eF-site ID 1umy-ABCD
PDB Code 1umy
Chain A, B, C, D

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Title BHMT from rat liver
Classification TRANSFERASE
Compound Betaine--homocysteine S-methyltransferase 1
Source (BHMT1_RAT)
Sequence A:  KRGILERLNAGEVVIGDGGFVFALEKRGYVKAGPWTPEAA
VEHPEAVRQLHREFLRAGSNVMQTFTFYASSGQKVNEAAC
DIARQVADEGDALVAGGVSQTPSYLSCKSETEVKKIFHQQ
LEVFMKKNVDFLIAEYFEHVEEAVWAVEALKTSGKPIAAT
MCIGPEGDLHGVSPGECAVRLVKAGAAIVGVNCHFDPSTS
LQTIKLMKEGLEAARLKAYLMSQPLAYHTPDCGKQGFIDL
PEFPFGLEPRVATRWDIQKYAREAYNLGVRYIGGCCGFEP
YHIRAIAEELAPERGFLPPASEKHGSWGSGLDMHTKPWIR
ARARKEYWQNLRIASGRPYNPSMSKPDAWGVTKGAAELMQ
QKEATTEQQLRALFE
B:  KRGILERLNAGEVVIGDGGFVFALEKRGYVKAGPWTPEAA
VEHPEAVRQLHREFLRAGSNVMQTFTFYASEDAEKISGQK
VNEAACDIARQVADEGDALVAGGVSQTPSYLSCKSETEVK
KIFHQQLEVFMKKNVDFLIAEYFEHVEEAVWAVEALKTSG
KPIAATMCIGPEGDLHGVSPGECAVRLVKAGAAIVGVNCH
FDPSTSLQTIKLMKEGLEAARLKAYLMSQPLAYHTPDCGK
QGFIDLPEFPFGLEPRVATRWDIQKYAREAYNLGVRYIGG
CCGFEPYHIRAIAEELAPERGFLPPASEKHGSWGSGLDMH
TKPWIRARARKEYWQNLRIASGRPYNPSMSKPDAWGVTKG
AAELMQQKEATTEQQLRALFE
C:  KRGILERLNAGEVVIGDGGFVFALEKRGYVKAGPWTPEAA
VEHPEAVRQLHREFLRAGSNVMQTFTFYASGQKVNEAACD
IARQVADEGDALVAGGVSQTPSYLSCKSETEVKKIFHQQL
EVFMKKNVDFLIAEYFEHVEEAVWAVEALKTSGKPIAATM
CIGPEGDLHGVSPGECAVRLVKAGAAIVGVNCHFDPSTSL
QTIKLMKEGLEAARLKAYLMSQPLAYHTPDCGKQGFIDLP
EFPFGLEPRVATRWDIQKYAREAYNLGVRYIGGCCGFEPY
HIRAIAEELAPERGFLPPASEKHGSWGSGLDMHTKPWIRA
RARKEYWQNLRIASGRPYNPSMSKPDAWGVTKGAAELMQQ
KEATTEQQLRALFEKQKFKSA
D:  KRGILERLNAGEVVIGDGGFVFALEKRGYVKAGPWTPEAA
VEHPEAVRQLHREFLRAGSNVMQTFTFYAKISGQKVNEAA
CDIARQVADEGDALVAGGVSQTPSYLSCKSETEVKKIFHQ
QLEVFMKKNVDFLIAEYFEHVEEAVWAVEALKTSGKPIAA
TMCIGPEGDLHGVSPGECAVRLVKAGAAIVGVNCHFDPST
SLQTIKLMKEGLEAARLKAYLMSQPLAYHTPDCGKQGFID
LPEFPFGLEPRVATRWDIQKYAREAYNLGVRYIGGCCGFE
PYHIRAIAEELAPERGFLPPASEKHGSWGSGLDMHTKPWI
RARARKEYWQNLRIASGRPYNPSMSKPDAWGVTKGAAELM
QQKEATTEQQLRALFEKQKFKS
Description


Functional site

1) chain A
residue 160
type
sequence Y
description BINDING SITE FOR RESIDUE ZN A1399
source : AC1

2) chain A
residue 217
type
sequence C
description BINDING SITE FOR RESIDUE ZN A1399
source : AC1

3) chain A
residue 299
type
sequence C
description BINDING SITE FOR RESIDUE ZN A1399
source : AC1

4) chain A
residue 300
type
sequence C
description BINDING SITE FOR RESIDUE ZN A1399
source : AC1

5) chain B
residue 160
type
sequence Y
description BINDING SITE FOR RESIDUE ZN B1399
source : AC2

6) chain B
residue 217
type
sequence C
description BINDING SITE FOR RESIDUE ZN B1399
source : AC2

