eF-site ID 3tg4-A
PDB Code 3tg4
Chain A

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Title Structure of SMYD2 in complex with SAM
Classification TRANSFERASE
Compound N-lysine methyltransferase SMYD2
Source Homo sapiens (Human) (SMYD2_HUMAN)
Sequence A:  LGGLERFCSPGKGRGLRALQPFQVGDLLFSCPAYAYVLTV
NERGNHCEYCFTRKEGLSKCGRCKQAFYCNVECQKEDWPM
HKLECSPMVVFGENWNPSETVRLTARILAKQKIHPERTPS
EKLLAVKEFESHLDKLDNEKKDLIQSDIAALHHFYSKHLG
FPDNDSLVVLFAQVNCNGFTIEDEELSHLGSAIFPDVALM
NHSCCPNVIVTYKGTLAEVRAVQEIKPGEEVFTSYIDLLY
PTEDRNDRLRDSYFFTCECQECTTKDKDKAKVEIRKLSDP
PKAEAIRDMVRYARNVIEEFRRAKHYKSPSELLEICELSQ
EKMSSVFEDSNVYMLHMMYQAMGVCLYMQDWEGALQYGQK
IIKPYSKHYPLYSLNVASMWLKLGRLYMGLEHKAAGEKAL
KKAIAIMEVAHGKDHPYISEIKQEIES
Description


Functional site

1) chain A
residue 16
type
sequence G
description BINDING SITE FOR RESIDUE SAM A 434
source : AC1

2) chain A
residue 17
type
sequence K
description BINDING SITE FOR RESIDUE SAM A 434
source : AC1

3) chain A
residue 19
type
sequence R
description BINDING SITE FOR RESIDUE SAM A 434
source : AC1

4) chain A
residue 137
type
sequence H
description BINDING SITE FOR RESIDUE SAM A 434
source : AC1

5) chain A
residue 181
type
sequence C
description BINDING SITE FOR RESIDUE SAM A 434
source : AC1

6) chain A
residue 182
type
sequence N
description BINDING SITE FOR RESIDUE SAM A 434
source : AC1

7) chain A
residue 203
type
sequence A
description BINDING SITE FOR RESIDUE SAM A 434
source : AC1

8) chain A
residue 204
type
sequence L
description BINDING SITE FOR RESIDUE SAM A 434
source : AC1

9) chain A
residue 206
type
sequence N
description BINDING SITE FOR RESIDUE SAM A 434
source : AC1

10) chain A
residue 207
type
sequence H
description BINDING SITE FOR RESIDUE SAM A 434
source : AC1

11) chain A
residue 240
type
sequence Y
description BINDING SITE FOR RESIDUE SAM A 434
source : AC1

12) chain A
residue 258
type
sequence Y
description BINDING SITE FOR RESIDUE SAM A 434
source : AC1

13) chain A
residue 260
type
sequence F
description BINDING SITE FOR RESIDUE SAM A 434
source : AC1

14) chain A
residue 52
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 435
source : AC2

15) chain A
residue 55
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 435
source : AC2

16) chain A
residue 74
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 435
source : AC2

17) chain A
residue 78
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 435
source : AC2

18) chain A
residue 65
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 436
source : AC3

19) chain A
residue 68
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 436
source : AC3

20) chain A
residue 86
type
sequence H
description BINDING SITE FOR RESIDUE ZN A 436
source : AC3

21) chain A
residue 90
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 436
source : AC3

22) chain A
residue 209
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 437
source : AC4

23) chain A
residue 262
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 437
source : AC4

24) chain A
residue 264
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 437
source : AC4

25) chain A
residue 267
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 437
source : AC4

26) chain A
residue 181
type
sequence C
description BINDING SITE FOR RESIDUE GOL A 438
source : AC5

27) chain A
residue 182
type
sequence N
description BINDING SITE FOR RESIDUE GOL A 438
source : AC5

28) chain A
residue 183
type
sequence G
description BINDING SITE FOR RESIDUE GOL A 438
source : AC5

29) chain A
residue 184
type
sequence F
description BINDING SITE FOR RESIDUE GOL A 438
source : AC5

30) chain A
residue 203
type
sequence A
description BINDING SITE FOR RESIDUE GOL A 438
source : AC5

31) chain A
residue 240
type
sequence Y
description BINDING SITE FOR RESIDUE GOL A 438
source : AC5

32) chain A
residue 258
type
sequence Y
description BINDING SITE FOR RESIDUE GOL A 438
source : AC5

