eF-site ID 4da4-ABCDEF
PDB Code 4da4
Chain A, B, C, D, E, F

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Title Structure of mouse DNMT1 (731-1602) bound to hemimethylated CpG DNA
Classification Transferase/DNA
Compound DNA (cytosine-5)-methyltransferase 1
Source Mus musculus (Mouse) (4DA4)
Sequence A:  DRISWLGQPMKIEENRTYYQKVSIDEEMLEVGDCVSVIPD
DSSKPLYLARVTALWEDKNGQMMFHAHWFCAGTDTVLGAT
SDPLELFLVGECENMQLSYIHSKVKVIYKAPSENWAMEGG
EDGKTYFFQLWYNQEYARFESPPKTQPTEDNKHKFCLSCI
RLAELRQKEMPKVLEQIEEVDGRVYCSSITKNGVVYRLGD
SVYLPPEAFTFNIKVASPVKRPKKDPVNETLYPEHYRKYS
DYIKGSNLDAPEPYRIGRIKEIHCGKKKGKVNEADIKLRL
YKFYRPENTHRSYNGSYHTDINMLYWSDEEAVVNFSDVQG
RCTVEYGEDLLESIQDYSQGGPDRFYFLEAYNSKTKNFED
PPNHARSPGNIKLPKLRTLDVFSGCGGLSEGFHQAGISET
LWAIEMWDPAAQAFRLNNPGTTVFTEDCNVLLKLVMAGEV
TNSLGQRLPQKGDVEMLCGGPPCQGFSGMNRFNSRTYSKF
KNSLVVSFLSYCDYYRPRFFLLENVRNFVSYRRSMVLKLT
LRCLVRMGYQCTFGVLQAGQYGVAQTRRRAIILAAAPGEK
LPLFPEPLHVFAPRACQLSVVVDDKKFVSNITRLSSGPFR
TITVRDTMSDLPEIQNGASNSEIPYNGEPLSWFQRQLRGS
HYQPILRDHICKDMSPLVAARMRHIPLFPGSDWRDLPNIQ
VRLGDGVIAHKLQYTFHDVKNGYSSTGALRGVCSCAEGKA
CDPESRQFSTLIPWCLPHTGNRHNHWAGLYGRLEWDGFFS
TTVTNPEPMGKQGRVLHPEQHRVVSVRECARSQGFPDSYR
FFGNILDRHRQVGNAVPPPLAKAIGLEIKLCLLS
B:  DRISWLGQPMKIEENRTYYQKVSIDEEMLEVGDCVSVIPD
DSSKPLYLARVTALWEDKNGQMMFHAHWFCAGTDTVLGAT
SDPLELFLVGECENMQLSYIHSKVKVIYKAPSENWAMEGG
GKTYFFQLWYNQEYARFESPPKTQPTEDNKHKFCLSCIRL
AELRQKEMPKVLEQIEEVDGRVYCSSITKNGVVYRLGDSV
YLPPEAFTFNIKVASPVKRPKKDPVNETLYPEHYRKYSDY
IKGSNLDAPEPYRIGRIKEIHCGKKKGKVNEADIKLRLYK
FYRPENTHRSYNGSYHTDINMLYWSDEEAVVNFSDVQGRC
TVEYGEDLLESIQDYSQGGPDRFYFLEAYNSKTKNFEDPP
NHARSPGNIKLPKLRTLDVFSGCGGLSEGFHQAGISETLW
AIEMWDPAAQAFRLNNPGTTVFTEDCNVLLKLVMAGEVTN
SLGQRLPQKGDVEMLCGGPPCQGFSGMNRFNSRTYSKFKN
SLVVSFLSYCDYYRPRFFLLENVRNFVSYRRSMVLKLTLR
CLVRMGYQCTFGVLQAGQYGVAQTRRRAIILAAAPGEKLP
LFPEPLHVFAPRACQLSVVVDDKKFVSNITRLSSGPFRTI
TVRDTMSDLPEIQNGASNSEIPYNGEPLSWFQRQLRGSHY
QPILRDHICKDMSPLVAARMRHIPLFPGSDWRDLPNIQVR
LGDGVIAHKLQYTFHDVKNGYSSTGALRGVCSCAEGKACD
PESRQFSTLIPWCLPHTGNRHNHWAGLYGRLEWDGFFSTT
VTNPEPMGKQGRVLHPEQHRVVSVRECARSQGFPDSYRFF
GNILDRHRQVGNAVPPPLAKAIGLEIKLCLLS
C:  GAGGCXGCCTGC
D:  GCAGGXGGCCTC
E:  GAGGCXGCCTGC
F:  GCAGGXGGCCTC
Description


