eF-site ID 5j9q-ABCDEFGHIJKLMNO
PDB Code 5j9q
Chain A, B, C, D, E, F, G, H, I, J, K, L, M, N, O

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Title Crystal structure of the NuA4 core complex
Classification TRANSFERASE
Compound Histone acetyltransferase ESA1
Source Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (5J9Q)
Sequence A:  MTQNPHEVARVRNLNRIIMGKYEIEPWYFSPYPIELTDED
FIYIDDFTLQYFGSKKQYERYRKKCTLRHPPGNEIYRDDY
VSFFEIDGRKQRTWCRNLCLLSKLFLDHXTLYYDVDPFLF
YCMTRRDELGHHLVGYFSKEKESADGYNVACILTLPQYQR
MGYGKLLIEFSYELSKKENKVGSPQKPLSDLGLLSYRAYW
SDTLITLLVEHQKEITIDEISSMTSMTTTDILHTAKTLNI
LRYYKGQHIIFLNEDILDRYNRLKAKKRRTIDPNRLIWKP
PVFTASQLRFAW
B:  MTDELKSYEALKAELKKSLQDRREQEDTFDNLQQEIYDKE
TEYFSHYSGNIIKGFDTFSAFNNNDRIFSLSSATYVKQQ
C:  ISVKQHLKIYLPNDLKHLKDYIPTPDASMTWNEYDKFYTG
SFQETTSYIKFSATVEDCCGTNYNMDERDETFLNEQVNKG
SSDILTEDEFEILCSSFEHAIHERQPFLSMDPESILSFEE
LKPTLIKSDFNLRNQLNHEINSHKTHFITQFDPVSQMNTR
PLIQLIEKFGSKIYDYWRERKIEVNGYEIFPQLKFERPGE
KEEIDPYVCFRRREVRHPRKTRRIDILNSQRLRALHQELK
NAKDLALLVAKRENVSLNWINDELKIFDQRVKIKNLKRSL
NISGEDDDLINHK
D:  MDPSLVLEQTIQDVSNLPSEFRYLLEEIGSNDLKLIEEKK
KYEQKESQIHKFIRQQGSIPKHPQEDGLDKEIKESLLKCQ
SLQREKCVLANTALFLIARHLNKLEKNIALLEEDGVLAPV
E:  SMTQNPHEVARVRNLNRIIMGKYEIEPWYFSPYPIELTDE
DFIYIDDFTLQYFGSKKQYERYRKKCTLRHPPGNEIYRDD
YVSFFEIDGRKQRTWCRNLCLLSKLFLDHXTLYYDVDPFL
FYCMTRRDELGHHLVGYFSKEKESADGYNVACILTLPQYQ
RMGYGKLLIEFSYELSKKENKVGSPQKPLSDLGLLSYRAY
WSDTLITLLVEHQKEITIDEISSMTSMTTTDILHTAKTLN
ILRYYKGQHIIFLNEDILDRYNRLKAKKRRTIDPNRLIWK
PPVFTASQLRFAW
F:  MTDELKSYEALKAELKKSLQDRREQEDTFDNLQQEIYDKE
TEYFSYSGNIIKGFDTFSSAFNNNDRIFSLSSATY
G:  ISVKQHLKIYLPNDLKHDYIPTPDASMTWNEYDKFYTGSF
QETTSYIKFSATVEDCCGTNYNMDERDETFLNEQVNKGSS
DILTEDEFEILCSSFEHAIHERQPFLSMDPESILSFEELK
PTLIKSDFNLRNQLNHEINSHKTHFITQFDPVSQMNTRPL
IQLIEKFGSKIYDYWRERKIEVNGYEIFPQLKFERPGEKE
EIDPYVCFRRREVRHPRKTRRIDILNSQRLRALHQELKNA
KDLALLVAKRENVSLNWINDELKIFDQRVKIKNLKRSLNI
SGEDDDLINHKRKRP
H:  MDPSLVLEQTIQDVSNLPSEFRYLLEEIGSNDLKLIEEKK
KYEQKESQIHKFIRQQGSIPKHPQEDGLDKEIKESLLKCQ
SLQREKCVLANTALFLIARHLNKLEKNIALLEEDGVLAPV
I:  MTQNPHEVARVRNLNRIIMGKYEIEPWYFSPYPIELTDED
FIYIDDFTLQYFGSKKQYERYRKKCTLRHPPGNEIYRDDY
VSFFEIDGRKQRTWCRNLCLLSKLFLDHXTLYYDVDPFLF
YCMTRRDELGHHLVGYFSKEKESADGYNVACILTLPQYQR
MGYGKLLIEFSYELSKKENKVGSPQKPLSDLGLLSYRAYW
SDTLITLLVEHQKEITIDEISSMTSMTTTDILHTAKTLNI
LRYYKGQHIIFLNEDILDRYNRLKAKKRRTIDPNRLIWKP
PVFTASQLRFAW
J:  MTDELKSYEALKAELKKSLQDRREQEDTFDNLQQEIYDKE
TEYFSHYSGNIIKGFDTFSSAFNNNDRIFSLSSATY
K:  MDPSLVLEQTIQDVSNLPSEFRYLLEEIGSNDLKLIEEKK
KYEQKESQIHKFIRQQGSIPKHPQEDGLDKEIKESLLKCQ
SLQREKCVLANTALFLIARHLNKLEKNIALLEEDGVLAPV
L:  SGAKD
M:  GAKD
N:  KQHLKIYLPNDLKHKDYIPTPDASMTWNEYDKFYTGSFQE
TTSYIKFSATVEDCCGTNYNMDERDETFLNEQVNKGSSDI
LTEDEFEILCSSFEHAIHERQPFLSMDPESILSFEELKPT
LIKSDFNLRNQLNHEINSHKTHFITQFDPVSQMNTRPLIQ
LIEKFGSKIYDYWRERKIEVNGYEIFPQLKFERPGEKEEI
DPYVCFRRREVRHPRKTRRIDILNSQRLRALHQELKNAKD
LALLVAKRENVSLNWINDELKIFDQRVKIKNLKRSLNISG
EDDDLINHK
O:  GAK
Description (1)  Histone acetyltransferase ESA1 (E.C.2.3.1.48), Chromatin modification-related protein EAF6, Enhancer of polycomb-like protein 1, Chromatin modification-related protein YNG2, Htz1


