Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

9LJ2

Structure of isw1-nucleosome double-bound complex in ADP-ADP+ state

Functional Information from GO Data

Chain	GOid	namespace	contents
K	0000166	molecular_function	nucleotide binding
K	0000182	molecular_function	rDNA binding
K	0000785	cellular_component	chromatin
K	0000976	molecular_function	transcription cis-regulatory region binding
K	0001178	biological_process	regulation of transcriptional start site selection at RNA polymerase II promoter
K	0003677	molecular_function	DNA binding
K	0003682	molecular_function	chromatin binding
K	0003730	molecular_function	mRNA 3'-UTR binding
K	0004386	molecular_function	helicase activity
K	0005515	molecular_function	protein binding
K	0005524	molecular_function	ATP binding
K	0005634	cellular_component	nucleus
K	0006325	biological_process	chromatin organization
K	0006338	biological_process	chromatin remodeling
K	0006354	biological_process	DNA-templated transcription elongation
K	0006355	biological_process	regulation of DNA-templated transcription
K	0006363	biological_process	termination of RNA polymerase I transcription
K	0006369	biological_process	termination of RNA polymerase II transcription
K	0007062	biological_process	sister chromatid cohesion
K	0009408	biological_process	response to heat
K	0016587	cellular_component	Isw1 complex
K	0016787	molecular_function	hydrolase activity
K	0016887	molecular_function	ATP hydrolysis activity
K	0030874	cellular_component	nucleolar chromatin
K	0031491	molecular_function	nucleosome binding
K	0031507	biological_process	heterochromatin formation
K	0036436	cellular_component	Isw1a complex
K	0036437	cellular_component	Isw1b complex
K	0045944	biological_process	positive regulation of transcription by RNA polymerase II
K	0046832	biological_process	negative regulation of RNA export from nucleus
K	0140750	molecular_function	nucleosome array spacer activity
K	1902275	biological_process	regulation of chromatin organization
K	1903895	biological_process	negative regulation of IRE1-mediated unfolded protein response
N	0000166	molecular_function	nucleotide binding
N	0000182	molecular_function	rDNA binding
N	0000785	cellular_component	chromatin
N	0000976	molecular_function	transcription cis-regulatory region binding
N	0001178	biological_process	regulation of transcriptional start site selection at RNA polymerase II promoter
N	0003677	molecular_function	DNA binding
N	0003682	molecular_function	chromatin binding
N	0003730	molecular_function	mRNA 3'-UTR binding
N	0004386	molecular_function	helicase activity
N	0005515	molecular_function	protein binding
N	0005524	molecular_function	ATP binding
N	0005634	cellular_component	nucleus
N	0006325	biological_process	chromatin organization
N	0006338	biological_process	chromatin remodeling
N	0006354	biological_process	DNA-templated transcription elongation
N	0006355	biological_process	regulation of DNA-templated transcription
N	0006363	biological_process	termination of RNA polymerase I transcription
N	0006369	biological_process	termination of RNA polymerase II transcription
N	0007062	biological_process	sister chromatid cohesion
N	0009408	biological_process	response to heat
N	0016587	cellular_component	Isw1 complex
N	0016787	molecular_function	hydrolase activity
N	0016887	molecular_function	ATP hydrolysis activity
N	0030874	cellular_component	nucleolar chromatin
N	0031491	molecular_function	nucleosome binding
N	0031507	biological_process	heterochromatin formation
N	0036436	cellular_component	Isw1a complex
N	0036437	cellular_component	Isw1b complex
N	0045944	biological_process	positive regulation of transcription by RNA polymerase II
N	0046832	biological_process	negative regulation of RNA export from nucleus
N	0140750	molecular_function	nucleosome array spacer activity
N	1902275	biological_process	regulation of chromatin organization
N	1903895	biological_process	negative regulation of IRE1-mediated unfolded protein response

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	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	2
Details	CARBOHYD: O-linked (GlcNAc) serine => ECO:0000250\|UniProtKB:P62807

Chain	Residue	Details
D	SER109
H	SER109

site_id	SWS_FT_FI2
Number of Residues	4
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250\|UniProtKB:P0C1H4

Chain	Residue	Details
D	LYS117
N	THR693
H	LYS117
F	LYS16
F	LYS44
F	LYS79

site_id	SWS_FT_FI3
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0007744\|PubMed:18407956

Chain	Residue	Details
K	SER846
N	SER845

site_id	SWS_FT_FI4
Number of Residues	4
Details	MOD_RES: N6-succinyllysine; alternate => ECO:0000250\|UniProtKB:P62805

Chain	Residue	Details
B	LYS31
B	LYS91
F	LYS31
F	LYS91

site_id	SWS_FT_FI5
Number of Residues	2
Details	MOD_RES: Phosphoserine; by PAK2 => ECO:0000250\|UniProtKB:P62805

Chain	Residue	Details
B	SER47
F	SER47

site_id	SWS_FT_FI6
Number of Residues	4
Details	MOD_RES: Phosphotyrosine => ECO:0000250\|UniProtKB:P62805

Chain	Residue	Details
B	TYR51
B	TYR88
F	TYR51
F	TYR88

site_id	SWS_FT_FI7
Number of Residues	2
Details	MOD_RES: N6-glutaryllysine; alternate => ECO:0000250\|UniProtKB:P62805

Chain	Residue	Details
B	LYS59
F	LYS59

site_id	SWS_FT_FI8
Number of Residues	2
Details	MOD_RES: N6-succinyllysine => ECO:0000250\|UniProtKB:P62805

Chain	Residue	Details
B	LYS77
F	LYS77

site_id	SWS_FT_FI9
Number of Residues	2
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in UFM1); alternate => ECO:0000250\|UniProtKB:P62805

Chain	Residue	Details
B	LYS31
F	LYS31

site_id	SWS_FT_FI10
Number of Residues	4
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000250\|UniProtKB:P62805

Chain	Residue	Details
B	LYS91
F	LYS91

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