7) chain B
residue 299
type
sequence C
description BINDING SITE FOR RESIDUE ZN B1399
source : AC2

8) chain B
residue 300
type
sequence C
description BINDING SITE FOR RESIDUE ZN B1399
source : AC2

9) chain C
residue 160
type
sequence Y
description BINDING SITE FOR RESIDUE ZN C1406
source : AC3

10) chain C
residue 217
type
sequence C
description BINDING SITE FOR RESIDUE ZN C1406
source : AC3

11) chain C
residue 299
type
sequence C
description BINDING SITE FOR RESIDUE ZN C1406
source : AC3

12) chain C
residue 300
type
sequence C
description BINDING SITE FOR RESIDUE ZN C1406
source : AC3

13) chain D
residue 160
type
sequence Y
description BINDING SITE FOR RESIDUE ZN D1405
source : AC4

14) chain D
residue 217
type
sequence C
description BINDING SITE FOR RESIDUE ZN D1405
source : AC4

15) chain D
residue 299
type
sequence C
description BINDING SITE FOR RESIDUE ZN D1405
source : AC4

16) chain D
residue 300
type
sequence C
description BINDING SITE FOR RESIDUE ZN D1405
source : AC4

17) chain A
residue 217
type BINDING
sequence C
description BINDING => ECO:0000250|UniProtKB:Q93088, ECO:0000255|PROSITE-ProRule:PRU00333
source Swiss-Prot : SWS_FT_FI1

18) chain D
residue 217
type BINDING
sequence C
description BINDING => ECO:0000250|UniProtKB:Q93088, ECO:0000255|PROSITE-ProRule:PRU00333
source Swiss-Prot : SWS_FT_FI1

19) chain D
residue 299
type BINDING
sequence C
description BINDING => ECO:0000250|UniProtKB:Q93088, ECO:0000255|PROSITE-ProRule:PRU00333
source Swiss-Prot : SWS_FT_FI1

20) chain D
residue 300
type BINDING
sequence C
description BINDING => ECO:0000250|UniProtKB:Q93088, ECO:0000255|PROSITE-ProRule:PRU00333
source Swiss-Prot : SWS_FT_FI1

21) chain A
residue 299
type BINDING
sequence C
description BINDING => ECO:0000250|UniProtKB:Q93088, ECO:0000255|PROSITE-ProRule:PRU00333
source Swiss-Prot : SWS_FT_FI1

22) chain A
residue 300
type BINDING
sequence C
description BINDING => ECO:0000250|UniProtKB:Q93088, ECO:0000255|PROSITE-ProRule:PRU00333
source Swiss-Prot : SWS_FT_FI1

23) chain B
residue 217
type BINDING
sequence C
description BINDING => ECO:0000250|UniProtKB:Q93088, ECO:0000255|PROSITE-ProRule:PRU00333
source Swiss-Prot : SWS_FT_FI1

24) chain B
residue 299
type BINDING
sequence C
description BINDING => ECO:0000250|UniProtKB:Q93088, ECO:0000255|PROSITE-ProRule:PRU00333
source Swiss-Prot : SWS_FT_FI1

25) chain B
residue 300
type BINDING
sequence C
description BINDING => ECO:0000250|UniProtKB:Q93088, ECO:0000255|PROSITE-ProRule:PRU00333
source Swiss-Prot : SWS_FT_FI1

26) chain C
residue 217
type BINDING
sequence C
description BINDING => ECO:0000250|UniProtKB:Q93088, ECO:0000255|PROSITE-ProRule:PRU00333
source Swiss-Prot : SWS_FT_FI1

27) chain C
residue 299
type BINDING
sequence C
description BINDING => ECO:0000250|UniProtKB:Q93088, ECO:0000255|PROSITE-ProRule:PRU00333
source Swiss-Prot : SWS_FT_FI1

28) chain C
residue 300
type BINDING
sequence C
description BINDING => ECO:0000250|UniProtKB:Q93088, ECO:0000255|PROSITE-ProRule:PRU00333
source Swiss-Prot : SWS_FT_FI1

29) chain A
residue 40
type MOD_RES
sequence K
description N6-succinyllysine => ECO:0000250|UniProtKB:O35490
source Swiss-Prot : SWS_FT_FI2

30) chain B
residue 98
type MOD_RES
sequence K
description N6-succinyllysine => ECO:0000250|UniProtKB:O35490
source Swiss-Prot : SWS_FT_FI2

31) chain B
residue 232
type MOD_RES
sequence K
description N6-succinyllysine => ECO:0000250|UniProtKB:O35490
source Swiss-Prot : SWS_FT_FI2

