eF-site ID 1bmf-C PDB Code 1bmf Chain C click to enlarge Title BOVINE MITOCHONDRIAL F1-ATPASE Classification ATP PHOSPHORYLASE Compound BOVINE MITOCHONDRIAL F1-ATPASE Source ORGANISM_COMMON: cattle; 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 175 type sequence K description LYSINE WITHIN THE P-LOOP (PHOSPHATE BINDING) MOTIF, GXXXXGKT/S. source : PLP 2) chain C residue 373 type sequence R description THE CARBOXYLATE GROUP OF THE GLUTAMIC ACID RESIDUE IS BELIEVED TO ACTIVATE A WATER MOLECULE FOR INLINE ATTACK ON THE GAMMA PHOSPHATE DURING ATP HYDROLYSIS. THE ARGININE RESIDUE (WHICH IS LOCATED ON AN ADJACENT ALPHA SUBUNIT) COULD HELP TO STABLIZE THE NEGATIVE CHARGE THAT DEVELOPS ON THE TERMINAL PHOSPHATE IN THE PUTATIVE PENTACOORDINATED TRANSITION STATE. source : CAT 3) chain C residue 176 type sequence T description BINDING SITE FOR RESIDUE MG C 601 source : AC3 4) chain C residue 171 type sequence R description BINDING SITE FOR RESIDUE ANP C 600 source : AC8 5) chain C residue 172 type sequence Q description BINDING SITE FOR RESIDUE ANP C 600 source : AC8 6) chain C residue 173 type sequence T description BINDING SITE FOR RESIDUE ANP C 600 source : AC8 7) chain C residue 174 type sequence G description BINDING SITE FOR RESIDUE ANP C 600 source : AC8 8) chain C residue 175 type sequence K description BINDING SITE FOR RESIDUE ANP C 600 source : AC8 9) chain C residue 176 type sequence T description BINDING SITE FOR RESIDUE ANP C 600 source : AC8 10) chain C residue 177 type sequence S description BINDING SITE FOR RESIDUE ANP C 600 source : AC8 11) chain C residue 357 type sequence F description BINDING SITE FOR RESIDUE ANP C 600 source : AC8 12) chain C residue 362 type sequence R description BINDING SITE FOR RESIDUE ANP C 600 source : AC8 13) chain C residue 430 type sequence Q description BINDING SITE FOR RESIDUE ANP C 600 source : AC8 14) chain C residue 432 type sequence Q description BINDING SITE FOR RESIDUE ANP C 600 source : AC8 15) chain C residue 372 type sequence S description BINDING SITE FOR RESIDUE ADP D 600 source : AC9 16) chain C residue 373 type sequence R description BINDING SITE FOR RESIDUE ADP D 600 source : AC9 17) chain C residue 170 type MOD_RES sequence D description N6-acetyllysine => ECO:0000250|UniProtKB:Q91VR2 source Swiss-Prot : SWS_FT_FI1 18) chain C residue 430 type MOD_RES sequence Q description N6-acetyllysine => ECO:0000250|UniProtKB:Q91VR2 source Swiss-Prot : SWS_FT_FI1 19) chain C residue 161 type MOD_RES sequence R description Omega-N-methylarginine => ECO:0000250|UniProtKB:Q03265 source Swiss-Prot : SWS_FT_FI10 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 22 type MOD_RES sequence S description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q91VR2 source Swiss-Prot : SWS_FT_FI4 23) chain C residue 123 type MOD_RES sequence S description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q91VR2 source Swiss-Prot : SWS_FT_FI4 24) chain C residue 141 type MOD_RES sequence S description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q91VR2 source Swiss-Prot : SWS_FT_FI4 25) chain C residue 80 type MOD_RES sequence K description Phosphoserine => ECO:0000250|UniProtKB:P10719 source Swiss-Prot : SWS_FT_FI7 26) chain C residue 83 type MOD_RES sequence K description Phosphoserine => ECO:0000250|UniProtKB:P10719 source Swiss-Prot : SWS_FT_FI7 27) chain C residue 89 type MOD_RES sequence K description Phosphoserine => ECO:0000250|UniProtKB:P10719 source Swiss-Prot : SWS_FT_FI7 28) chain C residue 197 type MOD_RES sequence K description Phosphoserine => ECO:0000250|UniProtKB:P10719 source Swiss-Prot : SWS_FT_FI7 29) chain C residue 498 type MOD_RES sequence K description Phosphoserine => ECO:0000250|UniProtKB:P10719 source Swiss-Prot : SWS_FT_FI7 30) chain C residue 118 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 31) chain C residue 124 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 32) chain C residue 187 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 33) chain C residue 196 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 34) chain C residue 218 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 35) chain C residue 262 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 36) chain C residue 384 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 37) chain C residue 455 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 38) chain C residue 463 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 39) chain C residue 488 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 40) chain C residue 496 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9

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