eF-site ID 2jj2-K PDB Code 2jj2 Chain K 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 K:  TTGRIVAVIGAVVDVQFDEGLPPILNALEVQGRETRLVLE VAQHLGESTVRTIAMDGTEGLVRGQKVLDSGAPIRIPVGP ETLGRIMNVIGEPIDERGPIKTKQFAAIHAEAPEFVEMSV EQEILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIME LINNVAKAHGGYSVFAGVGERTREGNDLYHEMIESGVINL KDATSKVALVYGQMNEPPGARARVALTGLTVAEYFRDQEG QDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATD MGTMQERITTTKKGSITSVQAIYVPADDLTDPAPATTFAH LDATTVLSRAIAELGIYPAVDPLDSTSRIMDPNIVGSEHY DVARGVQKILQDYKSLQDIIAILGMDELSEEDKLTVSRAR KIQRFLSQPFQVAEVFTGHLGKLVPLKETIKGFQQILAGE YDHLPEQAFYMVGPIEEAVAKADKLAE Description Functional site 1) chain K residue 159 type sequence G description BINDING SITE FOR RESIDUE ADP K 1476 source : DC3 2) chain K residue 160 type sequence V description BINDING SITE FOR RESIDUE ADP K 1476 source : DC3 3) chain K residue 161 type sequence G description BINDING SITE FOR RESIDUE ADP K 1476 source : DC3 4) chain K residue 162 type sequence K description BINDING SITE FOR RESIDUE ADP K 1476 source : DC3 5) chain K residue 163 type sequence T description BINDING SITE FOR RESIDUE ADP K 1476 source : DC3 6) chain K residue 164 type sequence V description BINDING SITE FOR RESIDUE ADP K 1476 source : DC3 7) chain K residue 345 type sequence Y description BINDING SITE FOR RESIDUE ADP K 1476 source : DC3 8) chain K residue 418 type sequence F description BINDING SITE FOR RESIDUE ADP K 1476 source : DC3 9) chain K residue 421 type sequence A description BINDING SITE FOR RESIDUE ADP K 1476 source : DC3 10) chain K residue 424 type sequence F description BINDING SITE FOR RESIDUE ADP K 1476 source : DC3 11) chain K residue 425 type sequence T description BINDING SITE FOR RESIDUE ADP K 1476 source : DC3 12) chain K residue 163 type sequence T description BINDING SITE FOR RESIDUE MG K 1477 source : DC4 13) chain K residue 158 type sequence A description BINDING SITE FOR RESIDUE AZI K 1478 source : DC5 14) chain K residue 159 type sequence G description BINDING SITE FOR RESIDUE AZI K 1478 source : DC5 15) chain K residue 162 type sequence K description BINDING SITE FOR RESIDUE AZI K 1478 source : DC5 16) chain K residue 189 type sequence R description BINDING SITE FOR RESIDUE AZI K 1478 source : DC5 17) chain K residue 311 type sequence Y description BINDING SITE FOR RESIDUE AZI K 1478 source : DC5 18) chain K residue 231 type sequence R description BINDING SITE FOR RESIDUE GOL K 1479 source : DC6 19) chain K residue 265 type sequence G description BINDING SITE FOR RESIDUE GOL K 1479 source : DC6 20) chain K residue 274 type sequence R description BINDING SITE FOR RESIDUE GOL K 1479 source : DC6 21) chain K residue 284 type sequence T description BINDING SITE FOR RESIDUE GOL K 1479 source : DC6 22) chain K residue 288 type sequence D description BINDING SITE FOR RESIDUE GOL K 1479 source : DC6 23) chain K residue 127 type sequence S description BINDING SITE FOR RESIDUE GOL K 1480 source : DC7 24) chain K residue 129 type sequence E description BINDING SITE FOR RESIDUE GOL K 1480 source : DC7 25) chain K residue 150 type sequence G description BINDING SITE FOR RESIDUE GOL K 1480 source : DC7 26) chain K residue 162 type catalytic sequence K description 178 source MCSA : MCSA4 27) chain K residue 188 type catalytic sequence E description 178 source MCSA : MCSA4 28) chain K residue 189 type catalytic sequence R description 178 source MCSA : MCSA4 29) chain K residue 157 type MOD_RES sequence G description N6-acetyllysine => ECO:0000250|UniProtKB:Q91VR2 source Swiss-Prot : SWS_FT_FI1 30) chain K residue 262 type MOD_RES sequence T description Phosphoserine => ECO:0000250|UniProtKB:P36542 source Swiss-Prot : SWS_FT_FI5 31) chain K residue 365 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P06576 source Swiss-Prot : SWS_FT_FI6 32) chain K residue 383 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P10719 source Swiss-Prot : SWS_FT_FI7 33) chain K residue 430 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P56480 source Swiss-Prot : SWS_FT_FI8 34) chain K residue 435 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P56480 source Swiss-Prot : SWS_FT_FI8 35) chain K residue 56 type CARBOHYD sequence S description O-linked (GlcNAc) serine => ECO:0000250 source Swiss-Prot : SWS_FT_FI9 36) chain K residue 74 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P36542 source Swiss-Prot : SWS_FT_FI3 37) chain K residue 111 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P36542 source Swiss-Prot : SWS_FT_FI3 38) chain K residue 209 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P36542 source Swiss-Prot : SWS_FT_FI3 39) chain K residue 214 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P36542 source Swiss-Prot : SWS_FT_FI3 40) chain K residue 472 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P36542 source Swiss-Prot : SWS_FT_FI3 41) chain K residue 148 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q91VR2 source Swiss-Prot : SWS_FT_FI4 42) chain K residue 376 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q91VR2 source Swiss-Prot : SWS_FT_FI4

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