eF-site ID 5qrc-B PDB Code 5qrc Chain 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 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 262 type sequence N description binding site for residue PLP B 601 source : AC1 5) chain B residue 285 type sequence H description binding site for residue PLP B 601 source : AC1 6) chain B residue 328 type sequence E description binding site for residue PLP B 601 source : AC1 7) chain B residue 332 type sequence S description binding site for residue PLP B 601 source : AC1 8) chain B residue 357 type sequence D description binding site for residue PLP B 601 source : AC1 9) chain B residue 360 type sequence H description binding site for residue PLP B 601 source : AC1 10) chain B residue 388 type sequence T description binding site for residue PLP B 601 source : AC1 11) chain B residue 391 type sequence K description binding site for residue PLP B 601 source : AC1 12) chain B residue 152 type sequence K description binding site for residue NW4 B 602 source : AC2 13) chain B residue 155 type sequence E description binding site for residue NW4 B 602 source : AC2 14) chain B residue 573 type sequence S description binding site for residue NW4 B 602 source : AC2 15) chain B residue 574 type sequence Y description binding site for residue NW4 B 602 source : AC2 16) chain B residue 419 type sequence F description binding site for residue PLP A 601 source : AC3 17) chain B residue 420 type sequence T description binding site for residue PLP A 601 source : AC3 18) chain B residue 421 type sequence T description binding site for residue PLP A 601 source : AC3 19) chain B residue 389 type ACT_SITE sequence L description ACT_SITE => ECO:0000250|UniProtKB:P18079 source Swiss-Prot : SWS_FT_FI1 20) chain B residue 161 type BINDING sequence T description BINDING => ECO:0000250|UniProtKB:P18079 source Swiss-Prot : SWS_FT_FI2 21) chain B residue 278 type BINDING sequence I description BINDING => ECO:0000250|UniProtKB:P18079 source Swiss-Prot : SWS_FT_FI2 22) chain B residue 297 type BINDING sequence A description BINDING => ECO:0000250|UniProtKB:P18079 source Swiss-Prot : SWS_FT_FI2 23) chain B residue 506 type BINDING sequence Y description BINDING => ECO:0000250|UniProtKB:P18079 source Swiss-Prot : SWS_FT_FI2 24) chain B residue 256 type BINDING sequence S description in other chain => ECO:0000269|PubMed:32499479 source Swiss-Prot : SWS_FT_FI3 25) chain B residue 257 type BINDING sequence S description in other chain => ECO:0000269|PubMed:32499479 source Swiss-Prot : SWS_FT_FI3 26) chain B residue 358 type BINDING sequence E description in other chain => ECO:0000269|PubMed:32499479 source Swiss-Prot : SWS_FT_FI3 27) chain B residue 386 type BINDING sequence S description in other chain => ECO:0000269|PubMed:32499479 source Swiss-Prot : SWS_FT_FI3 28) chain B residue 389 type MOD_RES sequence L description N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:32499479 source Swiss-Prot : SWS_FT_FI6 29) 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 30) chain B residue 330 type BINDING sequence V description in other chain => ECO:0000250|UniProtKB:P18079 source Swiss-Prot : SWS_FT_FI4 31) chain B residue 418 type BINDING sequence I description BINDING => ECO:0000269|PubMed:32499479 source Swiss-Prot : SWS_FT_FI5 32) chain B residue 419 type BINDING sequence F description BINDING => ECO:0000269|PubMed:32499479 source Swiss-Prot : SWS_FT_FI5

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