eF-site ID 2jj2-I PDB Code 2jj2 Chain I click to enlarge Title The Structure of F1-ATPase inhibited by quercetin. Classification HYDROLASE Compound ATP SYNTHASE SUBUNIT ALPHA HEART ISOFORM Source ORGANISM_COMMON: BOVINE; ORGANISM_SCIENTIFIC: BOS TAURUS; Sequence I:  VDLEETGRVLSIGDGIARVHGLRNVQAEEMVEFSSGLKGM SLNLEPDNVGVVVFGNDKLIKEGDIVKRTGAIVDVPVGEE LLGRVVDALGNAIDGKGPIGSKARRRVGLKAPGIIPRISV REPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKTSIAIDT IINQKRFNDGTDEKKKLYCIYVAIGQKRSTVAQLVKRLTD ADAMKYTIVVSATASDAAPLQYLAPYSGCSMGEYFRDNGK HALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLH SRLLERAAKMNDAFGGGSLTALPVIETQAGDVSAYIPTNV ISITDGQIFLETELFYKGIRPAINVGLSVSRVGSAAQTRA MKQVAGTMKLELAQYREVALDAATQQLLSRGVRLTELLKQ GQYSPMAIEEQVAVIYAGVRGYLDKLEPSKITKFENAFLS HVISQHQALLSKIRTDGKISEESDAKLKEIVTNFLAGFE Description Functional site 1) chain I residue 171 type sequence R description BINDING SITE FOR RESIDUE ANP I 1510 source : CC6 2) chain I residue 172 type sequence Q description BINDING SITE FOR RESIDUE ANP I 1510 source : CC6 3) chain I residue 173 type sequence T description BINDING SITE FOR RESIDUE ANP I 1510 source : CC6 4) chain I residue 174 type sequence G description BINDING SITE FOR RESIDUE ANP I 1510 source : CC6 5) chain I residue 175 type sequence K description BINDING SITE FOR RESIDUE ANP I 1510 source : CC6 6) chain I residue 176 type sequence T description BINDING SITE FOR RESIDUE ANP I 1510 source : CC6 7) chain I residue 177 type sequence S description BINDING SITE FOR RESIDUE ANP I 1510 source : CC6 8) chain I residue 357 type sequence F description BINDING SITE FOR RESIDUE ANP I 1510 source : CC6 9) chain I residue 362 type sequence R description BINDING SITE FOR RESIDUE ANP I 1510 source : CC6 10) chain I residue 430 type sequence Q description BINDING SITE FOR RESIDUE ANP I 1510 source : CC6 11) chain I residue 432 type sequence Q description BINDING SITE FOR RESIDUE ANP I 1510 source : CC6 12) chain I residue 176 type sequence T description BINDING SITE FOR RESIDUE MG I 1511 source : CC7 13) chain I residue 129 type sequence V description BINDING SITE FOR RESIDUE GOL I 1512 source : CC8 14) chain I residue 130 type sequence G description BINDING SITE FOR RESIDUE GOL I 1512 source : CC8 15) chain I residue 244 type sequence Y description BINDING SITE FOR RESIDUE GOL I 1512 source : CC8 16) chain I residue 248 type sequence Y description BINDING SITE FOR RESIDUE GOL I 1512 source : CC8 17) chain I residue 304 type sequence R description BINDING SITE FOR RESIDUE GOL I 1512 source : CC8 18) chain I residue 343 type sequence I description BINDING SITE FOR RESIDUE ANP M 1475 source : DC9 19) chain I residue 344 type sequence S description BINDING SITE FOR RESIDUE ANP M 1475 source : DC9 20) chain I residue 371 type sequence V description BINDING SITE FOR RESIDUE ANP M 1475 source : DC9 21) chain I residue 373 type sequence R description BINDING SITE FOR RESIDUE ANP M 1475 source : DC9 22) chain I residue 291 type sequence R description BINDING SITE FOR RESIDUE QUE N 1273 source : EC2 23) chain I residue 292 type sequence E description BINDING SITE FOR RESIDUE QUE N 1273 source : EC2 24) chain I residue 430 type MOD_RES sequence Q description N6-acetyllysine => ECO:0000250|UniProtKB:Q91VR2 source Swiss-Prot : SWS_FT_FI1 25) chain I residue 170 type MOD_RES sequence D description N6-acetyllysine => ECO:0000250|UniProtKB:Q91VR2 source Swiss-Prot : SWS_FT_FI1 26) chain I residue 391 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P25705 source Swiss-Prot : SWS_FT_FI11 27) chain I residue 33 type CARBOHYD sequence S description O-linked (GlcNAc) serine; alternate => ECO:0000250 source Swiss-Prot : SWS_FT_FI12 28) chain I residue 80 type MOD_RES sequence K description Phosphoserine => ECO:0000250|UniProtKB:P10719 source Swiss-Prot : SWS_FT_FI7 29) chain I residue 83 type MOD_RES sequence K description Phosphoserine => ECO:0000250|UniProtKB:P10719 source Swiss-Prot : SWS_FT_FI7 30) chain I residue 89 type MOD_RES sequence K description Phosphoserine => ECO:0000250|UniProtKB:P10719 source Swiss-Prot : SWS_FT_FI7 31) chain I residue 197 type MOD_RES sequence K description Phosphoserine => ECO:0000250|UniProtKB:P10719 source Swiss-Prot : SWS_FT_FI7 32) chain I residue 498 type MOD_RES sequence K description Phosphoserine => ECO:0000250|UniProtKB:P10719 source Swiss-Prot : SWS_FT_FI7 33) chain I residue 118 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 34) chain I residue 124 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 35) chain I residue 187 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 36) chain I residue 196 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 37) chain I residue 218 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 38) chain I residue 262 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 39) chain I residue 384 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 40) chain I residue 455 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 41) chain I residue 463 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 42) chain I residue 488 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 43) chain I residue 496 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 44) chain I residue 161 type MOD_RES sequence R description Omega-N-methylarginine => ECO:0000250|UniProtKB:Q03265 source Swiss-Prot : SWS_FT_FI10 45) chain I residue 123 type MOD_RES sequence S description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q91VR2 source Swiss-Prot : SWS_FT_FI4 46) chain I residue 141 type MOD_RES sequence S description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q91VR2 source Swiss-Prot : SWS_FT_FI4

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