eF-site ID 2ou2-A
PDB Code 2ou2
Chain A

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Title Acetyltransferase domain of Human HIV-1 Tat interacting protein, 60kDa, isoform 3
Classification TRANSFERASE
Compound Histone acetyltransferase HTATIP
Source Homo sapiens (Human) (TIP60_HUMAN)
Sequence A:  KNIECIELGRHRLKPWYFSPYPQELTTLPVLYLCEFCLKY
GRSLKCLQRHLTKCDLRHPPGNEIYRKGTISFFEIDGRKN
KSYSQNLCLLAKCFLDHXTLYYDTDPFLFYVMTEYDCKGF
HIVGYFSKEKESTEDYNVACILTLPPYQRRGYGKLLIEFS
YELSKVEGKTGTPEKPLSDLGLLSYRSYWSQTILEILQIT
INEISEITSIKKEDVISTLQYLNLINYYKGQYILLRIDSK
CLHFTP
Description


Functional site

1) chain A
residue 211
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 490
source : AC1

2) chain A
residue 214
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 490
source : AC1

3) chain A
residue 227
type
sequence H
description BINDING SITE FOR RESIDUE ZN A 490
source : AC1

4) chain A
residue 231
type
sequence C
description BINDING SITE FOR RESIDUE ZN A 490
source : AC1

5) chain A
residue 187
type
sequence R
description BINDING SITE FOR RESIDUE ACO A 500
source : AC2

6) chain A
residue 188
type
sequence H
description BINDING SITE FOR RESIDUE ACO A 500
source : AC2

7) chain A
residue 189
type
sequence R
description BINDING SITE FOR RESIDUE ACO A 500
source : AC2

8) chain A
residue 193
type
sequence W
description BINDING SITE FOR RESIDUE ACO A 500
source : AC2

9) chain A
residue 271
type
sequence F
description BINDING SITE FOR RESIDUE ACO A 500
source : AC2

10) chain A
residue 272
type
sequence L
description BINDING SITE FOR RESIDUE ACO A 500
source : AC2

11) chain A
residue 316
type
sequence A
description BINDING SITE FOR RESIDUE ACO A 500
source : AC2

12) chain A
residue 317
type
sequence C
description BINDING SITE FOR RESIDUE ACO A 500
source : AC2

13) chain A
residue 318
type
sequence I
description BINDING SITE FOR RESIDUE ACO A 500
source : AC2

14) chain A
residue 319
type
sequence L
description BINDING SITE FOR RESIDUE ACO A 500
source : AC2

15) chain A
residue 320
type
sequence T
description BINDING SITE FOR RESIDUE ACO A 500
source : AC2

16) chain A
residue 325
type
sequence Q
description BINDING SITE FOR RESIDUE ACO A 500
source : AC2

17) chain A
residue 326
type
sequence R
description BINDING SITE FOR RESIDUE ACO A 500
source : AC2

18) chain A
residue 327
type
sequence R
description BINDING SITE FOR RESIDUE ACO A 500
source : AC2

19) chain A
residue 328
type
sequence G
description BINDING SITE FOR RESIDUE ACO A 500
source : AC2

20) chain A
residue 330
type
sequence G
description BINDING SITE FOR RESIDUE ACO A 500
source : AC2

21) chain A
residue 331
type
sequence K
description BINDING SITE FOR RESIDUE ACO A 500
source : AC2

22) chain A
residue 351
type
sequence E
description BINDING SITE FOR RESIDUE ACO A 500
source : AC2

23) chain A
residue 355
type
sequence S
description BINDING SITE FOR RESIDUE ACO A 500
source : AC2

24) chain A
residue 357
type
sequence L
description BINDING SITE FOR RESIDUE ACO A 500
source : AC2

25) chain A
residue 361
type
sequence S
description BINDING SITE FOR RESIDUE ACO A 500
source : AC2

26) chain A
residue 364
type
sequence S
description BINDING SITE FOR RESIDUE ACO A 500
source : AC2

27) chain A
residue 368
type
sequence Q
description BINDING SITE FOR RESIDUE ACO A 500
source : AC2

28) chain A
residue 351
type ACT_SITE
sequence E
description Proton donor/acceptor => ECO:0000250|UniProtKB:Q9H7Z6
source Swiss-Prot : SWS_FT_FI2

29) chain A
residue 399
type CROSSLNK
sequence K
description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1) => ECO:0000269|PubMed:17704809
source Swiss-Prot : SWS_FT_FI7

30) chain A
residue 364
type BINDING
sequence S
description BINDING => ECO:0000250|UniProtKB:Q9H7Z6
source Swiss-Prot : SWS_FT_FI4

31) chain A
residue 208-233
type ZN_FING
sequence LYLCEFCLKYGRSLKCLQRHLTKCDL
description C2HC MYST-type => ECO:0000255|PROSITE-ProRule:PRU01063, ECO:0000305|Ref.69
source Swiss-Prot : SWS_FT_FI1

32) chain A
residue 318
type BINDING
sequence I
description BINDING => ECO:0000269|Ref.69
source Swiss-Prot : SWS_FT_FI3

33) chain A
residue 325
type BINDING
sequence Q
description BINDING => ECO:0000269|Ref.69
source Swiss-Prot : SWS_FT_FI3

34) chain A
residue 355
type BINDING
sequence S
description BINDING => ECO:0000269|Ref.69
source Swiss-Prot : SWS_FT_FI3

35) chain A
residue 275
type MOD_RES
sequence X
description N6-acetyllysine; by autocatalysis => ECO:0000269|PubMed:24835996, ECO:0000269|Ref.69
source Swiss-Prot : SWS_FT_FI5


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