eF-site ID 2jj2-H PDB Code 2jj2 Chain H 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 H:  DLEETGRVLSIGDGIARVHGLRNVQAEEMVEFSSGLKGMS LNLEPDNVGVVVFGNDKLIKEGDIVKRTGAIVDVPVGEEL LGRVVDALGNAIDGKGPIGSKARRRVGLKAPGIIPRISVR EPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKTSIAIDTI INQKRFNDGTDEKKKLYCIYVAIGQKRSTVAQLVKRLTDA DAMKYTIVVSATASDAAPLQYLAPYSGCSMGEYFRDNGKH ALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHS RLLERAAKMNDAFGGGSLTALPVIETQAGDVSAYIPTNVI SITDGQIFLETELFYKGIRPAINVGLSVSRVGSAAQTRAM KQVAGTMKLELAQYREVAAFAQFGSDLDAATQQLLSRGVR LTELLKQGQYSPMAIEEQVAVIYAGVRGYLDKLEPSKITK FENAFLSHVISQHQALLSKIRTDGKISEESDAKLKEIVTN FLAGFEA Description Functional site 1) chain H residue 171 type sequence R description BINDING SITE FOR RESIDUE ANP H 1511 source : CC2 2) chain H residue 172 type sequence Q description BINDING SITE FOR RESIDUE ANP H 1511 source : CC2 3) chain H residue 173 type sequence T description BINDING SITE FOR RESIDUE ANP H 1511 source : CC2 4) chain H residue 174 type sequence G description BINDING SITE FOR RESIDUE ANP H 1511 source : CC2 5) chain H residue 175 type sequence K description BINDING SITE FOR RESIDUE ANP H 1511 source : CC2 6) chain H residue 176 type sequence T description BINDING SITE FOR RESIDUE ANP H 1511 source : CC2 7) chain H residue 177 type sequence S description BINDING SITE FOR RESIDUE ANP H 1511 source : CC2 8) chain H residue 357 type sequence F description BINDING SITE FOR RESIDUE ANP H 1511 source : CC2 9) chain H residue 362 type sequence R description BINDING SITE FOR RESIDUE ANP H 1511 source : CC2 10) chain H residue 363 type sequence P description BINDING SITE FOR RESIDUE ANP H 1511 source : CC2 11) chain H residue 430 type sequence Q description BINDING SITE FOR RESIDUE ANP H 1511 source : CC2 12) chain H residue 432 type sequence Q description BINDING SITE FOR RESIDUE ANP H 1511 source : CC2 13) chain H residue 176 type sequence T description BINDING SITE FOR RESIDUE MG H 1512 source : CC3 14) chain H residue 130 type sequence G description BINDING SITE FOR RESIDUE GOL H 1513 source : CC4 15) chain H residue 244 type sequence Y description BINDING SITE FOR RESIDUE GOL H 1513 source : CC4 16) chain H residue 245 type sequence L description BINDING SITE FOR RESIDUE GOL H 1513 source : CC4 17) chain H residue 248 type sequence Y description BINDING SITE FOR RESIDUE GOL H 1513 source : CC4 18) chain H residue 304 type sequence R description BINDING SITE FOR RESIDUE GOL H 1513 source : CC4 19) chain H residue 290 type sequence G description BINDING SITE FOR RESIDUE GOL H 1514 source : CC5 20) chain H residue 291 type sequence R description BINDING SITE FOR RESIDUE GOL H 1514 source : CC5 21) chain H residue 294 type sequence Y description BINDING SITE FOR RESIDUE GOL H 1514 source : CC5 22) chain H residue 295 type sequence P description BINDING SITE FOR RESIDUE GOL H 1514 source : CC5 23) chain H residue 296 type sequence G description BINDING SITE FOR RESIDUE GOL H 1514 source : CC5 24) chain H residue 337 type sequence Y description BINDING SITE FOR RESIDUE GOL H 1514 source : CC5 25) chain H residue 215 type sequence Q description BINDING SITE FOR RESIDUE GOL K 1480 source : DC7 26) chain H residue 391 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P25705 source Swiss-Prot : SWS_FT_FI11 27) chain H residue 33 type CARBOHYD sequence S description O-linked (GlcNAc) serine; alternate => ECO:0000250 source Swiss-Prot : SWS_FT_FI12 28) chain H residue 430 type MOD_RES sequence Q description N6-acetyllysine => ECO:0000250|UniProtKB:Q91VR2 source Swiss-Prot : SWS_FT_FI1 29) chain H residue 170 type MOD_RES sequence D description N6-acetyllysine => ECO:0000250|UniProtKB:Q91VR2 source Swiss-Prot : SWS_FT_FI1 30) chain H residue 123 type MOD_RES sequence S description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q91VR2 source Swiss-Prot : SWS_FT_FI4 31) chain H residue 141 type MOD_RES sequence S description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q91VR2 source Swiss-Prot : SWS_FT_FI4 32) chain H residue 80 type MOD_RES sequence K description Phosphoserine => ECO:0000250|UniProtKB:P10719 source Swiss-Prot : SWS_FT_FI7 33) chain H residue 83 type MOD_RES sequence K description Phosphoserine => ECO:0000250|UniProtKB:P10719 source Swiss-Prot : SWS_FT_FI7 34) chain H residue 89 type MOD_RES sequence K description Phosphoserine => ECO:0000250|UniProtKB:P10719 source Swiss-Prot : SWS_FT_FI7 35) chain H residue 197 type MOD_RES sequence K description Phosphoserine => ECO:0000250|UniProtKB:P10719 source Swiss-Prot : SWS_FT_FI7 36) chain H residue 498 type MOD_RES sequence K description Phosphoserine => ECO:0000250|UniProtKB:P10719 source Swiss-Prot : SWS_FT_FI7 37) chain H residue 118 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 38) chain H residue 124 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 39) chain H residue 187 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 40) chain H residue 196 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 41) chain H residue 218 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 42) chain H residue 262 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 43) chain H residue 384 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 44) chain H residue 455 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 45) chain H residue 463 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 46) chain H residue 488 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 47) chain H residue 496 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 48) chain H residue 161 type MOD_RES sequence R description Omega-N-methylarginine => ECO:0000250|UniProtKB:Q03265 source Swiss-Prot : SWS_FT_FI10

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