eF-site ID 5znr-ABPQ
PDB Code 5znr
Chain A, B, P, Q

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Title Crystal structure of PtSHL in complex with an H3K27me3 peptide
Classification GENE REGULATION
Compound SHORT LIFE family protein
Source (H32_ARATH)
Sequence A:  PRRTLDSYTVKPINKTVKPGDCVLMRPSDPSKPSYVAKIE
RIESDGRGPNVRVRVRWYYRPEESIGGRRQFHGSKEVFLS
DHYDTQSADTIEGKCMVHSFKNYTKLDAVGNDDFFCRFEY
NSSTGAFNPDRVAVYCKCEMPYNPDDLMVQCEGCSDWFHP
ACIEMSAEEAKRLDHFFCENC
B:  RRTLDSYTVKPINKTVKPGDCVLMRPSDPSKPSYVAKIER
IESDGPNVRVRVRWYYRPEESIGGRRQFHGSKEVFLSDHY
DTQSADTIEGKCMVHSFKNYTKLDAVGNDDFFCRFEYNSS
TGAFNPDRVAVYCKCEMPYNPDDLMVQCEGCSDWFHPACI
EMSAEEAKRLDHFFCENC
P:  ATKAARXSAPATGGVK
Q:  ATKAARXSAPATGGVK
Description


Functional site

1) chain A
residue 142
type
sequence C
description binding site for residue ZN A 501
source : AC1

2) chain A
residue 144
type
sequence C
description binding site for residue ZN A 501
source : AC1

3) chain A
residue 165
type
sequence H
description binding site for residue ZN A 501
source : AC1

4) chain A
residue 168
type
sequence C
description binding site for residue ZN A 501
source : AC1

5) chain A
residue 157
type
sequence C
description binding site for residue ZN A 502
source : AC2

6) chain A
residue 159
type
sequence G
description binding site for residue ZN A 502
source : AC2

7) chain A
residue 160
type
sequence C
description binding site for residue ZN A 502
source : AC2

8) chain A
residue 184
type
sequence C
description binding site for residue ZN A 502
source : AC2

9) chain A
residue 187
type
sequence C
description binding site for residue ZN A 502
source : AC2

10) chain A
residue 60
type
sequence R
description binding site for residue SO4 A 503
source : AC3

11) chain P
residue 32
type
sequence T
description binding site for residue SO4 A 503
source : AC3

12) chain P
residue 34
type
sequence G
description binding site for residue SO4 A 503
source : AC3

13) chain A
residue 104
type
sequence H
description binding site for residue SO4 A 504
source : AC4

14) chain A
residue 105
type
sequence S
description binding site for residue SO4 A 504
source : AC4

15) chain A
residue 108
type
sequence N
description binding site for residue SO4 A 504
source : AC4

16) chain A
residue 148
type
sequence Y
description binding site for residue SO4 A 505
source : AC5

17) chain A
residue 154
type
sequence M
description binding site for residue SO4 A 505
source : AC5

18) chain A
residue 137
type
sequence R
description binding site for residue SO4 A 506
source : AC6

19) chain B
residue 142
type
sequence C
description binding site for residue ZN B 501
source : AC7

20) chain B
residue 144
type
sequence C
description binding site for residue ZN B 501
source : AC7

21) chain B
residue 165
type
sequence H
description binding site for residue ZN B 501
source : AC7

22) chain B
residue 168
type
sequence C
description binding site for residue ZN B 501
source : AC7

23) chain B
residue 157
type
sequence C
description binding site for residue ZN B 502
source : AC8

24) chain B
residue 159
type
sequence G
description binding site for residue ZN B 502
source : AC8

25) chain B
residue 160
type
sequence C
description binding site for residue ZN B 502
source : AC8

26) chain B
residue 184
type
sequence C
description binding site for residue ZN B 502
source : AC8

27) chain B
residue 60
type
sequence R
description binding site for residue SO4 B 503
source : AC9

28) chain B
residue 75
type
sequence R
description binding site for residue SO4 B 504
source : AD1

29) chain B
residue 76
type
sequence Q
description binding site for residue SO4 B 504
source : AD1

30) chain B
residue 104
type
sequence H
description binding site for residue SO4 B 505
source : AD2

31) chain B
residue 105
type
sequence S
description binding site for residue SO4 B 505
source : AD2

32) chain B
residue 108
type
sequence N
description binding site for residue SO4 B 505
source : AD2

