Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

7XYG

Cryo-EM structure of Fft3-nucleosome complex with Fft3 bound to SHL+3 position of the nucleosome

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000785	cellular_component	chromatin
A	0000786	cellular_component	nucleosome
A	0003677	molecular_function	DNA binding
A	0005515	molecular_function	protein binding
A	0005634	cellular_component	nucleus
A	0005694	cellular_component	chromosome
A	0005700	cellular_component	polytene chromosome
A	0006334	biological_process	nucleosome assembly
A	0030527	molecular_function	structural constituent of chromatin
A	0031492	molecular_function	nucleosomal DNA binding
A	0032991	cellular_component	protein-containing complex
A	0035059	cellular_component	RCAF complex
A	0046982	molecular_function	protein heterodimerization activity
B	0000228	cellular_component	nuclear chromosome
B	0000786	cellular_component	nucleosome
B	0003677	molecular_function	DNA binding
B	0005515	molecular_function	protein binding
B	0005634	cellular_component	nucleus
B	0005694	cellular_component	chromosome
B	0006334	biological_process	nucleosome assembly
B	0030527	molecular_function	structural constituent of chromatin
B	0035059	cellular_component	RCAF complex
B	0046982	molecular_function	protein heterodimerization activity
C	0000786	cellular_component	nucleosome
C	0003677	molecular_function	DNA binding
C	0005515	molecular_function	protein binding
C	0005634	cellular_component	nucleus
C	0005694	cellular_component	chromosome
C	0005700	cellular_component	polytene chromosome
C	0005704	cellular_component	polytene chromosome band
C	0006325	biological_process	chromatin organization
C	0006334	biological_process	nucleosome assembly
C	0007526	biological_process	larval somatic muscle development
C	0030527	molecular_function	structural constituent of chromatin
C	0031507	biological_process	heterochromatin formation
C	0046982	molecular_function	protein heterodimerization activity
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	0030527	molecular_function	structural constituent of chromatin
D	0044877	molecular_function	protein-containing complex binding
D	0046982	molecular_function	protein heterodimerization activity
E	0000785	cellular_component	chromatin
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	0005700	cellular_component	polytene chromosome
E	0006334	biological_process	nucleosome assembly
E	0030527	molecular_function	structural constituent of chromatin
E	0031492	molecular_function	nucleosomal DNA binding
E	0032991	cellular_component	protein-containing complex
E	0035059	cellular_component	RCAF complex
E	0046982	molecular_function	protein heterodimerization activity
F	0000228	cellular_component	nuclear chromosome
F	0000786	cellular_component	nucleosome
F	0003677	molecular_function	DNA binding
F	0005515	molecular_function	protein binding
F	0005634	cellular_component	nucleus
F	0005694	cellular_component	chromosome
F	0006334	biological_process	nucleosome assembly
F	0030527	molecular_function	structural constituent of chromatin
F	0035059	cellular_component	RCAF complex
F	0046982	molecular_function	protein heterodimerization activity
G	0000786	cellular_component	nucleosome
G	0003677	molecular_function	DNA binding
G	0005515	molecular_function	protein binding
G	0005634	cellular_component	nucleus
G	0005694	cellular_component	chromosome
G	0005700	cellular_component	polytene chromosome
G	0005704	cellular_component	polytene chromosome band
G	0006325	biological_process	chromatin organization
G	0006334	biological_process	nucleosome assembly
G	0007526	biological_process	larval somatic muscle development
G	0030527	molecular_function	structural constituent of chromatin
G	0031507	biological_process	heterochromatin formation
G	0046982	molecular_function	protein heterodimerization activity
H	0000786	cellular_component	nucleosome
H	0003677	molecular_function	DNA binding
H	0005515	molecular_function	protein binding
H	0005634	cellular_component	nucleus
H	0005694	cellular_component	chromosome
H	0006325	biological_process	chromatin organization
H	0030527	molecular_function	structural constituent of chromatin
H	0044877	molecular_function	protein-containing complex binding
H	0046982	molecular_function	protein heterodimerization activity
K	0000729	biological_process	DNA double-strand break processing
K	0000785	cellular_component	chromatin
K	0000792	cellular_component	heterochromatin
K	0003677	molecular_function	DNA binding
K	0003682	molecular_function	chromatin binding
K	0003684	molecular_function	damaged DNA binding
K	0005515	molecular_function	protein binding
K	0005524	molecular_function	ATP binding
K	0005634	cellular_component	nucleus
K	0005694	cellular_component	chromosome
K	0006338	biological_process	chromatin remodeling
K	0006355	biological_process	regulation of DNA-templated transcription
K	0006357	biological_process	regulation of transcription by RNA polymerase II
K	0010526	biological_process	transposable element silencing
K	0016887	molecular_function	ATP hydrolysis activity
K	0031297	biological_process	replication fork processing
K	0031507	biological_process	heterochromatin formation
K	0045944	biological_process	positive regulation of transcription by RNA polymerase II
K	0140665	molecular_function	ATP-dependent H3-H4 histone complex chaperone activity
K	0140673	biological_process	transcription elongation-coupled chromatin remodeling
K	0140698	biological_process	attachment of telomeric heterochromatin to nuclear envelope
K	0140713	molecular_function	histone chaperone activity
K	0140750	molecular_function	nucleosome array spacer activity
K	0140861	biological_process	DNA repair-dependent chromatin remodeling

Functional Information from PROSITE/UniProt

site_id	PS00046
Number of Residues	7
Details	HISTONE_H2A Histone H2A signature. AGLqFPV

Chain	Residue	Details
C	ALA21-VAL27

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

Chain	Residue	Details
B	GLY14-HIS18

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

Chain	Residue	Details
A	LYS14-LEU20

site_id	PS00357
Number of Residues	23
Details	HISTONE_H2B Histone H2B signature. REIQTavRlLLpGELaKHAVSEG

Chain	Residue	Details
D	ARG89-GLY111

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

Chain	Residue	Details
A	PRO66-ILE74

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	18
Details	Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"PubMed","id":"22389435","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	2
Details	Modified residue: {"description":"N5-methylglutamine","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	2
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"15386022","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	2
Details	Glycosylation: {"description":"O-linked (GlcNAc) serine","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	4
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"21764853","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18188155","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	3
Details	Motif: {"description":"DEGH box"}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	7
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00541","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18257517","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	2
Details	Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"PubMed","id":"22389435","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	4
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"18327897","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)