eF-site ID 5qrc-AB PDB Code 5qrc Chain A, B click to enlarge Title PanDDA analysis group deposition -- Crystal Structure of human ALAS2A in complex with Z31721798 Classification TRANSFERASE Compound 5-aminolevulinate synthase, erythroid-specific, mitochondrial Source (HEM0_HUMAN) Sequence A:  LYFQSMFSYDQFFRDKIMEKKQDHTYRVFKTVNRWADAYP FAQHFSKDVSVWCSNDYLGMSRHPQVLQATQETLQRHGVG AGGTRNISGTSKFHVELEQELAELHQKDSALLFSSCFVAN DSTLFTLAKILPGCEIYSDAGNHASMIQGIRNSGAAKFVF RHNDPDHLKKLLEKSNPKIPKIVAFETVHSMDGAICPLEE LCDVSHQYGALTFVDEVHAVGLYGSRGAGIGERDGIMHKI DIISGTLGKAFGCVGGYIASTRDLVDMVRSYAAGFIFTTS LPPMVLSGALESVRLLKGEEGQALRRAHQRNVKHMRQLLM DRGLPVIPCPSHIIPIRVGNAALNSKLCDLLLSKHGIYVQ AINYPTVPRGEELLRLAPSPHHSPQMMEDFVEKLLLAWTA VGLPLQNFCRRPVHFELMSEWERSYFGNM B:  LYFQSMFSYDQFFRDKIMEKKQDHTYRVFKTVNRWADAYP FAQHFSSKDVSVWCSNDYLGMSRHPQVLQATQETLQRHGV GAGGTRNISGTSKFHVELEQELAELHQKDSALLFSSCFVA NDSTLFTLAKILPGCEIYSDAGNHASMIQGIRNSGAAKFV FRHNDPDHLKKLLEKSNPKIPKIVAFETVHSMDGAICPLE ELCDVSHQYGALTFVDEVHAVGLYGSRGAGIGERDGIMHK IDIISGTLGKAFGCVGGYIASTRDLVDMVRSYAAGFIFTT SLPPMVLSGALESVRLLKGEEGQALRRAHQRNVKHMRQLL MDRGLPVIPCPSHIIPIRVGNAALNSKLCDLLLSKHGIYV QAINYPTVPRGEELLRLAPSPHHSPQMMEDFVEKLLLAWT AVGLPLQCRRPVHFELMSEWERSYFGNM Description Functional site 1) chain A residue 420 type sequence T description binding site for residue PLP B 601 source : AC1 2) chain A residue 421 type sequence T description binding site for residue PLP B 601 source : AC1 3) chain B residue 257 type sequence S description binding site for residue PLP B 601 source : AC1 4) chain B residue 258 type sequence C description binding site for residue PLP B 601 source : AC1 5) chain B residue 259 type sequence F description binding site for residue PLP B 601 source : AC1 6) chain B residue 262 type sequence N description binding site for residue PLP B 601 source : AC1 7) chain B residue 285 type sequence H description binding site for residue PLP B 601 source : AC1 8) chain B residue 328 type sequence E description binding site for residue PLP B 601 source : AC1 9) chain B residue 332 type sequence S description binding site for residue PLP B 601 source : AC1 10) chain B residue 357 type sequence D description binding site for residue PLP B 601 source : AC1 11) chain B residue 360 type sequence H description binding site for residue PLP B 601 source : AC1 12) chain B residue 388 type sequence T description binding site for residue PLP B 601 source : AC1 13) chain B residue 391 type sequence K description binding site for residue PLP B 601 source : AC1 14) chain A residue 271 type sequence K description binding site for residue NW4 B 602 source : AC2 15) chain A residue 272 type sequence I description binding site for residue NW4 B 602 source : AC2 16) chain A residue 413 type sequence Y description binding site for residue NW4 B 602 source : AC2 17) chain B residue 152 type sequence K description binding site for residue NW4 B 602 source : AC2 18) chain B residue 155 type sequence E description binding site for residue NW4 B 602 source : AC2 19) chain B residue 573 type sequence S description binding site for residue NW4 B 602 source : AC2 20) chain B residue 574 type sequence Y description binding site for residue NW4 B 602 source : AC2 21) chain A residue 257 type sequence S description binding site for residue PLP A 601 source : AC3 22) chain A residue 258 type sequence C description binding site for residue PLP A 601 source : AC3 23) chain A residue 259 type sequence F description binding site for residue PLP A 601 source : AC3 24) chain A residue 262 type sequence N description binding site for residue PLP A 601 source : AC3 25) chain A residue 285 type sequence H description binding site for residue PLP A 601 source : AC3 26) chain A residue 328 type sequence E description binding site for residue PLP A 601 source : AC3 27) chain A residue 332 type sequence S description binding site for residue PLP A 601 source : AC3 28) chain A residue 357 type sequence D description binding site for residue PLP A 601 source : AC3 29) chain A residue 359 type sequence V description binding site for residue PLP A 601 source : AC3 30) chain A residue 360 type sequence H description binding site for residue PLP A 601 source : AC3 31) chain A residue 