eF-site ID 2jj2-E PDB Code 2jj2 Chain E 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 E:  TTGRIVAVIGAVVDVQFDEGLPPILNALEVQGRETRLVLE VAQHLGESTVRTIAMDGTEGLVRGQKVLDSGAPIRIPVGP ETLGRIMNVIGEPIDERGPIKTKQFAAIHAEAPEFVEMSV EQEILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIME LINNVAKAHGGYSVFAGVGERTREGNDLYHEMIESGVINL KDATSKVALVYGQMNEPPGARARVALTGLTVAEYFRDQEG QDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATD MGTMQERITTTKKGSITSVQAIYVPADDLTDPAPATTFAH LDATTVLSRAIAELGIYPAVDPLDSTSRIMDPNIVGSEHY DVARGVQKILQDYKSLQDIIAILGMDELSEEDKLTVSRAR KIQRFLSQPFQVAEVFTGHLGKLVPLKETIKGFQQILAGE YDHLPEQAFYMVGPIEEAVAKADKLA Description Functional site 1) chain E residue 266 type sequence S description BINDING SITE FOR RESIDUE GOL A 1514 source : AC4 2) chain E residue 280 type sequence G description BINDING SITE FOR RESIDUE GOL A 1514 source : AC4 3) chain E residue 356 type sequence R description BINDING SITE FOR RESIDUE ANP B 1510 source : AC5 4) chain E residue 359 type sequence D description BINDING SITE FOR RESIDUE ANP B 1510 source : AC5 5) chain E residue 157 type sequence G description BINDING SITE FOR RESIDUE PO4 E 1475 source : BC7 6) chain E residue 158 type sequence A description BINDING SITE FOR RESIDUE PO4 E 1475 source : BC7 7) chain E residue 159 type sequence G description BINDING SITE FOR RESIDUE PO4 E 1475 source : BC7 8) chain E residue 162 type sequence K description BINDING SITE FOR RESIDUE PO4 E 1475 source : BC7 9) chain E residue 163 type sequence T description BINDING SITE FOR RESIDUE PO4 E 1475 source : BC7 10) chain E residue 162 type catalytic sequence K description 178 source MCSA : MCSA2 11) chain E residue 188 type catalytic sequence E description 178 source MCSA : MCSA2 12) chain E residue 189 type catalytic sequence R description 178 source MCSA : MCSA2 13) chain E residue 472 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P36542 source Swiss-Prot : SWS_FT_FI3 14) chain E residue 74 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P36542 source Swiss-Prot : SWS_FT_FI3 15) chain E residue 111 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P36542 source Swiss-Prot : SWS_FT_FI3 16) chain E residue 209 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P36542 source Swiss-Prot : SWS_FT_FI3 17) chain E residue 214 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P36542 source Swiss-Prot : SWS_FT_FI3 18) chain E residue 365 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P06576 source Swiss-Prot : SWS_FT_FI6 19) chain E residue 383 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P10719 source Swiss-Prot : SWS_FT_FI7 20) chain E residue 430 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P56480 source Swiss-Prot : SWS_FT_FI8 21) chain E residue 435 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P56480 source Swiss-Prot : SWS_FT_FI8 22) chain E residue 56 type CARBOHYD sequence S description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9

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