Functional site

1) chain E
residue 198
type ACT_SITE
ligand
sequence D
description Proton donor/acceptor. {ECO:0000303|PubMed:12368900, ECO:0000303|PubMed:17223684, ECO:0000303|PubMed:18245364, ECO:0000303|PubMed:22020126, ECO:0000305}.
source Swiss-Prot : SWS_FT_FI1

2) chain E
residue 202
type BINDING
ligand
sequence L
description Acetyl-CoA. {ECO:0000269|PubMed:11106757, ECO:0000269|PubMed:12368900, ECO:0000269|PubMed:22020126}.
source Swiss-Prot : SWS_FT_FI2

3) chain E
residue 164
type SITE
ligand
sequence V
description Important for catalytic activity. {ECO:0000305}.
source Swiss-Prot : SWS_FT_FI3

4) chain A
residue 198
type ACT_SITE
ligand
sequence D
description Proton donor/acceptor. {ECO:0000303|PubMed:12368900, ECO:0000303|PubMed:17223684, ECO:0000303|PubMed:18245364, ECO:0000303|PubMed:22020126, ECO:0000305}.
source Swiss-Prot : SWS_FT_FI4

5) chain A
residue 202
type BINDING
ligand
sequence L
description Acetyl-CoA. {ECO:0000269|PubMed:11106757, ECO:0000269|PubMed:12368900, ECO:0000269|PubMed:22020126}.
source Swiss-Prot : SWS_FT_FI5

6) chain A
residue 164
type SITE
ligand
sequence V
description Important for catalytic activity. {ECO:0000305}.
source Swiss-Prot : SWS_FT_FI6

7) chain I
residue 198
type ACT_SITE
ligand
sequence D
description Proton donor/acceptor. {ECO:0000303|PubMed:12368900, ECO:0000303|PubMed:17223684, ECO:0000303|PubMed:18245364, ECO:0000303|PubMed:22020126, ECO:0000305}.
source Swiss-Prot : SWS_FT_FI7

8) chain I
residue 202
type BINDING
ligand
sequence L
description Acetyl-CoA. {ECO:0000269|PubMed:11106757, ECO:0000269|PubMed:12368900, ECO:0000269|PubMed:22020126}.
source Swiss-Prot : SWS_FT_FI8

9) chain I
residue 164
type SITE
ligand
sequence V
description Important for catalytic activity. {ECO:0000305}.
source Swiss-Prot : SWS_FT_FI9

10) chain E
residue 252
type binding
ligand ALY: N(6)-ACETYLLYSINE
sequence C
description N(6)-ACETYLLYSINE binding site
source pdb_hetatom : ALY_5j9q_E_262

11) chain E
residue 255-256
type binding
ligand ALY: N(6)-ACETYLLYSINE
sequence SK
description N(6)-ACETYLLYSINE binding site
source pdb_hetatom : ALY_5j9q_E_262

12) chain E
residue 259-261
type binding
ligand ALY: N(6)-ACETYLLYSINE
sequence LDH
description N(6)-ACETYLLYSINE binding site
source pdb_hetatom : ALY_5j9q_E_262

13) chain E
residue 263-264
type binding
ligand ALY: N(6)-ACETYLLYSINE
sequence TL
description N(6)-ACETYLLYSINE binding site
source pdb_hetatom : ALY_5j9q_E_262

14) chain E
residue 271
type binding
ligand ALY: N(6)-ACETYLLYSINE
sequence F
description N(6)-ACETYLLYSINE binding site
source pdb_hetatom : ALY_5j9q_E_262

15) chain E
residue 273
type binding
ligand ALY: N(6)-ACETYLLYSINE
sequence F
description N(6)-ACETYLLYSINE binding site
source pdb_hetatom : ALY_5j9q_E_262

16) chain E
residue 289
type binding
ligand ALY: N(6)-ACETYLLYSINE
sequence Y
description N(6)-ACETYLLYSINE binding site
source pdb_hetatom : ALY_5j9q_E_262

