eF-site ID 1efr-F PDB Code 1efr Chain F 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 F:  TTGRIVAVIGAVVDVQFDEGLPPILNALEVQGRETRLVLE VAQHLGESTVRTIAMDGTEGLVRGQKVLDSGAPIRIPVGP ETLGRIMNVIGEPIDERGPIKTKQFAAIHAEAPEFVEMSV EQEILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIME LINNVAKAHGGYSVFAGVGERTREGNDLYHEMIESGVINL KDATSKVALVYGQMNEPPGARARVALTGLTVAEYFRDQEG QDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATD MGTMQERITTTKKGSITSVQAIYVPADDLTDPAPATTFAH LDATTVLSRAIAELGIYPAVDPLDSTSRIMDPNIVGSEHY DVARGVQKILQDYKSLQDIIAILGMDELSEEDKLTVSRAR KIQRFLSQPFQVAEVFTGHLGKLVPLKETIKGFQQILAGE YDHLPEQAFYMVGPIEEAVAKADKLA Description Functional site 1) chain F residue 162 type sequence K description THE RESIDUE LISTED IS THE LYSINE WITHIN THE P-LOOP (PHOSPHATE BINDING) MOTIF, GXXXXGKT/S. source : PLP 2) chain F residue 188 type sequence E 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 F residue 163 type sequence T description BINDING SITE FOR RESIDUE MG F 601 source : AC5 4) chain F residue 188 type sequence E description BINDING SITE FOR RESIDUE MG F 601 source : AC5 5) chain F residue 158 type sequence A description BINDING SITE FOR RESIDUE ANP F 600 source : BC1 6) chain F residue 159 type sequence G description BINDING SITE FOR RESIDUE ANP F 600 source : BC1 7) chain F residue 160 type sequence V description BINDING SITE FOR RESIDUE ANP F 600 source : BC1 8) chain F residue 161 type sequence G description BINDING SITE FOR RESIDUE ANP F 600 source : BC1 9) chain F residue 162 type sequence K description BINDING SITE FOR RESIDUE ANP F 600 source : BC1 10) chain F residue 163 type sequence T description BINDING SITE FOR RESIDUE ANP F 600 source : BC1 11) chain F residue 164 type sequence V description BINDING SITE FOR RESIDUE ANP F 600 source : BC1 12) chain F residue 189 type sequence R description BINDING SITE FOR RESIDUE ANP F 600 source : BC1 13) chain F residue 345 type sequence Y description BINDING SITE FOR RESIDUE ANP F 600 source : BC1 14) chain F residue 418 type sequence F description BINDING SITE FOR RESIDUE ANP F 600 source : BC1 15) chain F residue 421 type sequence A description BINDING SITE FOR RESIDUE ANP F 600 source : BC1 16) chain F residue 424 type sequence F description BINDING SITE FOR RESIDUE ANP F 600 source : BC1 17) chain F residue 162 type catalytic sequence K description 178 source MCSA : MCSA3 18) chain F residue 188 type catalytic sequence E description 178 source MCSA : MCSA3 19) chain F residue 189 type catalytic sequence R description 178 source MCSA : MCSA3 20) chain F residue 157 type MOD_RES sequence G description N6-acetyllysine => ECO:0000250|UniProtKB:Q91VR2 source Swiss-Prot : SWS_FT_FI1 21) chain F residue 189 type MOD_RES sequence R description N6-succinyllysine => ECO:0000250|UniProtKB:Q91VR2 source Swiss-Prot : SWS_FT_FI2 22) chain F residue 74 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P36542 source Swiss-Prot : SWS_FT_FI3 23) chain F residue 111 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P36542 source Swiss-Prot : SWS_FT_FI3 24) chain F residue 209 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P36542 source Swiss-Prot : SWS_FT_FI3 25) chain F residue 214 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P36542 source Swiss-Prot : SWS_FT_FI3 26) chain F residue 472 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P36542 source Swiss-Prot : SWS_FT_FI3 27) chain F residue 148 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q91VR2 source Swiss-Prot : SWS_FT_FI4 28) chain F residue 376 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q91VR2 source Swiss-Prot : SWS_FT_FI4 29) chain F residue 262 type MOD_RES sequence T description Phosphoserine => ECO:0000250|UniProtKB:P36542 source Swiss-Prot : SWS_FT_FI5 30) chain F residue 365 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P06576 source Swiss-Prot : SWS_FT_FI6 31) chain F residue 383 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P10719 source Swiss-Prot : SWS_FT_FI7 32) chain F residue 430 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P56480 source Swiss-Prot : SWS_FT_FI8 33) chain F residue 435 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P56480 source Swiss-Prot : SWS_FT_FI8 34) chain F residue 56 type CARBOHYD sequence S description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9

Display surface Download Links