eF-site ID 2ld1_18-A
PDB Code 2ld1
Model 18
Chain A

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Title Structures and chemical shift assignments for the ADD domain of the ATRX protein
Classification METAL BINDING PROTEIN
Compound Transcriptional regulator ATRX
Source Homo sapiens (Human) (ATRX_HUMAN)
Sequence A:  GAMADKRGDGLHGIVSCTACGQQVNHFQKDSIYRHPSLQV
LICKNCFKYYMSDDISRDSDGMDEQCRWCAEGGNLICCDF
CHNAFCKKCILRNLGRKELSTIMDENNQWYCYICHPEPLL
DLVTACNSVFENLEQLLQQNKK
Description (1)  Transcriptional regulator ATRX (E.C.3.6.4.12)


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 A
residue 171-207
type ZN_FING
sequence CTACGQQVNHFQKDSIYRHPSLQVLICKNCFKYYMSD
description GATA-type; atypical => ECO:0000255|PROSITE-ProRule:PRU00865
source Swiss-Prot : SWS_FT_FI1

14) chain A
residue 218-273
type ZN_FING
sequence EQCRWCAEGGNLICCDFCHNAFCKKCILRNLGRKELSTIM
DENNQWYCYICHPEPL
description PHD-type; atypical => ECO:0000255|PROSITE-ProRule:PRU00865
source Swiss-Prot : SWS_FT_FI2

15) chain A
residue 214
type MOD_RES
sequence D
description Phosphoserine => ECO:0000250|UniProtKB:Q61687
source Swiss-Prot : SWS_FT_FI3


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