDUE 25H B 218 source : AC2 21) chain B residue 187 type sequence V description BINDING SITE FOR RESIDUE 25H B 218 source : AC2 22) chain B residue 192 type sequence L description BINDING SITE FOR RESIDUE 25H B 218 source : AC2 23) chain B residue 193 type sequence D description BINDING SITE FOR RESIDUE 25H B 218 source : AC2 24) chain A residue 133 type catalytic sequence E description 48 source MCSA : MCSA1 25) chain A residue 134 type catalytic sequence D description 48 source MCSA : MCSA1 26) chain A residue 137 type catalytic sequence D description 48 source MCSA : MCSA1 27) chain A residue 186 type catalytic sequence F description 48 source MCSA : MCSA1 28) chain A residue 199 type catalytic sequence R description 48 source MCSA : MCSA1 29) chain B residue 133 type catalytic sequence E description 48 source MCSA : MCSA2 30) chain B residue 134 type catalytic sequence D description 48 source MCSA : MCSA2 31) chain B residue 137 type catalytic sequence D description 48 source MCSA : MCSA2 32) chain B residue 186 type catalytic sequence F description 48 source MCSA : MCSA2 33) chain B residue 199 type catalytic sequence R description 48 source MCSA : MCSA2 34) chain A residue 137 type ACT_SITE sequence D description Proton acceptor => ECO:0000305 source Swiss-Prot : SWS_FT_FI1 35) chain B residue 137 type ACT_SITE sequence D description Proton acceptor => ECO:0000305 source Swiss-Prot : SWS_FT_FI1 36) chain A residue 68 type BINDING sequence K description BINDING => ECO:0000269|PubMed:8044844 source Swiss-Prot : SWS_FT_FI2 37) chain A residue 133 type BINDING sequence E description BINDING => ECO:0000269|PubMed:8044844 source Swiss-Prot : SWS_FT_FI2 38) chain A residue 165 type BINDING sequence K description BINDING => ECO:0000269|PubMed:8044844 source Swiss-Prot : SWS_FT_FI2 39) chain A residue 185 type BINDING sequence K description BINDING => ECO:0000269|PubMed:8044844 source Swiss-Prot : SWS_FT_FI2 40) chain B residue 68 type BINDING sequence K description BINDING => ECO:0000269|PubMed:8044844 source Swiss-Prot : SWS_FT_FI2 41) chain B residue 133 type BINDING sequence E description BINDING => ECO:0000269|PubMed:8044844 source Swiss-Prot : SWS_FT_FI2 42) chain B residue 165 type BINDING sequence K description BINDING => ECO:0000269|PubMed:8044844 source Swiss-Prot : SWS_FT_FI2 43) chain B residue 185 type BINDING sequence K description BINDING => ECO:0000269|PubMed:8044844 source Swiss-Prot : SWS_FT_FI2 44) chain A residue 193 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI3 45) chain B residue 193 type BINDING sequence D description source Swiss-Prot : SWS_FT_FI3 46) chain A residue 129-141 type prosite sequence VLIVEDIIDTGKT description PUR_PYR_PR_TRANSFER Purine/pyrimidine phosphoribosyl transferases signature. VLIVEDIIDTGkT source prosite : PS00103 47) chain A residue 102 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P00493 source Swiss-Prot : SWS_FT_FI5 48) chain B residue 102 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P00493 source Swiss-Prot : SWS_FT_FI5 49) chain A residue 141 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P27605 source Swiss-Prot : SWS_FT_FI6 50) chain B residue 141 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P27605 source Swiss-Prot : SWS_FT_FI6 51) chain A residue 114 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0007744|PubMed:28112733 source Swiss-Prot : SWS_FT_FI7 52) chain B residue 114 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0007744|PubMed:28112733 source Swiss-Prot : SWS_FT_FI7

Display surface Download Links