Functional site

1) chain A
residue 1148
type
sequence F
description BINDING SITE FOR RESIDUE SAH A 1701
source : AC1

2) chain A
residue 1149
type
sequence S
description BINDING SITE FOR RESIDUE SAH A 1701
source : AC1

3) chain A
residue 1150
type
sequence G
description BINDING SITE FOR RESIDUE SAH A 1701
source : AC1

4) chain A
residue 1152
type
sequence G
description BINDING SITE FOR RESIDUE SAH A 1701
source : AC1

5) chain A
residue 1153
type
sequence G
description BINDING SITE FOR RESIDUE SAH A 1701
source : AC1

6) chain A
residue 1154
type
sequence L
description BINDING SITE FOR RESIDUE SAH A 1701
source : AC1

7) chain A
residue 1171
type
sequence E
description BINDING SITE FOR RESIDUE SAH A 1701
source : AC1

8) chain A
residue 1172
type
sequence M
description BINDING SITE FOR RESIDUE SAH A 1701
source : AC1

9) chain A
residue 1173
type
sequence W
description BINDING SITE FOR RESIDUE SAH A 1701
source : AC1

10) chain A
residue 1193
type
sequence D
description BINDING SITE FOR RESIDUE SAH A 1701
source : AC1

11) chain A
residue 1194
type
sequence C
description BINDING SITE FOR RESIDUE SAH A 1701
source : AC1

12) chain A
residue 1226
type
sequence G
description BINDING SITE FOR RESIDUE SAH A 1701
source : AC1

13) chain A
residue 1247
type
sequence K
description BINDING SITE FOR RESIDUE SAH A 1701
source : AC1

14) chain A
residue 1250
type
sequence L
description BINDING SITE FOR RESIDUE SAH A 1701
source : AC1

15) chain A
residue 1581
type
sequence A
description BINDING SITE FOR RESIDUE SAH A 1701
source : AC1

16) chain A
residue 1582
type
sequence V
description BINDING SITE FOR RESIDUE SAH A 1701
source : AC1

17) chain D
residue 18
type
sequence X
description BINDING SITE FOR RESIDUE SAH A 1701
source : AC1

18) chain A
residue 1479
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 1702
source : AC2

19) chain A
residue 1481
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 1702
source : AC2

20) chain A
residue 1487
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 1702
source : AC2

21) chain A
residue 1504
type
sequence H
description BINDING SITE FOR RESIDUE ZN A 1702
source : AC2

22) chain A
residue 796
type
sequence H
description BINDING SITE FOR RESIDUE ZN A 1703
source : AC3

23) chain A
residue 823
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 1703
source : AC3

24) chain A
residue 897
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 1703
source : AC3

25) chain A
residue 900
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 1703
source : AC3

26) chain B
residue 1148
type
sequence F
description BINDING SITE FOR RESIDUE SAH B 1701
source : AC4

27) chain B
residue 1149
type
sequence S
description BINDING SITE FOR RESIDUE SAH B 1701
source : AC4

28) chain B
residue 1150
type
sequence G
description BINDING SITE FOR RESIDUE SAH B 1701
source : AC4

29) chain B
residue 1152
type
sequence G
description BINDING SITE FOR RESIDUE SAH B 1701
source : AC4

30) chain B
residue 1153
type
sequence G
description BINDING SITE FOR RESIDUE SAH B 1701
source : AC4

31) chain B
residue 1154
type
sequence L
description BINDING SITE FOR RESIDUE SAH B 1701
source : AC4

32) chain B
residue 1171
type
sequence E
description BINDING SITE FOR RESIDUE SAH B 1701
source : AC4

33) chain B
residue 1172
type
sequence M
description BINDING SITE FOR RESIDUE SAH B 1701
source : AC4

34) chain B
residue 1173
type
sequence W
description BINDING SITE FOR RESIDUE SAH B 1701
source : AC4

35) chain B
residue 1193
type
sequence D
description BINDING SITE FOR RESIDUE SAH B 1701
source : AC4

36) chain B
residue 1194
type
sequence C
description BINDING SITE FOR RESIDUE SAH B 1701
source : AC4

