eF-site ID 1w0j-A PDB Code 1w0j Chain A click to enlarge Title Beryllium fluoride inhibited bovine F1-ATPase Classification HYDROLASE Compound ATP SYNTHASE ALPHA CHAIN HEART ISOFORM, MITOCHONDRIAL PRECURSOR Source ORGANISM_COMMON: BOVINE; ORGANISM_SCIENTIFIC: BOS TAURUS; Sequence A:  DLEETGRVLSIGDGIARVHGLRNVQAEEMVEFSSGLKGMS LNLEPDNVGVVVFGNDKLIKEGDIVKRTGAIVDVPVGEEL LGRVVDALGNAIDGKGPIGSKARRRVGLKAPGIIPRISVR EPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKTSIAIDTI INQKRFNDGTDEKKKLYCIYVAIGQKRSTVAQLVKRLTDA DAMKYTIVVSATASDAAPLQYLAPYSGCSMGEYFRDNGKH ALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHS RLLERAAKMNDAFGGGSLTALPVIETQAGDVSAYIPTNVI SITDGQIFLETELFYKGIRPAINVGLSVSRVGSAAQTRAM KQVAGTMKLELAQYREVAAFAQFGSDLDAATQQLLSRGVR LTELLKQGQYSPMAIEEQVAVIYAGVRGYLDKLEPSKITK FENAFLSHVISQHQALLGKIRTDGKISEESDAKLKEIVTN FLAGFEA Description Functional site 1) chain A residue 176 type sequence T description BINDING SITE FOR RESIDUE MG A 1512 source : AC2 2) chain A residue 172 type sequence Q description BINDING SITE FOR RESIDUE ADP A 1511 source : AC7 3) chain A residue 173 type sequence T description BINDING SITE FOR RESIDUE ADP A 1511 source : AC7 4) chain A residue 174 type sequence G description BINDING SITE FOR RESIDUE ADP A 1511 source : AC7 5) chain A residue 175 type sequence K description BINDING SITE FOR RESIDUE ADP A 1511 source : AC7 6) chain A residue 176 type sequence T description BINDING SITE FOR RESIDUE ADP A 1511 source : AC7 7) chain A residue 177 type sequence S description BINDING SITE FOR RESIDUE ADP A 1511 source : AC7 8) chain A residue 357 type sequence F description BINDING SITE FOR RESIDUE ADP A 1511 source : AC7 9) chain A residue 362 type sequence R description BINDING SITE FOR RESIDUE ADP A 1511 source : AC7 10) chain A residue 430 type sequence Q description BINDING SITE FOR RESIDUE ADP A 1511 source : AC7 11) chain A residue 432 type sequence Q description BINDING SITE FOR RESIDUE ADP A 1511 source : AC7 12) chain A residue 130 type sequence G description BINDING SITE FOR RESIDUE GOL A 1513 source : BC5 13) chain A residue 244 type sequence Y description BINDING SITE FOR RESIDUE GOL A 1513 source : BC5 14) chain A residue 245 type sequence L description BINDING SITE FOR RESIDUE GOL A 1513 source : BC5 15) chain A residue 248 type sequence Y description BINDING SITE FOR RESIDUE GOL A 1513 source : BC5 16) chain A residue 304 type sequence R description BINDING SITE FOR RESIDUE GOL A 1513 source : BC5 17) chain A residue 391 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P25705 source Swiss-Prot : SWS_FT_FI11 18) chain A residue 33 type CARBOHYD sequence S description O-linked (GlcNAc) serine; alternate => ECO:0000250 source Swiss-Prot : SWS_FT_FI12 19) chain A residue 488 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 20) chain A residue 496 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 21) chain A residue 196 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 22) chain A residue 218 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 23) chain A residue 262 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 24) chain A residue 384 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 25) chain A residue 455 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 26) chain A residue 463 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 27) chain A residue 161 type MOD_RES sequence R description Omega-N-methylarginine => ECO:0000250|UniProtKB:Q03265 source Swiss-Prot : SWS_FT_FI10 28) chain A residue 197 type MOD_RES sequence K description Phosphoserine => ECO:0000250|UniProtKB:P10719 source Swiss-Prot : SWS_FT_FI7 29) chain A residue 498 type MOD_RES sequence K description Phosphoserine => ECO:0000250|UniProtKB:P10719 source Swiss-Prot : SWS_FT_FI7 30) chain A residue 363-372 type prosite sequence PAINVGLSVS description ATPASE_ALPHA_BETA ATP synthase alpha and beta subunits signature. PAINVGLSVS source prosite : PS00152

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