eF-site ID 5qrc-AB
PDB Code 5qrc
Chain A, B

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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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