eF-site ID 6hrh-B PDB Code 6hrh Chain B 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 B:  LYFQSMFSYDQFFRDKIMEKKQDHTYRVFKTVNRWADAYP FAQHFSSKDVSVWCSNDYLGMSRHPQVLQATQETLQRHGV GAGGTRNISGTSKFHVELEQELAELHQKDSALLFSSCFVA NDSTLFTLAKILPGCEIYSDAGNHASMIQGIRNSGAAKFV FRHNDPDHLKKLLEKSNPKIPKIVAFETVHSMDGAICPLE ELCDVSHQYGALTFVDEVHAVGLYGSRGAGIGERDGIMHK IDIISGTLGKAFGCVGGYIASTRDLVDMVRSYAAGFIFTT SLPPMVLSGALESVRLLKGEEGQALRRAHQRNVKHMRQLL MDRGLPVIPCPSHIIPIRVGNAALNSKLCDLLLSKHGIYV QAINYPTVPRGEELLRLAPSPHHSPQMMEDFVEKLLLAWT AVGLPLQCRRPVHFELMSEWERSYFGNM Description Functional site 1) chain B residue 257 type sequence S description binding site for residue PLP B 601 source : AC1 2) chain B residue 258 type sequence C description binding site for residue PLP B 601 source : AC1 3) chain B residue 259 type sequence F description binding site for residue PLP B 601 source : AC1 4) chain B residue 285 type sequence H description binding site for residue PLP B 601 source : AC1 5) chain B residue 328 type sequence E description binding site for residue PLP B 601 source : AC1 6) chain B residue 332 type sequence S description binding site for residue PLP B 601 source : AC1 7) chain B residue 357 type sequence D description binding site for residue PLP B 601 source : AC1 8) chain B residue 360 type sequence H description binding site for residue PLP B 601 source : AC1 9) chain B residue 388 type sequence T description binding site for residue PLP B 601 source : AC1 10) chain B residue 391 type sequence K description binding site for residue PLP B 601 source : AC1 11) chain B residue 419 type sequence F description binding site for residue PLP A 601 source : AC2 12) chain B residue 420 type sequence T description binding site for residue PLP A 601 source : AC2 13) chain B residue 421 type sequence T description binding site for residue PLP A 601 source : AC2 14) chain B residue 391 type ACT_SITE sequence K description ACT_SITE => ECO:0000250|UniProtKB:P18079 source Swiss-Prot : SWS_FT_FI1 15) chain B residue 163 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P18079 source Swiss-Prot : SWS_FT_FI2 16) chain B residue 280 type BINDING sequence S description BINDING => ECO:0000250|UniProtKB:P18079 source Swiss-Prot : SWS_FT_FI2 17) chain B residue 299 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:P18079 source Swiss-Prot : SWS_FT_FI2 18) chain B residue 508 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:P18079 source Swiss-Prot : SWS_FT_FI2 19) 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 20) chain B residue 391 type MOD_RES sequence K description N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:32499479 source Swiss-Prot : SWS_FT_FI6 21) chain B residue 258 type BINDING sequence C description in other chain => ECO:0000269|PubMed:32499479 source Swiss-Prot : SWS_FT_FI3 22) chain B residue 259 type BINDING sequence F description in other chain => ECO:0000269|PubMed:32499479 source Swiss-Prot : SWS_FT_FI3 23) chain B residue 360 type BINDING sequence H description in other chain => ECO:0000269|PubMed:32499479 source Swiss-Prot : SWS_FT_FI3 24) chain B residue 388 type BINDING sequence T description in other chain => ECO:0000269|PubMed:32499479 source Swiss-Prot : SWS_FT_FI3 25) chain B residue 332 type BINDING sequence S description in other chain => ECO:0000250|UniProtKB:P18079 source Swiss-Prot : SWS_FT_FI4 26) chain B residue 420 type BINDING sequence T description BINDING => ECO:0000269|PubMed:32499479 source Swiss-Prot : SWS_FT_FI5 27) chain B residue 421 type BINDING sequence T description BINDING => ECO:0000269|PubMed:32499479 source Swiss-Prot : SWS_FT_FI5

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