eF-site ID 1w0k-C PDB Code 1w0k Chain C click to enlarge Title ADP inhibited bovine F1-ATPase Classification HYDROLASE Compound ATP SYNTHASE ALPHA CHAIN HEART ISOFORM, MITOCHONDRIAL PRECURSOR Source ORGANISM_COMMON: BOVINE; ORGANISM_SCIENTIFIC: BOS TAURUS; Sequence C:  ADTSVDLEETGRVLSIGDGIARVHGLRNVQAEEMVEFSSG LKGMSLNLEPDNVGVVVFGNDKLIKEGDIVKRTGAIVDVP VGEELLGRVVDALGNAIDGKGPIGSKARRRVGLKAPGIIP RISVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKTSI AIDTIINQKRFNDGTDEKKKLYCIYVAIGQKRSTVAQLVK RLTDADAMKYTIVVSATASDAAPLQYLAPYSGCSMGEYFR DNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDV FYLHSRLLERAAKMNDAFGGGSLTALPVIETQAGDVSAYI PTNVISITDGQIFLETELFYKGIRPAINVGLSVSRVGSAA QTRAMKQVAGTMKLELAQYREVAAFAQFGSDLDAATQQLL SRGVRLTELLKQGQYSPMAIEEQVAVIYAGVRGYLDKLEP SKITKFENAFLSHVISQHQALLGKIRTDGKISEESDAKLK EIVTNFLAGFEA Description Functional site 1) chain C residue 176 type sequence T description BINDING SITE FOR RESIDUE MG C 1512 source : AC3 2) chain C residue 170 type sequence D description BINDING SITE FOR RESIDUE ADP C 1511 source : AC9 3) chain C residue 172 type sequence Q description BINDING SITE FOR RESIDUE ADP C 1511 source : AC9 4) chain C residue 173 type sequence T description BINDING SITE FOR RESIDUE ADP C 1511 source : AC9 5) chain C residue 174 type sequence G description BINDING SITE FOR RESIDUE ADP C 1511 source : AC9 6) chain C residue 175 type sequence K description BINDING SITE FOR RESIDUE ADP C 1511 source : AC9 7) chain C residue 176 type sequence T description BINDING SITE FOR RESIDUE ADP C 1511 source : AC9 8) chain C residue 177 type sequence S description BINDING SITE FOR RESIDUE ADP C 1511 source : AC9 9) chain C residue 357 type sequence F description BINDING SITE FOR RESIDUE ADP C 1511 source : AC9 10) chain C residue 362 type sequence R description BINDING SITE FOR RESIDUE ADP C 1511 source : AC9 11) chain C residue 430 type sequence Q description BINDING SITE FOR RESIDUE ADP C 1511 source : AC9 12) chain C residue 432 type sequence Q description BINDING SITE FOR RESIDUE ADP C 1511 source : AC9 13) chain C residue 372 type sequence S description BINDING SITE FOR RESIDUE ADP D 1476 source : BC1 14) chain C residue 373 type sequence R description BINDING SITE FOR RESIDUE ADP D 1476 source : BC1 15) chain C residue 50 type sequence E description BINDING SITE FOR RESIDUE GOL C 1513 source : BC4 16) chain C residue 130 type sequence G description BINDING SITE FOR RESIDUE GOL C 1513 source : BC4 17) chain C residue 244 type sequence Y description BINDING SITE FOR RESIDUE GOL C 1513 source : BC4 18) chain C residue 248 type sequence Y description BINDING SITE FOR RESIDUE GOL C 1513 source : BC4 19) chain C residue 304 type sequence R description BINDING SITE FOR RESIDUE GOL C 1513 source : BC4 20) chain C residue 391 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P25705 source Swiss-Prot : SWS_FT_FI11 21) chain C residue 33 type CARBOHYD sequence S description O-linked (GlcNAc) serine; alternate => ECO:0000250 source Swiss-Prot : SWS_FT_FI12 22) chain C residue 170 type MOD_RES sequence D description N6-acetyllysine => ECO:0000250|UniProtKB:Q91VR2 source Swiss-Prot : SWS_FT_FI1 23) chain C residue 430 type MOD_RES sequence Q description N6-acetyllysine => ECO:0000250|UniProtKB:Q91VR2 source Swiss-Prot : SWS_FT_FI1 24) chain C residue 22 type MOD_RES sequence S description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q91VR2 source Swiss-Prot : SWS_FT_FI4 25) chain C residue 123 type MOD_RES sequence S description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q91VR2 source Swiss-Prot : SWS_FT_FI4 26) chain C residue 141 type MOD_RES sequence S description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q91VR2 source Swiss-Prot : SWS_FT_FI4 27) chain C residue 80 type MOD_RES sequence K description Phosphoserine => ECO:0000250|UniProtKB:P10719 source Swiss-Prot : SWS_FT_FI7 28) chain C residue 83 type MOD_RES sequence K description Phosphoserine => ECO:0000250|UniProtKB:P10719 source Swiss-Prot : SWS_FT_FI7 29) chain C residue 89 type MOD_RES sequence K description Phosphoserine => ECO:0000250|UniProtKB:P10719 source Swiss-Prot : SWS_FT_FI7 30) chain C residue 197 type MOD_RES sequence K description Phosphoserine => ECO:0000250|UniProtKB:P10719 source Swiss-Prot : SWS_FT_FI7 31) chain C residue 498 type MOD_RES sequence K description Phosphoserine => ECO:0000250|UniProtKB:P10719 source Swiss-Prot : SWS_FT_FI7 32) chain C residue 118 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 33) chain C residue 124 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 34) chain C residue 187 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 35) chain C residue 196 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 36) chain C residue 218 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 37) chain C residue 262 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 38) chain C residue 384 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 39) chain C residue 455 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 40) chain C residue 463 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 41) chain C residue 488 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 42) chain C residue 496 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 43) chain C 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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