37) chain B
residue 1226
type
sequence G
description BINDING SITE FOR RESIDUE SAH B 1701
source : AC4

38) chain B
residue 1247
type
sequence K
description BINDING SITE FOR RESIDUE SAH B 1701
source : AC4

39) chain B
residue 1250
type
sequence L
description BINDING SITE FOR RESIDUE SAH B 1701
source : AC4

40) chain B
residue 1581
type
sequence A
description BINDING SITE FOR RESIDUE SAH B 1701
source : AC4

41) chain B
residue 1582
type
sequence V
description BINDING SITE FOR RESIDUE SAH B 1701
source : AC4

42) chain F
residue 18
type
sequence X
description BINDING SITE FOR RESIDUE SAH B 1701
source : AC4

43) chain B
residue 1479
type
sequence C
description BINDING SITE FOR RESIDUE ZN B 1702
source : AC5

44) chain B
residue 1481
type
sequence C
description BINDING SITE FOR RESIDUE ZN B 1702
source : AC5

45) chain B
residue 1487
type
sequence C
description BINDING SITE FOR RESIDUE ZN B 1702
source : AC5

46) chain B
residue 1504
type
sequence H
description BINDING SITE FOR RESIDUE ZN B 1702
source : AC5

47) chain B
residue 796
type
sequence H
description BINDING SITE FOR RESIDUE ZN B 1703
source : AC6

48) chain B
residue 823
type
sequence C
description BINDING SITE FOR RESIDUE ZN B 1703
source : AC6

49) chain B
residue 897
type
sequence C
description BINDING SITE FOR RESIDUE ZN B 1703
source : AC6

50) chain B
residue 900
type
sequence C
description BINDING SITE FOR RESIDUE ZN B 1703
source : AC6

51) chain A
residue 1566
type
sequence R
description BINDING SITE FOR RESIDUE CIT B 1704
source : AC7

52) chain A
residue 1568
type
sequence F
description BINDING SITE FOR RESIDUE CIT B 1704
source : AC7

53) chain A
residue 1569
type
sequence G
description BINDING SITE FOR RESIDUE CIT B 1704
source : AC7

54) chain A
residue 1574
type
sequence R
description BINDING SITE FOR RESIDUE CIT B 1704
source : AC7

55) chain B
residue 1566
type
sequence R
description BINDING SITE FOR RESIDUE CIT B 1704
source : AC7

56) chain B
residue 1567
type
sequence F
description BINDING SITE FOR RESIDUE CIT B 1704
source : AC7

57) chain B
residue 1568
type
sequence F
description BINDING SITE FOR RESIDUE CIT B 1704
source : AC7

58) chain B
residue 1569
type
sequence G
description BINDING SITE FOR RESIDUE CIT B 1704
source : AC7

59) chain B
residue 1574
type
sequence R
description BINDING SITE FOR RESIDUE CIT B 1704
source : AC7

60) chain A
residue 1149
type BINDING
sequence S
description BINDING => ECO:0000269|PubMed:21163962, ECO:0007744|PDB:3PT6, ECO:0007744|PDB:4DA4
source Swiss-Prot : SWS_FT_FI2

61) chain B
residue 1149
type BINDING
sequence S
description BINDING => ECO:0000269|PubMed:21163962, ECO:0007744|PDB:3PT6, ECO:0007744|PDB:4DA4
source Swiss-Prot : SWS_FT_FI2

62) chain A
residue 1229
type ACT_SITE
sequence C
description ACT_SITE => ECO:0000269|PubMed:17576694
source Swiss-Prot : SWS_FT_FI1

63) chain B
residue 1229
type ACT_SITE
sequence C
description ACT_SITE => ECO:0000269|PubMed:17576694
source Swiss-Prot : SWS_FT_FI1

64) chain A
residue 735
type MOD_RES
sequence S
description Phosphoserine => ECO:0000250|UniProtKB:P26358
source Swiss-Prot : SWS_FT_FI5

65) chain A
residue 882
type MOD_RES
sequence S
description Phosphoserine => ECO:0000250|UniProtKB:P26358
source Swiss-Prot : SWS_FT_FI5

66) chain B
residue 735
type MOD_RES
sequence S
description Phosphoserine => ECO:0000250|UniProtKB:P26358
source Swiss-Prot : SWS_FT_FI5