33) chain B
residue 148
type
sequence Y
description binding site for residue SO4 B 506
source : AD3

34) chain B
residue 152
type
sequence D
description binding site for residue SO4 B 506
source : AD3

35) chain B
residue 153
type
sequence L
description binding site for residue SO4 B 506
source : AD3

36) chain B
residue 154
type
sequence M
description binding site for residue SO4 B 506
source : AD3

37) chain B
residue 148
type
sequence Y
description binding site for residue SO4 B 507
source : AD4

38) chain B
residue 163
type
sequence W
description binding site for residue SO4 B 507
source : AD4

39) chain P
residue 28
type MOD_RES
sequence S
description Phosphoserine => ECO:0000269|PubMed:14610360, ECO:0000269|PubMed:15753571
source Swiss-Prot : SWS_FT_FI5

40) chain Q
residue 28
type MOD_RES
sequence S
description Phosphoserine => ECO:0000269|PubMed:14610360, ECO:0000269|PubMed:15753571
source Swiss-Prot : SWS_FT_FI5

41) chain P
residue 36
type MOD_RES
sequence K
description N6-methyllysine; alternate => ECO:0000269|PubMed:15598823, ECO:0000269|PubMed:16299497
source Swiss-Prot : SWS_FT_FI6

42) chain Q
residue 36
type MOD_RES
sequence K
description N6-methyllysine; alternate => ECO:0000269|PubMed:15598823, ECO:0000269|PubMed:16299497
source Swiss-Prot : SWS_FT_FI6

43) chain A
residue 142-157
type prosite
sequence CKCEMPYNPDDLMVQC
description EGF_2 EGF-like domain signature 2. CkCemPYnpddlmvqC
source prosite : PS01186

44) chain A
residue 142-187
type prosite
sequence CKCEMPYNPDDLMVQCEGCSDWFHPACIEMSAEEAKRLDH
FFCENC
description ZF_PHD_1 Zinc finger PHD-type signature. Ck.Cempynpddlm...................................VqCeg..Csdw.FHpaCiemsaeeakrldh................................FfCenC
source prosite : PS01359

45) chain P
residue 27
type SITE
sequence X
description Not N6-acetylated => ECO:0000269|PubMed:15598823
source Swiss-Prot : SWS_FT_FI1

46) chain P
residue 36
type SITE
sequence K
description Not N6-acetylated => ECO:0000269|PubMed:15598823
source Swiss-Prot : SWS_FT_FI1

47) chain Q
residue 27
type SITE
sequence X
description Not N6-acetylated => ECO:0000269|PubMed:15598823
source Swiss-Prot : SWS_FT_FI1

48) chain Q
residue 36
type SITE
sequence K
description Not N6-acetylated => ECO:0000269|PubMed:15598823
source Swiss-Prot : SWS_FT_FI1

49) chain P
residue 31
type SITE
sequence A
description Required for interaction with TSK => ECO:0000269|PubMed:35298257
source Swiss-Prot : SWS_FT_FI2

50) chain Q
residue 31
type SITE
sequence A
description Required for interaction with TSK => ECO:0000269|PubMed:35298257
source Swiss-Prot : SWS_FT_FI2

51) chain P
residue 23
type MOD_RES
sequence K
description N6-methyllysine; alternate => ECO:0000269|PubMed:15598823
source Swiss-Prot : SWS_FT_FI3

52) chain Q
residue 23
type MOD_RES
sequence K
description N6-methyllysine; alternate => ECO:0000269|PubMed:15598823
source Swiss-Prot : SWS_FT_FI3

53) chain P
residue 27
type MOD_RES
sequence X
description N6-methyllysine; alternate => ECO:0000269|PubMed:14712277, ECO:0000269|PubMed:15598823, ECO:0000269|PubMed:17174094, ECO:0000269|PubMed:17439305, ECO:0000269|PubMed:19503079, ECO:0000269|PubMed:24626927, ECO:0000269|PubMed:35298257
source Swiss-Prot : SWS_FT_FI4

54) chain Q
residue 27
type MOD_RES
sequence X
description N6-methyllysine; alternate => ECO:0000269|PubMed:14712277, ECO:0000269|PubMed:15598823, ECO:0000269|PubMed:17174094, ECO:0000269|PubMed:17439305, ECO:0000269|PubMed:19503079, ECO:0000269|PubMed:24626927, ECO:0000269|PubMed:35298257
source Swiss-Prot : SWS_FT_FI4


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