eF-site ID 1cw3-D PDB Code 1cw3 Chain D click to enlarge Title HUMAN MITOCHONDRIAL ALDEHYDE DEHYDROGENASE COMPLEXED WITH NAD+ AND MN2+ Classification OXIDOREDUCTASE Compound MITOCHONDRIAL ALDEHYDE DEHYDROGENASE Source Homo sapiens (Human) (ALDH2_HUMAN) Sequence D:  AVPAPNQQPEVFCNQIFINNEWHDAVSRKTFPTVNPSTGE VICQVAEGDKEDVDKAVKAARAAFQLGSPWRRMDASHRGR LLNRLADLIERDRTYLAALETLDNGKPYVISYLVDLDMVL KCLRYYAGWADKYHGKTIPIDGDFFSYTRHEPVGVCGQII PWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLTALYVAN LIKEAGFPPGVVNIVPGFGPTAGAAIASHEDVDKVAFTGS TEIGRVIQVAAGSSNLKRVTLELGGKSPNIIMSDADMDWA VEQAHFALFFNQGQCCCAGSRTFVQEDIYDEFVERSVARA KSRVVGNPFDSKTEQGPQVDETQFKKILGYINTGKQEGAK LLCGGGIAADRGYFIQPTVFGDVQDGMTIAKEEIFGPVMQ ILKFKTIEEVVGRANNSTYGLAAAVFTKDLDKANYLSQAL QAGTVWVNCYDVFGAQSPFGGYKMSGSGRELGEYGLQAYT EVKTVTVKVPQKNS Description Functional site 1) chain D residue 40 type sequence V description BINDING SITE FOR RESIDUE MG D 4501 source : BC3 2) chain D residue 109 type sequence D description BINDING SITE FOR RESIDUE MG D 4501 source : BC3 3) chain D residue 196 type sequence Q description BINDING SITE FOR RESIDUE MG D 4501 source : BC3 4) chain D residue 165 type sequence I description BINDING SITE FOR RESIDUE NAD D 4502 source : CC2 5) chain D residue 166 type sequence I description BINDING SITE FOR RESIDUE NAD D 4502 source : CC2 6) chain D residue 167 type sequence P description BINDING SITE FOR RESIDUE NAD D 4502 source : CC2 7) chain D residue 168 type sequence W description BINDING SITE FOR RESIDUE NAD D 4502 source : CC2 8) chain D residue 169 type sequence N description BINDING SITE FOR RESIDUE NAD D 4502 source : CC2 9) chain D residue 192 type sequence K description BINDING SITE FOR RESIDUE NAD D 4502 source : CC2 10) chain D residue 195 type sequence E description BINDING SITE FOR RESIDUE NAD D 4502 source : CC2 11) chain D residue 225 type sequence G description BINDING SITE FOR RESIDUE NAD D 4502 source : CC2 12) chain D residue 229 type sequence G description BINDING SITE FOR RESIDUE NAD D 4502 source : CC2 13) chain D residue 230 type sequence A description BINDING SITE FOR RESIDUE NAD D 4502 source : CC2 14) chain D residue 243 type sequence F description BINDING SITE FOR RESIDUE NAD D 4502 source : CC2 15) chain D residue 245 type sequence G description BINDING SITE FOR RESIDUE NAD D 4502 source : CC2 16) chain D residue 246 type sequence S description BINDING SITE FOR RESIDUE NAD D 4502 source : CC2 17) chain D residue 249 type sequence I description BINDING SITE FOR RESIDUE NAD D 4502 source : CC2 18) chain D residue 253 type sequence I description BINDING SITE FOR RESIDUE NAD D 4502 source : CC2 19) chain D residue 269 type sequence L description BINDING SITE FOR RESIDUE NAD D 4502 source : CC2 20) chain D residue 270 type sequence G description BINDING SITE FOR RESIDUE NAD D 4502 source : CC2 21) chain D residue 302 type sequence C description BINDING SITE FOR RESIDUE NAD D 4502 source : CC2 22) chain D residue 349 type sequence Q description BINDING SITE FOR RESIDUE NAD D 4502 source : CC2 23) chain D residue 352 type sequence K description BINDING SITE FOR RESIDUE NAD D 4502 source : CC2 24) chain D residue 399 type sequence E description BINDING SITE FOR RESIDUE NAD D 4502 source : CC2 25) chain D residue 401 type sequence F description BINDING SITE FOR RESIDUE NAD D 4502 source : CC2 26) chain D residue 268 type ACT_SITE sequence E description Proton acceptor source Swiss-Prot : SWS_FT_FI1 27) chain D residue 302 type ACT_SITE sequence C description Nucleophile source Swiss-Prot : SWS_FT_FI2 28) chain D residue 169 type SITE sequence N description Transition state stabilizer => ECO:0000250|UniProtKB:P20000 source Swiss-Prot : SWS_FT_FI4 29) chain D residue 35 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 30) chain D residue 56 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 31) chain D residue 61 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 32) chain D residue 142 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 33) chain D residue 351 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 34) chain D residue 366 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 35) chain D residue 409 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 36) chain D residue 411 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 37) chain D residue 434 type MOD_RES sequence K description N6-acetyllysine => ECO:0000250|UniProtKB:P47738 source Swiss-Prot : SWS_FT_FI5 38) chain D residue 192 type catalytic sequence K description 803 source MCSA : MCSA4 39) chain D residue 268 type catalytic sequence E description 803 source MCSA : MCSA4 40) chain D residue 302 type catalytic sequence C description 803 source MCSA : MCSA4 41) chain D residue 399 type catalytic sequence E description 803 source MCSA : MCSA4 42) chain D residue 245 type BINDING sequence G description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3

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