eF-site ID 2lbm_10-AC
PDB Code 2lbm
Model 10
Chain A, C

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Title Solution structure of the ADD domain of ATRX complexed with histone tail H3 1-15 K9me3
Classification METAL BINDING PROTEIN/STRUCTURAL PROTEIN
Compound Transcriptional regulator ATRX
Source Homo sapiens (Human) (2LBM)
Sequence A:  GAMADKRGDGLHGIVSCTACGQQVNHFQKDSIYRHPSLQV
LICKNCFKYYMSDDISRDSDGMDEQCRWCAEGGNLICCDF
CHNAFCKKCILRNLGRKELSTIMDENNQWYCYICHPEPLL
DLVTACNSVFENLEQLLQQNKK
C:  ARTKQTARXSTGGKA
Description (1)  Transcriptional regulator ATRX (E.C.3.6.4.12), histone tail H3 K9me3


Functional site

1) chain A
residue 171
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 1
source : AC1

2) chain A
residue 174
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 1
source : AC1

3) chain A
residue 197
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 1
source : AC1

4) chain A
residue 200
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 1
source : AC1

5) chain A
residue 220
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 2
source : AC2

6) chain A
residue 223
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 2
source : AC2

7) chain A
residue 240
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 2
source : AC2

8) chain A
residue 243
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 2
source : AC2

9) chain A
residue 232
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 3
source : AC3

10) chain A
residue 235
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 3
source : AC3

11) chain A
residue 265
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 3
source : AC3

12) chain A
residue 268
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 3
source : AC3

13) chain C
residue 2
type MOD_RES
sequence R
description Citrulline; alternate => ECO:0000269|PubMed:16567635
source Swiss-Prot : SWS_FT_FI1

14) chain C
residue 3
type MOD_RES
sequence T
description Phosphothreonine; by HASPIN => ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:16185088
source Swiss-Prot : SWS_FT_FI2

15) chain C
residue 14
type MOD_RES
sequence K
description N6-succinyllysine; alternate => ECO:0000269|PubMed:22389435
source Swiss-Prot : SWS_FT_FI10

16) chain C
residue 4
type MOD_RES
sequence K
description N6-methyllysine; alternate => ECO:0000269|PubMed:16267050, ECO:0000269|PubMed:16457588, ECO:0000269|PubMed:17194708
source Swiss-Prot : SWS_FT_FI3

17) chain C
residue 11
type MOD_RES
sequence T
description Phosphothreonine; by PKC and CHEK1 => ECO:0000269|PubMed:12560483, ECO:0000269|PubMed:18066052, ECO:0000269|PubMed:18243098, ECO:0000269|PubMed:22901803
source Swiss-Prot : SWS_FT_FI9

18) chain C
residue 5
type MOD_RES
sequence Q
description 5-glutamyl serotonin; alternate => ECO:0000269|PubMed:30867594
source Swiss-Prot : SWS_FT_FI4

19) chain C
residue 6
type MOD_RES
sequence T
description Phosphothreonine; by PKC => ECO:0000269|PubMed:20228790
source Swiss-Prot : SWS_FT_FI5

20) chain C
residue 8
type MOD_RES
sequence R
description Symmetric dimethylarginine; by PRMT5; alternate => ECO:0000250|UniProtKB:P68433
source Swiss-Prot : SWS_FT_FI6

21) chain C
residue 9
type MOD_RES
sequence X
description N6-methyllysine; alternate => ECO:0000269|PubMed:11242053, ECO:0000269|PubMed:16185088, ECO:0000269|PubMed:16267050, ECO:0000269|PubMed:16457588, ECO:0000269|PubMed:17194708
source Swiss-Prot : SWS_FT_FI7

22) chain C
residue 10
type MOD_RES
sequence S
description Phosphoserine; alternate; by AURKB, AURKC, RPS6KA3, RPS6KA4 and RPS6KA5 => ECO:0000269|PubMed:10464286, ECO:0000269|PubMed:11856369, ECO:0000269|PubMed:12560483, ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:16185088, ECO:0000269|PubMed:16457588
source Swiss-Prot : SWS_FT_FI8


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