eF-site ID 1h8h-F PDB Code 1h8h Chain F click to enlarge Title Bovine mitochondrial F1-ATPase crystallised in the presence of 5mm AMPPNP Classification HYDROLASE Compound BOVINE MITOCHONDRIAL F1-ATPASE 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 163 type sequence T description BINDING SITE FOR RESIDUE MG F 601 source : AC6 2) chain F residue 192 type sequence E description BINDING SITE FOR RESIDUE MG F 601 source : AC6 3) chain F residue 158 type sequence A description BINDING SITE FOR RESIDUE ATP F 600 source : BC2 4) chain F residue 159 type sequence G description BINDING SITE FOR RESIDUE ATP F 600 source : BC2 5) chain F residue 160 type sequence V description BINDING SITE FOR RESIDUE ATP F 600 source : BC2 6) chain F residue 161 type sequence G description BINDING SITE FOR RESIDUE ATP F 600 source : BC2 7) chain F residue 162 type sequence K description BINDING SITE FOR RESIDUE ATP F 600 source : BC2 8) chain F residue 163 type sequence T description BINDING SITE FOR RESIDUE ATP F 600 source : BC2 9) chain F residue 164 type sequence V description BINDING SITE FOR RESIDUE ATP F 600 source : BC2 10) chain F residue 189 type sequence R description BINDING SITE FOR RESIDUE ATP F 600 source : BC2 11) chain F residue 345 type sequence Y description BINDING SITE FOR RESIDUE ATP F 600 source : BC2 12) chain F residue 418 type sequence F description BINDING SITE FOR RESIDUE ATP F 600 source : BC2 13) chain F residue 421 type sequence A description BINDING SITE FOR RESIDUE ATP F 600 source : BC2 14) chain F residue 424 type sequence F description BINDING SITE FOR RESIDUE ATP F 600 source : BC2 15) chain F residue 425 type sequence T description BINDING SITE FOR RESIDUE ATP F 600 source : BC2 16) chain F residue 162 type catalytic sequence K description 178 source MCSA : MCSA3 17) chain F residue 188 type catalytic sequence E description 178 source MCSA : MCSA3 18) chain F residue 189 type catalytic sequence R description 178 source MCSA : MCSA3 19) chain F residue 157 type MOD_RES sequence G description N6-acetyllysine => ECO:0000250|UniProtKB:Q91VR2 source Swiss-Prot : SWS_FT_FI1 20) chain F residue 189 type MOD_RES sequence R description N6-succinyllysine => ECO:0000250|UniProtKB:Q91VR2 source Swiss-Prot : SWS_FT_FI2 21) chain F residue 74 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P36542 source Swiss-Prot : SWS_FT_FI3 22) chain F residue 111 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P36542 source Swiss-Prot : SWS_FT_FI3 23) chain F residue 209 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P36542 source Swiss-Prot : SWS_FT_FI3 24) chain F residue 214 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P36542 source Swiss-Prot : SWS_FT_FI3 25) chain F residue 472 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P36542 source Swiss-Prot : SWS_FT_FI3 26) chain F residue 148 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q91VR2 source Swiss-Prot : SWS_FT_FI4 27) chain F residue 376 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q91VR2 source Swiss-Prot : SWS_FT_FI4 28) chain F residue 262 type MOD_RES sequence T description Phosphoserine => ECO:0000250|UniProtKB:P36542 source Swiss-Prot : SWS_FT_FI5 29) chain F residue 365 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P06576 source Swiss-Prot : SWS_FT_FI6 30) chain F residue 383 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P10719 source Swiss-Prot : SWS_FT_FI7 31) chain F residue 430 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P56480 source Swiss-Prot : SWS_FT_FI8 32) chain F residue 435 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P56480 source Swiss-Prot : SWS_FT_FI8 33) chain F residue 56 type CARBOHYD sequence S description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9

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