388 type sequence T description binding site for residue PLP A 601 source : AC3 32) chain A residue 391 type sequence K description binding site for residue PLP A 601 source : AC3 33) chain B residue 419 type sequence F description binding site for residue PLP A 601 source : AC3 34) chain B residue 420 type sequence T description binding site for residue PLP A 601 source : AC3 35) chain B residue 421 type sequence T description binding site for residue PLP A 601 source : AC3 36) chain B residue 388-397 type prosite sequence TLGKAFGCVG description AA_TRANSFER_CLASS_2 Aminotransferases class-II pyridoxal-phosphate attachment site. TLGKAFGCVG source prosite : PS00599 37) chain B residue 389 type ACT_SITE sequence L description ACT_SITE => ECO:0000250|UniProtKB:P18079 source Swiss-Prot : SWS_FT_FI1 38) chain A residue 389 type ACT_SITE sequence L description ACT_SITE => ECO:0000250|UniProtKB:P18079 source Swiss-Prot : SWS_FT_FI1 39) chain B residue 161 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:P18079 source Swiss-Prot : SWS_FT_FI2 40) chain B residue 278 type BINDING sequence I description BINDING => ECO:0000250|UniProtKB:P18079 source Swiss-Prot : SWS_FT_FI2 41) chain B residue 297 type BINDING sequence A description BINDING => ECO:0000250|UniProtKB:P18079 source Swiss-Prot : SWS_FT_FI2 42) chain B residue 506 type BINDING sequence Y description BINDING => ECO:0000250|UniProtKB:P18079 source Swiss-Prot : SWS_FT_FI2 43) chain A residue 161 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:P18079 source Swiss-Prot : SWS_FT_FI2 44) chain A residue 278 type BINDING sequence I description BINDING => ECO:0000250|UniProtKB:P18079 source Swiss-Prot : SWS_FT_FI2 45) chain A residue 297 type BINDING sequence A description BINDING => ECO:0000250|UniProtKB:P18079 source Swiss-Prot : SWS_FT_FI2 46) chain A residue 506 type BINDING sequence Y description BINDING => ECO:0000250|UniProtKB:P18079 source Swiss-Prot : SWS_FT_FI2 47) chain B residue 256 type BINDING sequence S description in other chain => ECO:0000269|PubMed:32499479 source Swiss-Prot : SWS_FT_FI3 48) chain B residue 257 type BINDING sequence S description in other chain => ECO:0000269|PubMed:32499479 source Swiss-Prot : SWS_FT_FI3 49) chain B residue 358 type BINDING sequence E description in other chain => ECO:0000269|PubMed:32499479 source Swiss-Prot : SWS_FT_FI3 50) chain B residue 386 type BINDING sequence S description in other chain => ECO:0000269|PubMed:32499479 source Swiss-Prot : SWS_FT_FI3 51) chain A residue 256 type BINDING sequence S description in other chain => ECO:0000269|PubMed:32499479 source Swiss-Prot : SWS_FT_FI3 52) chain A residue 257 type BINDING sequence S description in other chain => ECO:0000269|PubMed:32499479 source Swiss-Prot : SWS_FT_FI3 53) chain A residue 358 type BINDING sequence E description in other chain => ECO:0000269|PubMed:32499479 source Swiss-Prot : SWS_FT_FI3 54) chain A residue 386 type BINDING sequence S description in other chain => ECO:0000269|PubMed:32499479 source Swiss-Prot : SWS_FT_FI3 55) chain B residue 330 type BINDING sequence V description in other chain => ECO:0000250|UniProtKB:P18079 source Swiss-Prot : SWS_FT_FI4 56) chain A residue 330 type BINDING sequence V description in other chain => ECO:0000250|UniProtKB:P18079 source Swiss-Prot : SWS_FT_FI4 57) chain B residue 418 type BINDING sequence I description BINDING => ECO:0000269|PubMed:32499479 source Swiss-Prot : SWS_FT_FI5 58) chain B residue 419 type BINDING sequence F description BINDING => ECO:0000269|PubMed:32499479 source Swiss-Prot : SWS_FT_FI5 59) chain A residue 418 type BINDING sequence I description BINDING => ECO:0000269|PubMed:32499479 source Swiss-Prot : SWS_FT_FI5 60) chain A residue 419 type BINDING sequence F description BINDING => ECO:0000269|PubMed:32499479 source Swiss-Prot : SWS_FT_FI5 61) chain B residue 389 type MOD_RES sequence L description N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:32499479 source Swiss-Prot : SWS_FT_FI6 62) chain A residue 389 type MOD_RES sequence L description N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:32499479 source Swiss-Prot : SWS_FT_FI6

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