67) chain B
residue 882
type MOD_RES
sequence S
description Phosphoserine => ECO:0000250|UniProtKB:P26358
source Swiss-Prot : SWS_FT_FI5

68) chain A
residue 1221-1233
type prosite
sequence EMLCGGPPCQGFS
description C5_MTASE_1 C-5 cytosine-specific DNA methylases active site. EmLcgGpPCqGFS
source prosite : PS00094

69) chain A
residue 1576-1594
type prosite
sequence RQVGNAVPPPLAKAIGLEI
description C5_MTASE_2 C-5 cytosine-specific DNA methylases C-terminal signature. RqvGNAVpPpLakaIgleI
source prosite : PS00095

70) chain A
residue 1153
type BINDING
sequence G
description BINDING => ECO:0000269|PubMed:21163962, ECO:0007744|PDB:3PT6, ECO:0007744|PDB:3PT9, ECO:0007744|PDB:4DA4
source Swiss-Prot : SWS_FT_FI3

71) chain A
residue 1171
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:21163962, ECO:0007744|PDB:3PT6, ECO:0007744|PDB:3PT9, ECO:0007744|PDB:4DA4
source Swiss-Prot : SWS_FT_FI3

72) chain A
residue 1582
type BINDING
sequence V
description BINDING => ECO:0000269|PubMed:21163962, ECO:0007744|PDB:3PT6, ECO:0007744|PDB:3PT9, ECO:0007744|PDB:4DA4
source Swiss-Prot : SWS_FT_FI3

73) chain B
residue 1153
type BINDING
sequence G
description BINDING => ECO:0000269|PubMed:21163962, ECO:0007744|PDB:3PT6, ECO:0007744|PDB:3PT9, ECO:0007744|PDB:4DA4
source Swiss-Prot : SWS_FT_FI3

74) chain B
residue 1171
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:21163962, ECO:0007744|PDB:3PT6, ECO:0007744|PDB:3PT9, ECO:0007744|PDB:4DA4
source Swiss-Prot : SWS_FT_FI3

75) chain B
residue 1582
type BINDING
sequence V
description BINDING => ECO:0000269|PubMed:21163962, ECO:0007744|PDB:3PT6, ECO:0007744|PDB:3PT9, ECO:0007744|PDB:4DA4
source Swiss-Prot : SWS_FT_FI3

76) chain A
residue 1193
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:21163962, ECO:0007744|PDB:3PT6, ECO:0007744|PDB:3PT9
source Swiss-Prot : SWS_FT_FI4

77) chain B
residue 1193
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:21163962, ECO:0007744|PDB:3PT6, ECO:0007744|PDB:3PT9
source Swiss-Prot : SWS_FT_FI4

78) chain A
residue 752
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250|UniProtKB:P26358
source Swiss-Prot : SWS_FT_FI6

79) chain A
residue 1352
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250|UniProtKB:P26358
source Swiss-Prot : SWS_FT_FI6

80) chain A
residue 1418
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250|UniProtKB:P26358
source Swiss-Prot : SWS_FT_FI6

81) chain B
residue 752
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250|UniProtKB:P26358
source Swiss-Prot : SWS_FT_FI6

82) chain B
residue 895
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250|UniProtKB:P26358
source Swiss-Prot : SWS_FT_FI6

83) chain B
residue 961
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250|UniProtKB:P26358
source Swiss-Prot : SWS_FT_FI6

84) chain B
residue 965
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250|UniProtKB:P26358
source Swiss-Prot : SWS_FT_FI6

85) chain B
residue 979
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250|UniProtKB:P26358
source Swiss-Prot : SWS_FT_FI6

86) chain A
residue 895
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250|UniProtKB:P26358
source Swiss-Prot : SWS_FT_FI6

87) chain B
residue 1352
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250|UniProtKB:P26358
source Swiss-Prot : SWS_FT_FI6

88) chain B
residue 1418
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250|UniProtKB:P26358
source Swiss-Prot : SWS_FT_FI6

89) chain A
residue 961
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250|UniProtKB:P26358
source Swiss-Prot : SWS_FT_FI6

90) chain A
residue 965
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250|UniProtKB:P26358
source Swiss-Prot : SWS_FT_FI6

91) chain A
residue 979
type MOD_RES
sequence K
description N6-acetyllysine => ECO:0000250|UniProtKB:P26358
source Swiss-Prot : SWS_FT_FI6


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