17) chain E
residue 291
type binding
ligand ALY: N(6)-ACETYLLYSINE
sequence S
description N(6)-ACETYLLYSINE binding site
source pdb_hetatom : ALY_5j9q_E_262

18) chain E
residue 304
type binding
ligand ALY: N(6)-ACETYLLYSINE
sequence C
description N(6)-ACETYLLYSINE binding site
source pdb_hetatom : ALY_5j9q_E_262

19) chain L
residue 3-5
type binding
ligand ALY: N(6)-ACETYLLYSINE
sequence AKD
description N(6)-ACETYLLYSINE binding site
source pdb_hetatom : ALY_5j9q_E_262

20) chain A
residue 252
type binding
ligand ALY: N(6)-ACETYLLYSINE
sequence C
description N(6)-ACETYLLYSINE binding site
source pdb_hetatom : ALY_5j9q_A_262

21) chain A
residue 255-256
type binding
ligand ALY: N(6)-ACETYLLYSINE
sequence SK
description N(6)-ACETYLLYSINE binding site
source pdb_hetatom : ALY_5j9q_A_262

22) chain A
residue 259-261
type binding
ligand ALY: N(6)-ACETYLLYSINE
sequence LDH
description N(6)-ACETYLLYSINE binding site
source pdb_hetatom : ALY_5j9q_A_262

23) chain A
residue 263-264
type binding
ligand ALY: N(6)-ACETYLLYSINE
sequence TL
description N(6)-ACETYLLYSINE binding site
source pdb_hetatom : ALY_5j9q_A_262

24) chain A
residue 271
type binding
ligand ALY: N(6)-ACETYLLYSINE
sequence F
description N(6)-ACETYLLYSINE binding site
source pdb_hetatom : ALY_5j9q_A_262

25) chain A
residue 273
type binding
ligand ALY: N(6)-ACETYLLYSINE
sequence F
description N(6)-ACETYLLYSINE binding site
source pdb_hetatom : ALY_5j9q_A_262

26) chain A
residue 289
type binding
ligand ALY: N(6)-ACETYLLYSINE
sequence Y
description N(6)-ACETYLLYSINE binding site
source pdb_hetatom : ALY_5j9q_A_262

27) chain A
residue 291
type binding
ligand ALY: N(6)-ACETYLLYSINE
sequence S
description N(6)-ACETYLLYSINE binding site
source pdb_hetatom : ALY_5j9q_A_262

28) chain A
residue 303-304
type binding
ligand ALY: N(6)-ACETYLLYSINE
sequence AC
description N(6)-ACETYLLYSINE binding site
source pdb_hetatom : ALY_5j9q_A_262

29) chain O
residue 3
type binding
ligand ALY: N(6)-ACETYLLYSINE
sequence A
description N(6)-ACETYLLYSINE binding site
source pdb_hetatom : ALY_5j9q_A_262

30) chain I
residue 252
type binding
ligand ALY: N(6)-ACETYLLYSINE
sequence C
description N(6)-ACETYLLYSINE binding site
source pdb_hetatom : ALY_5j9q_I_262

31) chain I
residue 255-256
type binding
ligand ALY: N(6)-ACETYLLYSINE
sequence SK
description N(6)-ACETYLLYSINE binding site
source pdb_hetatom : ALY_5j9q_I_262

32) chain I
residue 259-261
type binding
ligand ALY: N(6)-ACETYLLYSINE
sequence LDH
description N(6)-ACETYLLYSINE binding site
source pdb_hetatom : ALY_5j9q_I_262

33) chain I
residue 263-264
type binding
ligand ALY: N(6)-ACETYLLYSINE
sequence TL
description N(6)-ACETYLLYSINE binding site
source pdb_hetatom : ALY_5j9q_I_262

34) chain I
residue 271
type binding
ligand ALY: N(6)-ACETYLLYSINE
sequence F
description N(6)-ACETYLLYSINE binding site
source pdb_hetatom : ALY_5j9q_I_262

35) chain I
residue 273
type binding
ligand ALY: N(6)-ACETYLLYSINE
sequence F
description N(6)-ACETYLLYSINE binding site
source pdb_hetatom : ALY_5j9q_I_262

36) chain I
residue 289
type binding
ligand ALY: N(6)-ACETYLLYSINE
sequence Y
description N(6)-ACETYLLYSINE binding site
source pdb_hetatom : ALY_5j9q_I_262

37) chain I
residue 291
type binding
ligand ALY: N(6)-ACETYLLYSINE
sequence S
description N(6)-ACETYLLYSINE binding site
source pdb_hetatom : ALY_5j9q_I_262

38) chain I
residue 303-304
type binding
ligand ALY: N(6)-ACETYLLYSINE
sequence AC
description N(6)-ACETYLLYSINE binding site
source pdb_hetatom : ALY_5j9q_I_262

39) chain M
residue 3
type binding
ligand ALY: N(6)-ACETYLLYSINE
sequence A
description N(6)-ACETYLLYSINE binding site
source pdb_hetatom : ALY_5j9q_I_262


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