Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6VZ4

Cryo-EM structure of Sth1-Arp7-Arp9-Rtt102 bound to the nucleosome in ADP Beryllium Fluoride state

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000786	cellular_component	nucleosome
A	0003677	molecular_function	DNA binding
A	0005634	cellular_component	nucleus
A	0030527	molecular_function	structural constituent of chromatin
A	0046982	molecular_function	protein heterodimerization activity
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	0030527	molecular_function	structural constituent of chromatin
B	0046982	molecular_function	protein heterodimerization activity
C	0000786	cellular_component	nucleosome
C	0003677	molecular_function	DNA binding
C	0005634	cellular_component	nucleus
C	0005694	cellular_component	chromosome
C	0030527	molecular_function	structural constituent of chromatin
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	0030527	molecular_function	structural constituent of chromatin
D	0046982	molecular_function	protein heterodimerization activity
E	0000786	cellular_component	nucleosome
E	0003677	molecular_function	DNA binding
E	0005634	cellular_component	nucleus
E	0030527	molecular_function	structural constituent of chromatin
E	0046982	molecular_function	protein heterodimerization activity
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	0030527	molecular_function	structural constituent of chromatin
F	0046982	molecular_function	protein heterodimerization activity
G	0000786	cellular_component	nucleosome
G	0003677	molecular_function	DNA binding
G	0005634	cellular_component	nucleus
G	0005694	cellular_component	chromosome
G	0030527	molecular_function	structural constituent of chromatin
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	0030527	molecular_function	structural constituent of chromatin
H	0046982	molecular_function	protein heterodimerization activity
K	0005524	molecular_function	ATP binding
K	0042393	molecular_function	histone binding
L	0000785	cellular_component	chromatin
L	0003674	molecular_function	molecular_function
L	0003682	molecular_function	chromatin binding
L	0005198	molecular_function	structural molecule activity
L	0005515	molecular_function	protein binding
L	0005634	cellular_component	nucleus
L	0006325	biological_process	chromatin organization
L	0006337	biological_process	nucleosome disassembly
L	0006338	biological_process	chromatin remodeling
L	0006355	biological_process	regulation of DNA-templated transcription
L	0006357	biological_process	regulation of transcription by RNA polymerase II
L	0006368	biological_process	transcription elongation by RNA polymerase II
L	0016514	cellular_component	SWI/SNF complex
L	0016586	cellular_component	RSC-type complex
L	0035267	cellular_component	NuA4 histone acetyltransferase complex
L	0043232	cellular_component	intracellular non-membrane-bounded organelle
L	0045944	biological_process	positive regulation of transcription by RNA polymerase II
M	0000785	cellular_component	chromatin
M	0005198	molecular_function	structural molecule activity
M	0005515	molecular_function	protein binding
M	0005634	cellular_component	nucleus
M	0006325	biological_process	chromatin organization
M	0006337	biological_process	nucleosome disassembly
M	0006338	biological_process	chromatin remodeling
M	0006355	biological_process	regulation of DNA-templated transcription
M	0006357	biological_process	regulation of transcription by RNA polymerase II
M	0006368	biological_process	transcription elongation by RNA polymerase II
M	0016514	cellular_component	SWI/SNF complex
M	0016586	cellular_component	RSC-type complex
M	0043232	cellular_component	intracellular non-membrane-bounded organelle
M	0045944	biological_process	positive regulation of transcription by RNA polymerase II
N	0000785	cellular_component	chromatin
N	0005515	molecular_function	protein binding
N	0005634	cellular_component	nucleus
N	0006337	biological_process	nucleosome disassembly
N	0006338	biological_process	chromatin remodeling
N	0006357	biological_process	regulation of transcription by RNA polymerase II
N	0006368	biological_process	transcription elongation by RNA polymerase II
N	0007059	biological_process	chromosome segregation
N	0015616	molecular_function	DNA translocase activity
N	0016514	cellular_component	SWI/SNF complex
N	0016586	cellular_component	RSC-type complex

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
C	ALA22-VAL28

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

Chain	Residue	Details
B	GLY15-HIS19

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

Chain	Residue	Details
A	LYS15-LEU21

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

Chain	Residue	Details
D	ARG93-GLY115

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

Chain	Residue	Details
A	PRO67-ILE75

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	8
Details	MOD_RES: N6-acetyllysine => ECO:0000250\|UniProtKB:P0C1H4

Chain	Residue	Details
D	LYS6
D	LYS13
D	LYS16
D	LYS21
H	LYS6
H	LYS13
H	LYS16
H	LYS21

site_id	SWS_FT_FI2
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0000269\|PubMed:12757711

Chain	Residue	Details
D	SER15
H	SER15

site_id	SWS_FT_FI3
Number of Residues	2
Details	CARBOHYD: O-linked (GlcNAc) serine => ECO:0000250\|UniProtKB:P62807

Chain	Residue	Details
D	SER113
H	SER113
G	LYS10
G	LYS96

site_id	SWS_FT_FI4
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	LYS121
G	LYS37
H	LYS121

site_id	SWS_FT_FI5
Number of Residues	4
Details	MOD_RES: N6-(2-hydroxyisobutyryl)lysine => ECO:0000250\|UniProtKB:P0C0S8

Chain	Residue	Details
C	LYS75
C	LYS76
G	LYS75
G	LYS76
F	LYS9
F	LYS17
F	LYS45
F	LYS80

site_id	SWS_FT_FI6
Number of Residues	2
Details	MOD_RES: N5-methylglutamine => ECO:0000250

Chain	Residue	Details
C	GLN105
G	GLN105
F	LYS13
F	LYS21

site_id	SWS_FT_FI7
Number of Residues	2
Details	MOD_RES: N6-glutaryllysine; alternate => ECO:0000250\|UniProtKB:P0C0S8

Chain	Residue	Details
C	LYS119
G	LYS119
F	LYS32
F	LYS92

site_id	SWS_FT_FI8
Number of Residues	8
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250

Chain	Residue	Details
C	LYS14
F	SER48
C	LYS16
C	LYS120
G	LYS14
G	LYS16
G	LYS120

site_id	SWS_FT_FI9
Number of Residues	4
Details	MOD_RES: Phosphotyrosine => ECO:0000250\|UniProtKB:P62805

Chain	Residue	Details
B	TYR52
B	TYR89
F	TYR52
F	TYR89

site_id	SWS_FT_FI10
Number of Residues	2
Details	MOD_RES: N6-glutaryllysine; alternate => ECO:0000250\|UniProtKB:P62805

Chain	Residue	Details
B	LYS60
F	LYS60

site_id	SWS_FT_FI11
Number of Residues	2
Details	MOD_RES: N6-succinyllysine => ECO:0000250\|UniProtKB:P62805

Chain	Residue	Details
B	LYS78
F	LYS78

site_id	SWS_FT_FI12
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	LYS32
F	LYS32

site_id	SWS_FT_FI13
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	LYS92
F	LYS92

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