Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

7XAY

Crystal structure of Hat1-Hat2-Asf1-H3-H4

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004402	molecular_function	histone acetyltransferase activity
A	0005506	molecular_function	iron ion binding
A	0005634	cellular_component	nucleus
A	0006325	biological_process	chromatin organization
A	0009055	molecular_function	electron transfer activity
A	0016747	molecular_function	acyltransferase activity, transferring groups other than amino-acyl groups
A	0020037	molecular_function	heme binding
A	0022900	biological_process	electron transport chain
A	0031509	biological_process	subtelomeric heterochromatin formation
A	0042393	molecular_function	histone binding
A	0042597	cellular_component	periplasmic space
A	0046872	molecular_function	metal ion 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	0005634	cellular_component	nucleus
C	0006325	biological_process	chromatin organization
D	0000776	cellular_component	kinetochore
D	0000786	cellular_component	nucleosome
D	0003677	molecular_function	DNA binding
D	0005515	molecular_function	protein binding
D	0005634	cellular_component	nucleus
D	0005694	cellular_component	chromosome
D	0006325	biological_process	chromatin organization
D	0006355	biological_process	regulation of DNA-templated transcription
D	0006878	biological_process	intracellular copper ion homeostasis
D	0007080	biological_process	mitotic metaphase chromosome alignment
D	0008823	molecular_function	cupric reductase (NADH) activity
D	0009060	biological_process	aerobic respiration
D	0009303	biological_process	rRNA transcription
D	0030527	molecular_function	structural constituent of chromatin
D	0031492	molecular_function	nucleosomal DNA binding
D	0031507	biological_process	heterochromatin formation
D	0042790	biological_process	nucleolar large rRNA transcription by RNA polymerase I
D	0042802	molecular_function	identical protein binding
D	0043505	cellular_component	CENP-A containing nucleosome
D	0043935	biological_process	sexual sporulation resulting in formation of a cellular spore
D	0045943	biological_process	positive regulation of transcription by RNA polymerase I
D	0046982	molecular_function	protein heterodimerization activity
D	0051382	biological_process	kinetochore assembly
D	0070911	biological_process	global genome nucleotide-excision repair
E	0000786	cellular_component	nucleosome
E	0003677	molecular_function	DNA binding
E	0005515	molecular_function	protein binding
E	0005634	cellular_component	nucleus
E	0005694	cellular_component	chromosome
E	0006325	biological_process	chromatin organization
E	0006334	biological_process	nucleosome assembly
E	0006355	biological_process	regulation of DNA-templated transcription
E	0030527	molecular_function	structural constituent of chromatin
E	0042790	biological_process	nucleolar large rRNA transcription by RNA polymerase I
E	0042802	molecular_function	identical protein binding
E	0045943	biological_process	positive regulation of transcription by RNA polymerase I
E	0046982	molecular_function	protein heterodimerization activity

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
E	GLY14-HIS18

site_id	PS00322
Number of Residues	7
Details	HISTONE_H3_1 Histone H3 signature 1. KAPRKQL

Chain	Residue	Details
D	LYS14-LEU20

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

site_id	PS00959
Number of Residues	9
Details	HISTONE_H3_2 Histone H3 signature 2. PFqRLVREI

Chain	Residue	Details
D	PRO66-ILE74

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	168
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	4
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	8
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	1
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	9
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	1
Details	Binding site: {"evidences":[{"source":"PubMed","id":"9727486","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	1
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	31
Details	Repeat: {"description":"WD 1"}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	31
Details	Repeat: {"description":"WD 2"}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	31
Details	Repeat: {"description":"WD 3"}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	31
Details	Repeat: {"description":"WD 4"}

Chain

Residue

Details

site_id	SWS_FT_FI12
Number of Residues	31
Details	Repeat: {"description":"WD 5"}

Chain

Residue

Details

site_id	SWS_FT_FI13
Number of Residues	31
Details	Repeat: {"description":"WD 6"}

Chain

Residue

Details

site_id	SWS_FT_FI14
Number of Residues	4
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	1
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	1
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_FI17
Number of Residues	1
Details	Modified residue: {"description":"N6-methyllysine; alternate","evidences":[{"source":"PubMed","id":"17194708","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI18
Number of Residues	1
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

site_id	SWS_FT_FI19
Number of Residues	1
Details	Modified residue: {"description":"N6-butyryllysine; alternate","evidences":[{"source":"PubMed","id":"19113941","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27105113","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI20
Number of Residues	1
Details	Modified residue: {"description":"N6-propionyllysine; alternate","evidences":[{"source":"PubMed","id":"19113941","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI21
Number of Residues	1
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"17194708","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI22
Number of Residues	1
Details	Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"PubMed","id":"22389435","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI23
Number of Residues	4
Details	DNA binding: {}

Chain

Residue

Details

site_id	SWS_FT_FI24
Number of Residues	2
Details	Modified residue: {"description":"N6-methyllysine; alternate","evidences":[{"source":"PubMed","id":"22343720","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI25
Number of Residues	1
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_FI26
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_FI27
Number of Residues	1
Details	Modified residue: {"description":"Omega-N-methylarginine","evidences":[{"source":"PubMed","id":"19113941","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI28
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18407956","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19779198","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI29
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"17287358","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19779198","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI30
Number of Residues	1
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"16768447","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI31
Number of Residues	1
Details	Modified residue: {"description":"N6-glutaryllysine","evidences":[{"source":"PubMed","id":"31542297","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

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