eF-site ID 1efr-A PDB Code 1efr Chain A click to enlarge Title BOVINE MITOCHONDRIAL F1-ATPASE COMPLEXED WITH THE PEPTIDE ANTIBIOTIC EFRAPEPTIN Classification HYDROLASE/ANTIBIOTIC Compound BOVINE MITOCHONDRIAL F1-ATPASE SUBUNIT ALPHA Source ORGANISM_COMMON: CATTLE; 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 175 type sequence K description THE RESIDUE LISTED IS THE LYSINE WITHIN THE P-LOOP (PHOSPHATE BINDING) MOTIF, GXXXXGKT/S. source : PLP 2) chain A 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 A residue 176 type sequence T description BINDING SITE FOR RESIDUE MG A 601 source : AC1 4) chain A residue 170 type sequence D description BINDING SITE FOR RESIDUE ANP A 600 source : AC6 5) chain A residue 171 type sequence R description BINDING SITE FOR RESIDUE ANP A 600 source : AC6 6) chain A residue 172 type sequence Q description BINDING SITE FOR RESIDUE ANP A 600 source : AC6 7) chain A residue 173 type sequence T description BINDING SITE FOR RESIDUE ANP A 600 source : AC6 8) chain A residue 174 type sequence G description BINDING SITE FOR RESIDUE ANP A 600 source : AC6 9) chain A residue 175 type sequence K description BINDING SITE FOR RESIDUE ANP A 600 source : AC6 10) chain A residue 176 type sequence T description BINDING SITE FOR RESIDUE ANP A 600 source : AC6 11) chain A residue 177 type sequence S description BINDING SITE FOR RESIDUE ANP A 600 source : AC6 12) chain A residue 357 type sequence F description BINDING SITE FOR RESIDUE ANP A 600 source : AC6 13) chain A residue 362 type sequence R description BINDING SITE FOR RESIDUE ANP A 600 source : AC6 14) chain A residue 363 type sequence P description BINDING SITE FOR RESIDUE ANP A 600 source : AC6 15) chain A residue 430 type sequence Q description BINDING SITE FOR RESIDUE ANP A 600 source : AC6 16) chain A residue 432 type sequence Q description BINDING SITE FOR RESIDUE ANP A 600 source : AC6 17) chain A residue 331 type sequence A description BINDING SITE FOR CHAIN Q OF EFRAPEPTIN C source : BC2 18) chain A residue 332 type sequence G description BINDING SITE FOR CHAIN Q OF EFRAPEPTIN C source : BC2 19) chain A residue 333 type sequence D description BINDING SITE FOR CHAIN Q OF EFRAPEPTIN C source : BC2 20) chain A residue 334 type sequence V description BINDING SITE FOR CHAIN Q OF EFRAPEPTIN C source : BC2 21) chain A residue 335 type sequence S description BINDING SITE FOR CHAIN Q OF EFRAPEPTIN C source : BC2 22) chain A residue 349 type sequence Q description BINDING SITE FOR CHAIN Q OF EFRAPEPTIN C source : BC2 23) chain A residue 351 type sequence F description BINDING SITE FOR CHAIN Q OF EFRAPEPTIN C source : BC2 24) chain A residue 369 type sequence L description BINDING SITE FOR CHAIN Q OF EFRAPEPTIN C source : BC2 25) chain A residue 363-372 type prosite sequence PAINVGLSVS description ATPASE_ALPHA_BETA ATP synthase alpha and beta subunits signature. PAVDPLDSTS source prosite : PS00152 26) chain A residue 161 type MOD_RES sequence R description Omega-N-methylarginine => ECO:0000250|UniProtKB:Q03265 source Swiss-Prot : SWS_FT_FI10 27) chain A residue 391 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P25705 source Swiss-Prot : SWS_FT_FI11 28) chain A residue 33 type CARBOHYD sequence S description O-linked (GlcNAc) serine; alternate => ECO:0000250 source Swiss-Prot : SWS_FT_FI12 29) chain A residue 197 type MOD_RES sequence K description Phosphoserine => ECO:0000250|UniProtKB:P10719 source Swiss-Prot : SWS_FT_FI7 30) chain A residue 498 type MOD_RES sequence K description Phosphoserine => ECO:0000250|UniProtKB:P10719 source Swiss-Prot : SWS_FT_FI7 31) chain A residue 488 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 32) chain A residue 496 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 33) chain A residue 196 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 34) chain A residue 218 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 35) chain A residue 262 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 36) chain A residue 384 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 37) chain A residue 455 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 38) chain A residue 463 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9

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