eF-site ID 2jj2-L PDB Code 2jj2 Chain L 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 L:  TTGRIVAVIGAVVDVQFDEGLPPILNALEVQGRETRLVLE VAQHLGESTVRTIAMDGTEGLVRGQKVLDSGAPIRIPVGP ETLGRIMNVIGEPIDERGPIKTKQFAAIHAEAPEFVEMSV EQEILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIME LINNVAKAHGGYSVFAGVGERTREGNDLYHEMIESGVINL KDATSKVALVYGQMNEPPGARARVALTGLTVAEYFRDQEG QDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATD MGTMQERITTTKKGSITSVQAIYVPADDLTDPAPATTFAH LDATTVLSRAIAELGIYPAVDPLDSTSRIMDPNIVGSEHY DVARGVQKILQDYKSLQDIIAILGMDELSEEDKLTVSRAR KIQRFLSQPFQVAEVFTGHLGKLVPLKETIKGFQQILAGE YDHLPEQAFYMVGPIEEAVAKADKLA Description Functional site 1) chain L residue 266 type sequence S description BINDING SITE FOR RESIDUE GOL H 1514 source : CC5 2) chain L residue 267 type sequence E description BINDING SITE FOR RESIDUE GOL H 1514 source : CC5 3) chain L residue 280 type sequence G description BINDING SITE FOR RESIDUE GOL H 1514 source : CC5 4) chain L residue 356 type sequence R description BINDING SITE FOR RESIDUE ANP I 1510 source : CC6 5) chain L residue 359 type sequence D description BINDING SITE FOR RESIDUE ANP I 1510 source : CC6 6) chain L residue 157 type sequence G description BINDING SITE FOR RESIDUE PO4 L 1475 source : DC8 7) chain L residue 158 type sequence A description BINDING SITE FOR RESIDUE PO4 L 1475 source : DC8 8) chain L residue 159 type sequence G description BINDING SITE FOR RESIDUE PO4 L 1475 source : DC8 9) chain L residue 160 type sequence V description BINDING SITE FOR RESIDUE PO4 L 1475 source : DC8 10) chain L residue 161 type sequence G description BINDING SITE FOR RESIDUE PO4 L 1475 source : DC8 11) chain L residue 162 type sequence K description BINDING SITE FOR RESIDUE PO4 L 1475 source : DC8 12) chain L residue 163 type sequence T description BINDING SITE FOR RESIDUE PO4 L 1475 source : DC8 13) chain L residue 162 type catalytic sequence K description 178 source MCSA : MCSA5 14) chain L residue 188 type catalytic sequence E description 178 source MCSA : MCSA5 15) chain L residue 189 type catalytic sequence R description 178 source MCSA : MCSA5 16) chain L residue 157 type MOD_RES sequence G description N6-acetyllysine => ECO:0000250|UniProtKB:Q91VR2 source Swiss-Prot : SWS_FT_FI1 17) chain L residue 189 type MOD_RES sequence R description N6-succinyllysine => ECO:0000250|UniProtKB:Q91VR2 source Swiss-Prot : SWS_FT_FI2 18) chain L residue 74 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P36542 source Swiss-Prot : SWS_FT_FI3 19) chain L residue 111 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P36542 source Swiss-Prot : SWS_FT_FI3 20) chain L residue 209 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P36542 source Swiss-Prot : SWS_FT_FI3 21) chain L residue 214 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P36542 source Swiss-Prot : SWS_FT_FI3 22) chain L residue 472 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P36542 source Swiss-Prot : SWS_FT_FI3 23) chain L residue 376 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q91VR2 source Swiss-Prot : SWS_FT_FI4 24) chain L residue 148 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q91VR2 source Swiss-Prot : SWS_FT_FI4 25) chain L residue 262 type MOD_RES sequence T description Phosphoserine => ECO:0000250|UniProtKB:P36542 source Swiss-Prot : SWS_FT_FI5 26) chain L residue 365 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P06576 source Swiss-Prot : SWS_FT_FI6 27) chain L residue 383 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P10719 source Swiss-Prot : SWS_FT_FI7 28) chain L residue 435 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P56480 source Swiss-Prot : SWS_FT_FI8 29) chain L residue 430 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P56480 source Swiss-Prot : SWS_FT_FI8 30) chain L residue 56 type CARBOHYD sequence S description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9

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