eF-site ID 5qrc-A PDB Code 5qrc Chain A 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 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 A residue 271 type sequence K description binding site for residue NW4 B 602 source : AC2 4) chain A residue 272 type sequence I description binding site for residue NW4 B 602 source : AC2 5) chain A residue 413 type sequence Y description binding site for residue NW4 B 602 source : AC2 6) chain A residue 257 type sequence S description binding site for residue PLP A 601 source : AC3 7) chain A residue 258 type sequence C description binding site for residue PLP A 601 source : AC3 8) chain A residue 259 type sequence F description binding site for residue PLP A 601 source : AC3 9) chain A residue 262 type sequence N description binding site for residue PLP A 601 source : AC3 10) chain A residue 285 type sequence H description binding site for residue PLP A 601 source : AC3 11) chain A residue 328 type sequence E description binding site for residue PLP A 601 source : AC3 12) chain A residue 332 type sequence S description binding site for residue PLP A 601 source : AC3 13) chain A residue 357 type sequence D description binding site for residue PLP A 601 source : AC3 14) chain A residue 359 type sequence V description binding site for residue PLP A 601 source : AC3 15) chain A residue 360 type sequence H description binding site for residue PLP A 601 source : AC3 16) chain A residue 388 type sequence T description binding site for residue PLP A 601 source : AC3 17) chain A residue 391 type sequence K description binding site for residue PLP A 601 source : AC3 18) chain A residue 389 type ACT_SITE sequence L description ACT_SITE => ECO:0000250|UniProtKB:P18079 source Swiss-Prot : SWS_FT_FI1 19) chain A residue 161 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:P18079 source Swiss-Prot : SWS_FT_FI2 20) chain A residue 278 type BINDING sequence I description BINDING => ECO:0000250|UniProtKB:P18079 source Swiss-Prot : SWS_FT_FI2 21) chain A residue 297 type BINDING sequence A description BINDING => ECO:0000250|UniProtKB:P18079 source Swiss-Prot : SWS_FT_FI2 22) chain A residue 506 type BINDING sequence Y description BINDING => ECO:0000250|UniProtKB:P18079 source Swiss-Prot : SWS_FT_FI2 23) chain A residue 256 type BINDING sequence S description in other chain => ECO:0000269|PubMed:32499479 source Swiss-Prot : SWS_FT_FI3 24) chain A residue 257 type BINDING sequence S description in other chain => ECO:0000269|PubMed:32499479 source Swiss-Prot : SWS_FT_FI3 25) chain A residue 358 type BINDING sequence E description in other chain => ECO:0000269|PubMed:32499479 source Swiss-Prot : SWS_FT_FI3 26) chain A residue 386 type BINDING sequence S description in other chain => ECO:0000269|PubMed:32499479 source Swiss-Prot : SWS_FT_FI3 27) chain A residue 389 type MOD_RES sequence L description N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:32499479 source Swiss-Prot : SWS_FT_FI6 28) chain A residue 330 type BINDING sequence V description in other chain => ECO:0000250|UniProtKB:P18079 source Swiss-Prot : SWS_FT_FI4 29) chain A residue 418 type BINDING sequence I description BINDING => ECO:0000269|PubMed:32499479 source Swiss-Prot : SWS_FT_FI5 30) chain A residue 419 type BINDING sequence F description BINDING => ECO:0000269|PubMed:32499479 source Swiss-Prot : SWS_FT_FI5

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