eF-site ID 2jj2-F PDB Code 2jj2 Chain F click to enlarge Title The Structure of F1-ATPase inhibited by quercetin. Classification HYDROLASE Compound ATP SYNTHASE SUBUNIT ALPHA HEART ISOFORM Source ORGANISM_COMMON: BOVINE; 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 266 type sequence S description BINDING SITE FOR RESIDUE GOL B 1513 source : AC8 2) chain F residue 279 type sequence V description BINDING SITE FOR RESIDUE GOL B 1513 source : AC8 3) chain F residue 368 type sequence Y description BINDING SITE FOR RESIDUE ANP C 1511 source : AC9 4) chain F residue 158 type sequence A description BINDING SITE FOR RESIDUE ANP F 1475 source : BC8 5) chain F residue 159 type sequence G description BINDING SITE FOR RESIDUE ANP F 1475 source : BC8 6) chain F residue 160 type sequence V description BINDING SITE FOR RESIDUE ANP F 1475 source : BC8 7) chain F residue 161 type sequence G description BINDING SITE FOR RESIDUE ANP F 1475 source : BC8 8) chain F residue 162 type sequence K description BINDING SITE FOR RESIDUE ANP F 1475 source : BC8 9) chain F residue 163 type sequence T description BINDING SITE FOR RESIDUE ANP F 1475 source : BC8 10) chain F residue 164 type sequence V description BINDING SITE FOR RESIDUE ANP F 1475 source : BC8 11) chain F residue 189 type sequence R description BINDING SITE FOR RESIDUE ANP F 1475 source : BC8 12) chain F residue 345 type sequence Y description BINDING SITE FOR RESIDUE ANP F 1475 source : BC8 13) chain F residue 418 type sequence F description BINDING SITE FOR RESIDUE ANP F 1475 source : BC8 14) chain F residue 421 type sequence A description BINDING SITE FOR RESIDUE ANP F 1475 source : BC8 15) chain F residue 424 type sequence F description BINDING SITE FOR RESIDUE ANP F 1475 source : BC8 16) chain F residue 425 type sequence T description BINDING SITE FOR RESIDUE ANP F 1475 source : BC8 17) chain F residue 163 type sequence T description BINDING SITE FOR RESIDUE MG F 1476 source : BC9 18) chain F residue 279 type sequence V description BINDING SITE FOR RESIDUE QUE G 1273 source : CC1 19) chain F residue 162 type catalytic sequence K description 178 source MCSA : MCSA3 20) chain F residue 188 type catalytic sequence E description 178 source MCSA : MCSA3 21) chain F residue 189 type catalytic sequence R description 178 source MCSA : MCSA3 22) chain F residue 157 type MOD_RES sequence G description N6-acetyllysine => ECO:0000250|UniProtKB:Q91VR2 source Swiss-Prot : SWS_FT_FI1 23) chain F residue 74 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P36542 source Swiss-Prot : SWS_FT_FI3 24) chain F residue 111 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P36542 source Swiss-Prot : SWS_FT_FI3 25) chain F residue 209 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P36542 source Swiss-Prot : SWS_FT_FI3 26) chain F residue 214 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P36542 source Swiss-Prot : SWS_FT_FI3 27) chain F residue 472 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P36542 source Swiss-Prot : SWS_FT_FI3 28) chain F residue 148 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q91VR2 source Swiss-Prot : SWS_FT_FI4 29) chain F residue 376 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q91VR2 source Swiss-Prot : SWS_FT_FI4 30) chain F residue 262 type MOD_RES sequence T description Phosphoserine => ECO:0000250|UniProtKB:P36542 source Swiss-Prot : SWS_FT_FI5 31) chain F residue 365 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P06576 source Swiss-Prot : SWS_FT_FI6 32) chain F residue 383 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P10719 source Swiss-Prot : SWS_FT_FI7 33) chain F residue 430 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P56480 source Swiss-Prot : SWS_FT_FI8 34) chain F residue 435 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P56480 source Swiss-Prot : SWS_FT_FI8 35) 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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