32) chain B
residue 241
type MOD_RES
sequence K
description N6-succinyllysine => ECO:0000250|UniProtKB:O35490
source Swiss-Prot : SWS_FT_FI2

33) chain B
residue 340
type MOD_RES
sequence K
description N6-succinyllysine => ECO:0000250|UniProtKB:O35490
source Swiss-Prot : SWS_FT_FI2

34) chain B
residue 377
type MOD_RES
sequence K
description N6-succinyllysine => ECO:0000250|UniProtKB:O35490
source Swiss-Prot : SWS_FT_FI2

35) chain C
residue 40
type MOD_RES
sequence K
description N6-succinyllysine => ECO:0000250|UniProtKB:O35490
source Swiss-Prot : SWS_FT_FI2

36) chain C
residue 98
type MOD_RES
sequence K
description N6-succinyllysine => ECO:0000250|UniProtKB:O35490
source Swiss-Prot : SWS_FT_FI2

37) chain C
residue 232
type MOD_RES
sequence K
description N6-succinyllysine => ECO:0000250|UniProtKB:O35490
source Swiss-Prot : SWS_FT_FI2

38) chain C
residue 241
type MOD_RES
sequence K
description N6-succinyllysine => ECO:0000250|UniProtKB:O35490
source Swiss-Prot : SWS_FT_FI2

39) chain C
residue 340
type MOD_RES
sequence K
description N6-succinyllysine => ECO:0000250|UniProtKB:O35490
source Swiss-Prot : SWS_FT_FI2

40) chain C
residue 377
type MOD_RES
sequence K
description N6-succinyllysine => ECO:0000250|UniProtKB:O35490
source Swiss-Prot : SWS_FT_FI2

41) chain D
residue 40
type MOD_RES
sequence K
description N6-succinyllysine => ECO:0000250|UniProtKB:O35490
source Swiss-Prot : SWS_FT_FI2

42) chain D
residue 93
type MOD_RES
sequence K
description N6-succinyllysine => ECO:0000250|UniProtKB:O35490
source Swiss-Prot : SWS_FT_FI2

43) chain D
residue 98
type MOD_RES
sequence K
description N6-succinyllysine => ECO:0000250|UniProtKB:O35490
source Swiss-Prot : SWS_FT_FI2

44) chain D
residue 232
type MOD_RES
sequence K
description N6-succinyllysine => ECO:0000250|UniProtKB:O35490
source Swiss-Prot : SWS_FT_FI2

45) chain D
residue 241
type MOD_RES
sequence K
description N6-succinyllysine => ECO:0000250|UniProtKB:O35490
source Swiss-Prot : SWS_FT_FI2

46) chain D
residue 340
type MOD_RES
sequence K
description N6-succinyllysine => ECO:0000250|UniProtKB:O35490
source Swiss-Prot : SWS_FT_FI2

47) chain D
residue 377
type MOD_RES
sequence K
description N6-succinyllysine => ECO:0000250|UniProtKB:O35490
source Swiss-Prot : SWS_FT_FI2

48) chain A
residue 98
type MOD_RES
sequence K
description N6-succinyllysine => ECO:0000250|UniProtKB:O35490
source Swiss-Prot : SWS_FT_FI2

49) chain A
residue 232
type MOD_RES
sequence K
description N6-succinyllysine => ECO:0000250|UniProtKB:O35490
source Swiss-Prot : SWS_FT_FI2

50) chain A
residue 241
type MOD_RES
sequence K
description N6-succinyllysine => ECO:0000250|UniProtKB:O35490
source Swiss-Prot : SWS_FT_FI2

51) chain A
residue 340
type MOD_RES
sequence K
description N6-succinyllysine => ECO:0000250|UniProtKB:O35490
source Swiss-Prot : SWS_FT_FI2

52) chain A
residue 377
type MOD_RES
sequence K
description N6-succinyllysine => ECO:0000250|UniProtKB:O35490
source Swiss-Prot : SWS_FT_FI2

53) chain B
residue 40
type MOD_RES
sequence K
description N6-succinyllysine => ECO:0000250|UniProtKB:O35490
source Swiss-Prot : SWS_FT_FI2

54) chain B
residue 93
type MOD_RES
sequence K
description N6-succinyllysine => ECO:0000250|UniProtKB:O35490
source Swiss-Prot : SWS_FT_FI2

55) chain A
residue 330
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:22673903
source Swiss-Prot : SWS_FT_FI3

56) chain B
residue 330
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:22673903
source Swiss-Prot : SWS_FT_FI3

57) chain C
residue 330
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:22673903
source Swiss-Prot : SWS_FT_FI3

58) chain D
residue 330
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:22673903
source Swiss-Prot : SWS_FT_FI3


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