33) chain A
residue 184
type
sequence F
description BINDING SITE FOR RESIDUE GOL A 439
source : AC6

34) chain A
residue 185
type
sequence T
description BINDING SITE FOR RESIDUE GOL A 439
source : AC6

35) chain A
residue 240
type
sequence Y
description BINDING SITE FOR RESIDUE GOL A 439
source : AC6

36) chain A
residue 209
type
sequence C
description BINDING SITE FOR RESIDUE GOL A 440
source : AC7

37) chain A
residue 243
type
sequence L
description BINDING SITE FOR RESIDUE GOL A 440
source : AC7

38) chain A
residue 250
type
sequence R
description BINDING SITE FOR RESIDUE GOL A 440
source : AC7

39) chain A
residue 266
type
sequence E
description BINDING SITE FOR RESIDUE GOL A 440
source : AC7

40) chain A
residue 272
type
sequence K
description BINDING SITE FOR RESIDUE GOL A 440
source : AC7

41) chain A
residue 276
type
sequence K
description BINDING SITE FOR RESIDUE GOL A 440
source : AC7

42) chain A
residue 373
type
sequence H
description BINDING SITE FOR RESIDUE GOL A 440
source : AC7

43) chain A
residue 374
type
sequence Y
description BINDING SITE FOR RESIDUE GOL A 440
source : AC7

44) chain A
residue 375
type
sequence P
description BINDING SITE FOR RESIDUE GOL A 440
source : AC7

45) chain A
residue 190
type
sequence E
description BINDING SITE FOR RESIDUE GOL A 441
source : AC8

46) chain A
residue 390
type
sequence R
description BINDING SITE FOR RESIDUE GOL A 441
source : AC8

47) chain A
residue 391
type
sequence L
description BINDING SITE FOR RESIDUE GOL A 441
source : AC8

48) chain A
residue 38
type
sequence A
description BINDING SITE FOR RESIDUE GOL A 442
source : AC9

49) chain A
residue 39
type
sequence Y
description BINDING SITE FOR RESIDUE GOL A 442
source : AC9

50) chain A
residue 115
type
sequence K
description BINDING SITE FOR RESIDUE GOL A 442
source : AC9

51) chain A
residue 283
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:23186163
source Swiss-Prot : SWS_FT_FI5

52) chain A
residue 17
type BINDING
sequence K
description
source Swiss-Prot : SWS_FT_FI2

53) chain A
residue 206
type BINDING
sequence N
description
source Swiss-Prot : SWS_FT_FI2

54) chain A
residue 258
type BINDING
sequence Y
description
source Swiss-Prot : SWS_FT_FI2

55) chain A
residue 52
type BINDING
sequence C
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00134
source Swiss-Prot : SWS_FT_FI3

56) chain A
residue 55
type BINDING
sequence C
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00134
source Swiss-Prot : SWS_FT_FI3

57) chain A
residue 65
type BINDING
sequence C
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00134
source Swiss-Prot : SWS_FT_FI3

58) chain A
residue 68
type BINDING
sequence C
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00134
source Swiss-Prot : SWS_FT_FI3

59) chain A
residue 74
type BINDING
sequence C
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00134
source Swiss-Prot : SWS_FT_FI3

60) chain A
residue 78
type BINDING
sequence C
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00134
source Swiss-Prot : SWS_FT_FI3

61) chain A
residue 86
type BINDING
sequence H
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00134
source Swiss-Prot : SWS_FT_FI3

62) chain A
residue 90
type BINDING
sequence C
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00134
source Swiss-Prot : SWS_FT_FI3

63) chain A
residue 137
type BINDING
sequence H
description BINDING => ECO:0000255|PROSITE-ProRule:PRU00190, ECO:0000269|PubMed:21724641
source Swiss-Prot : SWS_FT_FI4

64) chain A
residue 52-90
type ZN_FING
sequence CEYCFTRKEGLSKCGRCKQAFYCNVECQKEDWPMHKLEC
description MYND-type => ECO:0000255|PROSITE-ProRule:PRU00134
source Swiss-Prot : SWS_FT_FI1

65) chain A
residue 51-90
type prosite
sequence HCEYCFTRKEGLSKCGRCKQAFYCNVECQKEDWPMHKLEC
description ZF_MYND_1 Zinc finger MYND-type signature. Hcey.Cftrkeglsk........CgrCkqafYCnveCqkedwpm..Hkle.C
source prosite : PS01360


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