Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4PSX

Crystal structure of histone acetyltransferase complex

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004402	molecular_function	histone acetyltransferase activity
A	0005634	cellular_component	nucleus
A	0006325	biological_process	chromatin organization
A	0016747	molecular_function	acyltransferase activity, transferring groups other than amino-acyl groups
A	0031509	biological_process	subtelomeric heterochromatin formation
A	0042393	molecular_function	histone binding
B	0000123	cellular_component	histone acetyltransferase complex
B	0000781	cellular_component	chromosome, telomeric region
B	0004402	molecular_function	histone acetyltransferase activity
B	0005515	molecular_function	protein binding
B	0005634	cellular_component	nucleus
B	0005737	cellular_component	cytoplasm
B	0006325	biological_process	chromatin organization
B	0006338	biological_process	chromatin remodeling
B	0006355	biological_process	regulation of DNA-templated transcription
B	0031509	biological_process	subtelomeric heterochromatin formation
B	0033698	cellular_component	Rpd3L complex
B	0042393	molecular_function	histone binding
B	0070210	cellular_component	Rpd3L-Expanded complex
C	0000786	cellular_component	nucleosome
C	0003677	molecular_function	DNA binding
C	0030527	molecular_function	structural constituent of chromatin
C	0046982	molecular_function	protein heterodimerization activity
D	0004402	molecular_function	histone acetyltransferase activity
D	0005634	cellular_component	nucleus
D	0006325	biological_process	chromatin organization
D	0016747	molecular_function	acyltransferase activity, transferring groups other than amino-acyl groups
D	0031509	biological_process	subtelomeric heterochromatin formation
D	0042393	molecular_function	histone binding
E	0000123	cellular_component	histone acetyltransferase complex
E	0000781	cellular_component	chromosome, telomeric region
E	0004402	molecular_function	histone acetyltransferase activity
E	0005515	molecular_function	protein binding
E	0005634	cellular_component	nucleus
E	0005737	cellular_component	cytoplasm
E	0006325	biological_process	chromatin organization
E	0006338	biological_process	chromatin remodeling
E	0006355	biological_process	regulation of DNA-templated transcription
E	0031509	biological_process	subtelomeric heterochromatin formation
E	0033698	cellular_component	Rpd3L complex
E	0042393	molecular_function	histone binding
E	0070210	cellular_component	Rpd3L-Expanded complex
F	0000786	cellular_component	nucleosome
F	0003677	molecular_function	DNA binding
F	0030527	molecular_function	structural constituent of chromatin
F	0046982	molecular_function	protein heterodimerization activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	16
Details	BINDING SITE FOR RESIDUE COA A 401

Chain	Residue
A	PHE160
A	SER233
A	ASN258
A	HOH565
A	HOH594
A	HOH596
C	LYS12
C	HOH118
A	ILE161
A	PHE220
A	ILE222
A	GLN227
A	ASN228
A	LYS229
A	GLY230
A	GLY232

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SO4 B 501

Chain	Residue
B	GLN41
B	ARG123
B	ARG125
B	SER167
B	PHE168
B	HOH610

site_id	AC3
Number of Residues	19
Details	BINDING SITE FOR RESIDUE COA D 401

Chain	Residue
D	ILE161
D	PHE220
D	LEU221
D	ILE222
D	TYR226
D	GLN227
D	ASN228
D	GLY230
D	GLY232
D	SER233
D	ASN258
D	LEU264
D	ARG267
D	HOH530
D	HOH540
D	HOH595
D	HOH598
F	LYS12
F	HOH113

Functional Information from PROSITE/UniProt

site_id	PS00047
Number of Residues	5
Details	HISTONE_H4 Histone H4 signature. GAKRH

Chain	Residue	Details
C	GLY14-HIS18

site_id	PS00678
Number of Residues	15
Details	WD_REPEATS_1 Trp-Asp (WD) repeats signature. LLSGsdDhTVALWEV

Chain	Residue	Details
B	LEU176-VAL190
B	VAL311-LEU325

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	336
Details	Domain: {"description":"N-acetyltransferase","evidences":[{"source":"PROSITE-ProRule","id":"PRU00532","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	8
Details	Region: {"description":"Interaction with histone H4 N-terminus","evidences":[{"source":"PubMed","id":"24835250","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	16
Details	Region: {"description":"Interaction with HAT2","evidences":[{"source":"PubMed","id":"24835250","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8858151","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	2
Details	Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"PubMed","id":"24835250","evidenceCode":"ECO:0000303"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	18
Details	Binding site: {"evidences":[{"source":"PubMed","id":"24835250","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9727486","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"9727486","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	2
Details	Site: {"description":"Interaction with histone H4 N-terminus","evidences":[{"source":"PubMed","id":"24835250","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	62
Details	Repeat: {"description":"WD 1"}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	62
Details	Repeat: {"description":"WD 2"}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	62
Details	Repeat: {"description":"WD 3"}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	62
Details	Repeat: {"description":"WD 4"}

Chain

Residue

Details

site_id	SWS_FT_FI12
Number of Residues	62
Details	Repeat: {"description":"WD 5"}

Chain

Residue

Details

site_id	SWS_FT_FI13
Number of Residues	62
Details	Repeat: {"description":"WD 6"}

Chain

Residue

Details

site_id	SWS_FT_FI14
Number of Residues	8
Details	Region: {"description":"Interaction with the histone H4 N-terminus","evidences":[{"source":"PubMed","id":"24835250","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI15
Number of Residues	2
Details	Site: {"description":"Important for interaction with HAT1","evidences":[{"source":"PubMed","id":"24835250","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI16
Number of Residues	8
Details	DNA binding: {}

Chain

Residue

Details

site_id	SWS_FT_FI17
Number of Residues	4
Details	Modified residue: {"description":"N6-methyllysine; alternate","evidences":[{"source":"PubMed","id":"22343720","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI18
Number of Residues	2
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"11080160","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15150415","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17289592","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19113941","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI19
Number of Residues	2
Details	Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"PubMed","id":"22389435","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI20
Number of Residues	2
Details	Modified residue: {"description":"N6-methyllysine; alternate","evidences":[{"source":"PubMed","id":"11742990","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11751634","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11752412","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12152067","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12353038","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12845608","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15949446","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16122352","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16168379","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16185711","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17194708","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI21
Number of Residues	2
Details	Modified residue: {"description":"N6-methyllysine; alternate","evidences":[{"source":"PubMed","id":"17194708","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI22
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"10911986","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"10975519","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15719021","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	2
Details	M-CSA 224

Chain	Residue	Details
A	PHE220	electrostatic stabiliser, hydrogen bond donor
A	GLU255	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor

site_id	MCSA2
Number of Residues	2
Details	M-CSA 224

Chain	Residue	Details
D	PHE220	electrostatic stabiliser, hydrogen bond donor
D	GLU255	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)