eF-site ID 6oip-A
PDB Code 6oip
Chain A

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Title Crystal structure of MYST acetyltransferase domain in complex with inhibitor 34
Classification TRANSFERASE/TRANSFERASE INHIBITOR
Compound Histone acetyltransferase KAT8
Source (KAT8_HUMAN)
Sequence A:  KYVDKIHIGNYEIDAWYFSPFPEDYGKQPKLWLCEYCLKY
MKYEKSYRFHLGQCQWRQPPGKEIYRKSNISVHEVDGKDH
KIYCQNLCLLAKLFLDHXTLYFDVEPFVFYILTEVDRQGA
HIVGYFSKEKESPDGNNVSCIMILPPYQRRGYGRFLIAFS
YELSKLESTVGSPEKPLSDLGKLSYRSYWSWVLLENLRDF
RGTLSIKDLSQMTSITQNDIISTLQSLNMVKYWKGQHVIC
VTPKLVEEHLKSAQYKKPPITVDSVCLKWAPP
Description


Functional site

1) chain A
residue 210
type
sequence C
description binding site for residue ZN A 501
source : AC1

2) chain A
residue 213
type
sequence C
description binding site for residue ZN A 501
source : AC1

3) chain A
residue 226
type
sequence H
description binding site for residue ZN A 501
source : AC1

4) chain A
residue 230
type
sequence C
description binding site for residue ZN A 501
source : AC1

5) chain A
residue 243
type
sequence K
description binding site for residue GOL A 502
source : AC2

6) chain A
residue 246
type
sequence I
description binding site for residue GOL A 502
source : AC2

7) chain A
residue 401
type
sequence Q
description binding site for residue GOL A 502
source : AC2

8) chain A
residue 406
type
sequence V
description binding site for residue GOL A 502
source : AC2

9) chain A
residue 413
type
sequence H
description binding site for residue GOL A 502
source : AC2

10) chain A
residue 360
type
sequence S
description binding site for residue GOL A 503
source : AC3

11) chain A
residue 363
type
sequence S
description binding site for residue GOL A 503
source : AC3

12) chain A
residue 324
type
sequence Q
description binding site for residue MLS A 504
source : AC4

13) chain A
residue 325
type
sequence R
description binding site for residue MLS A 504
source : AC4

14) chain A
residue 326
type
sequence R
description binding site for residue MLS A 504
source : AC4

15) chain A
residue 327
type
sequence G
description binding site for residue MLS A 504
source : AC4

16) chain A
residue 328
type
sequence Y
description binding site for residue MLS A 504
source : AC4

17) chain A
residue 329
type
sequence G
description binding site for residue MLS A 504
source : AC4

18) chain A
residue 330
type
sequence R
description binding site for residue MLS A 504
source : AC4

19) chain A
residue 356
type
sequence L
description binding site for residue MLS A 504
source : AC4

20) chain A
residue 360
type
sequence S
description binding site for residue MLS A 504
source : AC4

21) chain A
residue 363
type
sequence S
description binding site for residue MLS A 504
source : AC4

22) chain A
residue 364
type
sequence Y
description binding site for residue MLS A 504
source : AC4

23) chain A
residue 430
type
sequence Q
description binding site for residue MLS A 504
source : AC4

24) chain A
residue 317
type BINDING
sequence I
description BINDING => ECO:0000269|PubMed:21217699, ECO:0000269|Ref.23
source Swiss-Prot : SWS_FT_FI3

25) chain A
residue 324
type BINDING
sequence Q
description BINDING => ECO:0000269|PubMed:21217699, ECO:0000269|Ref.23
source Swiss-Prot : SWS_FT_FI3

26) chain A
residue 354
type BINDING
sequence S
description BINDING => ECO:0000269|PubMed:21217699, ECO:0000269|Ref.23
source Swiss-Prot : SWS_FT_FI3

27) chain A
residue 363
type BINDING
sequence S
description BINDING => ECO:0000269|PubMed:21217699, ECO:0000269|Ref.23
source Swiss-Prot : SWS_FT_FI3

28) chain A
residue 432
type BINDING
sequence K
description BINDING => ECO:0000269|PubMed:21217699, ECO:0000269|Ref.23
source Swiss-Prot : SWS_FT_FI3

29) chain A
residue 207-232
type ZN_FING
sequence LWLCEYCLKYMKYEKSYRFHLGQCQW
description C2HC MYST-type => ECO:0000255|PROSITE-ProRule:PRU01063, ECO:0000269|PubMed:22020126
source Swiss-Prot : SWS_FT_FI1

30) chain A
residue 350
type ACT_SITE
sequence E
description Proton donor/acceptor => ECO:0000303|PubMed:21217699, ECO:0000303|PubMed:22020126, ECO:0000305
source Swiss-Prot : SWS_FT_FI2

31) chain A
residue 274
type MOD_RES
sequence X
description N6-acetyllysine; by autocatalysis => ECO:0000269|PubMed:21217699, ECO:0000269|PubMed:21691301, ECO:0000269|PubMed:22020126, ECO:0000269|PubMed:22547026, ECO:0000269|Ref.23
source Swiss-Prot : SWS_FT_FI4

32) chain A
residue 348
type MOD_RES
sequence S
description Phosphoserine => ECO:0007744|PubMed:23186163
source Swiss-Prot : SWS_FT_FI5


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