eF-site ID 6hrh-A PDB Code 6hrh Chain A click to enlarge Title Structure of human erythroid-specific 5'-aminolevulinate synthase, ALAS2 Classification OXIDOREDUCTASE 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 257 type sequence S description binding site for residue PLP A 601 source : AC2 4) chain A residue 258 type sequence C description binding site for residue PLP A 601 source : AC2 5) chain A residue 259 type sequence F description binding site for residue PLP A 601 source : AC2 6) chain A residue 262 type sequence N description binding site for residue PLP A 601 source : AC2 7) chain A residue 285 type sequence H description binding site for residue PLP A 601 source : AC2 8) chain A residue 328 type sequence E description binding site for residue PLP A 601 source : AC2 9) chain A residue 332 type sequence S description binding site for residue PLP A 601 source : AC2 10) chain A residue 357 type sequence D description binding site for residue PLP A 601 source : AC2 11) chain A residue 360 type sequence H description binding site for residue PLP A 601 source : AC2 12) chain A residue 388 type sequence T description binding site for residue PLP A 601 source : AC2 13) chain A residue 391 type sequence K description binding site for residue PLP A 601 source : AC2 14) chain A residue 391 type MOD_RES sequence K description N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:32499479 source Swiss-Prot : SWS_FT_FI6 15) chain A residue 332 type BINDING sequence S description in other chain => ECO:0000250|UniProtKB:P18079 source Swiss-Prot : SWS_FT_FI4 16) chain A residue 420 type BINDING sequence T description BINDING => ECO:0000269|PubMed:32499479 source Swiss-Prot : SWS_FT_FI5 17) chain A residue 421 type BINDING sequence T description BINDING => ECO:0000269|PubMed:32499479 source Swiss-Prot : SWS_FT_FI5 18) chain A residue 391 type ACT_SITE sequence K description ACT_SITE => ECO:0000250|UniProtKB:P18079 source Swiss-Prot : SWS_FT_FI1 19) chain A residue 163 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P18079 source Swiss-Prot : SWS_FT_FI2 20) chain A residue 280 type BINDING sequence S description BINDING => ECO:0000250|UniProtKB:P18079 source Swiss-Prot : SWS_FT_FI2 21) chain A residue 299 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:P18079 source Swiss-Prot : SWS_FT_FI2 22) chain A residue 508 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:P18079 source Swiss-Prot : SWS_FT_FI2 23) chain A residue 360 type BINDING sequence H description in other chain => ECO:0000269|PubMed:32499479 source Swiss-Prot : SWS_FT_FI3 24) chain A residue 388 type BINDING sequence T description in other chain => ECO:0000269|PubMed:32499479 source Swiss-Prot : SWS_FT_FI3 25) chain A residue 258 type BINDING sequence C description in other chain => ECO:0000269|PubMed:32499479 source Swiss-Prot : SWS_FT_FI3 26) chain A residue 259 type BINDING sequence F description in other chain => ECO:0000269|PubMed:32499479 source Swiss-Prot : SWS_FT_FI3

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