eF-site ID 2jj2-M PDB Code 2jj2 Chain M 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 M:  TTGRIVAVIGAVVDVQFDEGLPPILNALEVQGRETRLVLE VAQHLGESTVRTIAMDGTEGLVRGQKVLDSGAPIRIPVGP ETLGRIMNVIGEPIDERGPIKTKQFAAIHAEAPEFVEMSV EQEILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIME LINNVAKAHGGYSVFAGVGERTREGNDLYHEMIESGVINL KDATSKVALVYGQMNEPPGARARVALTGLTVAEYFRDQEG QDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATD MGTMQERITTTKKGSITSVQAIYVPADDLTDPAPATTFAH LDATTVLSRAIAELGIYPAVDPLDSTSRIMDPNIVGSEHY DVARGVQKILQDYKSLQDIIAILGMDELSEEDKLTVSRAR KIQRFLSQPFQVAEVFTGHLGKLVPLKETIKGFQQILAGE YDHLPEQAFYMVGPIEEAVAKADKLA Description Functional site 1) chain M residue 368 type sequence Y description BINDING SITE FOR RESIDUE ANP J 1511 source : CC9 2) chain M residue 158 type sequence A description BINDING SITE FOR RESIDUE ANP M 1475 source : DC9 3) chain M residue 159 type sequence G description BINDING SITE FOR RESIDUE ANP M 1475 source : DC9 4) chain M residue 160 type sequence V description BINDING SITE FOR RESIDUE ANP M 1475 source : DC9 5) chain M residue 161 type sequence G description BINDING SITE FOR RESIDUE ANP M 1475 source : DC9 6) chain M residue 162 type sequence K description BINDING SITE FOR RESIDUE ANP M 1475 source : DC9 7) chain M residue 163 type sequence T description BINDING SITE FOR RESIDUE ANP M 1475 source : DC9 8) chain M residue 164 type sequence V description BINDING SITE FOR RESIDUE ANP M 1475 source : DC9 9) chain M residue 188 type sequence E description BINDING SITE FOR RESIDUE ANP M 1475 source : DC9 10) chain M residue 189 type sequence R description BINDING SITE FOR RESIDUE ANP M 1475 source : DC9 11) chain M residue 345 type sequence Y description BINDING SITE FOR RESIDUE ANP M 1475 source : DC9 12) chain M residue 418 type sequence F description BINDING SITE FOR RESIDUE ANP M 1475 source : DC9 13) chain M residue 421 type sequence A description BINDING SITE FOR RESIDUE ANP M 1475 source : DC9 14) chain M residue 424 type sequence F description BINDING SITE FOR RESIDUE ANP M 1475 source : DC9 15) chain M residue 425 type sequence T description BINDING SITE FOR RESIDUE ANP M 1475 source : DC9 16) chain M residue 163 type sequence T description BINDING SITE FOR RESIDUE MG M 1476 source : EC1 17) chain M residue 278 type sequence A description BINDING SITE FOR RESIDUE QUE N 1273 source : EC2 18) chain M residue 279 type sequence V description BINDING SITE FOR RESIDUE QUE N 1273 source : EC2 19) chain M residue 162 type catalytic sequence K description 178 source MCSA : MCSA6 20) chain M residue 188 type catalytic sequence E description 178 source MCSA : MCSA6 21) chain M residue 189 type catalytic sequence R description 178 source MCSA : MCSA6 22) chain M residue 157 type MOD_RES sequence G description N6-acetyllysine => ECO:0000250|UniProtKB:Q91VR2 source Swiss-Prot : SWS_FT_FI1 23) chain M residue 189 type MOD_RES sequence R description N6-succinyllysine => ECO:0000250|UniProtKB:Q91VR2 source Swiss-Prot : SWS_FT_FI2 24) chain M residue 74 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P36542 source Swiss-Prot : SWS_FT_FI3 25) chain M residue 111 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P36542 source Swiss-Prot : SWS_FT_FI3 26) chain M residue 209 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P36542 source Swiss-Prot : SWS_FT_FI3 27) chain M residue 214 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P36542 source Swiss-Prot : SWS_FT_FI3 28) chain M residue 472 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P36542 source Swiss-Prot : SWS_FT_FI3 29) chain M residue 148 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q91VR2 source Swiss-Prot : SWS_FT_FI4 30) chain M residue 376 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q91VR2 source Swiss-Prot : SWS_FT_FI4 31) chain M residue 262 type MOD_RES sequence T description Phosphoserine => ECO:0000250|UniProtKB:P36542 source Swiss-Prot : SWS_FT_FI5 32) chain M residue 365 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P06576 source Swiss-Prot : SWS_FT_FI6 33) chain M residue 383 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P10719 source Swiss-Prot : SWS_FT_FI7 34) chain M residue 430 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P56480 source Swiss-Prot : SWS_FT_FI8 35) chain M residue 435 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P56480 source Swiss-Prot : SWS_FT_FI8 36) chain M residue 56 type CARBOHYD sequence S description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9

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