Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6UXW

SWI/SNF nucleosome complex with ADP-BeFx

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000182	molecular_function	rDNA binding
A	0000785	cellular_component	chromatin
A	0003677	molecular_function	DNA binding
A	0005515	molecular_function	protein binding
A	0005524	molecular_function	ATP binding
A	0005634	cellular_component	nucleus
A	0006261	biological_process	DNA-templated DNA replication
A	0006302	biological_process	double-strand break repair
A	0006338	biological_process	chromatin remodeling
A	0006355	biological_process	regulation of DNA-templated transcription
A	0006357	biological_process	regulation of transcription by RNA polymerase II
A	0016514	cellular_component	SWI/SNF complex
A	0016887	molecular_function	ATP hydrolysis activity
A	0031492	molecular_function	nucleosomal DNA binding
A	0031496	biological_process	positive regulation of mating type switching
A	0034198	biological_process	cellular response to amino acid starvation
A	0035973	biological_process	aggrephagy
A	0042148	biological_process	DNA strand invasion
A	0042393	molecular_function	histone binding
A	0045815	biological_process	transcription initiation-coupled chromatin remodeling
A	0045944	biological_process	positive regulation of transcription by RNA polymerase II
A	0061629	molecular_function	RNA polymerase II-specific DNA-binding transcription factor binding
A	0140008	molecular_function	histone H4 reader activity
A	0140015	molecular_function	histone H3K14ac reader activity
A	0140566	molecular_function	histone reader activity
A	0140658	molecular_function	ATP-dependent chromatin remodeler activity
A	1900189	biological_process	positive regulation of cell adhesion involved in single-species biofilm formation
A	2000219	biological_process	positive regulation of invasive growth in response to glucose limitation
B	0000785	cellular_component	chromatin
B	0000976	molecular_function	transcription cis-regulatory region binding
B	0003677	molecular_function	DNA binding
B	0005634	cellular_component	nucleus
B	0006261	biological_process	DNA-templated DNA replication
B	0006338	biological_process	chromatin remodeling
B	0006357	biological_process	regulation of transcription by RNA polymerase II
B	0008270	molecular_function	zinc ion binding
B	0016514	cellular_component	SWI/SNF complex
B	0031496	biological_process	positive regulation of mating type switching
B	0034198	biological_process	cellular response to amino acid starvation
B	0045944	biological_process	positive regulation of transcription by RNA polymerase II
B	0061629	molecular_function	RNA polymerase II-specific DNA-binding transcription factor binding
C	0000228	cellular_component	nuclear chromosome
C	0000724	biological_process	double-strand break repair via homologous recombination
C	0000785	cellular_component	chromatin
C	0005515	molecular_function	protein binding
C	0005634	cellular_component	nucleus
C	0005829	cellular_component	cytosol
C	0006338	biological_process	chromatin remodeling
C	0006357	biological_process	regulation of transcription by RNA polymerase II
C	0016514	cellular_component	SWI/SNF complex
C	0045944	biological_process	positive regulation of transcription by RNA polymerase II
C	0045991	biological_process	carbon catabolite activation of transcription
C	0061629	molecular_function	RNA polymerase II-specific DNA-binding transcription factor binding
C	2000219	biological_process	positive regulation of invasive growth in response to glucose limitation
D	0000785	cellular_component	chromatin
D	0003677	molecular_function	DNA binding
D	0005515	molecular_function	protein binding
D	0005634	cellular_component	nucleus
D	0005829	cellular_component	cytosol
D	0006338	biological_process	chromatin remodeling
D	0006355	biological_process	regulation of DNA-templated transcription
D	0006357	biological_process	regulation of transcription by RNA polymerase II
D	0016514	cellular_component	SWI/SNF complex
D	0031496	biological_process	positive regulation of mating type switching
D	0042393	molecular_function	histone binding
D	0045893	biological_process	positive regulation of DNA-templated transcription
D	0045944	biological_process	positive regulation of transcription by RNA polymerase II
E	0000785	cellular_component	chromatin
E	0003677	molecular_function	DNA binding
E	0005515	molecular_function	protein binding
E	0005634	cellular_component	nucleus
E	0005829	cellular_component	cytosol
E	0006338	biological_process	chromatin remodeling
E	0006355	biological_process	regulation of DNA-templated transcription
E	0006357	biological_process	regulation of transcription by RNA polymerase II
E	0016514	cellular_component	SWI/SNF complex
E	0031496	biological_process	positive regulation of mating type switching
E	0042393	molecular_function	histone binding
E	0045893	biological_process	positive regulation of DNA-templated transcription
E	0045944	biological_process	positive regulation of transcription by RNA polymerase II
F	0000785	cellular_component	chromatin
F	0003677	molecular_function	DNA binding
F	0005515	molecular_function	protein binding
F	0005634	cellular_component	nucleus
F	0005829	cellular_component	cytosol
F	0006338	biological_process	chromatin remodeling
F	0006355	biological_process	regulation of DNA-templated transcription
F	0006357	biological_process	regulation of transcription by RNA polymerase II
F	0016514	cellular_component	SWI/SNF complex
F	0031496	biological_process	positive regulation of mating type switching
F	0042393	molecular_function	histone binding
F	0045893	biological_process	positive regulation of DNA-templated transcription
F	0045944	biological_process	positive regulation of transcription by RNA polymerase II
G	0000785	cellular_component	chromatin
G	0003677	molecular_function	DNA binding
G	0005515	molecular_function	protein binding
G	0005634	cellular_component	nucleus
G	0005829	cellular_component	cytosol
G	0006338	biological_process	chromatin remodeling
G	0006355	biological_process	regulation of DNA-templated transcription
G	0006357	biological_process	regulation of transcription by RNA polymerase II
G	0016514	cellular_component	SWI/SNF complex
G	0031496	biological_process	positive regulation of mating type switching
G	0042393	molecular_function	histone binding
G	0045893	biological_process	positive regulation of DNA-templated transcription
G	0045944	biological_process	positive regulation of transcription by RNA polymerase II
H	0000727	biological_process	double-strand break repair via break-induced replication
H	0000785	cellular_component	chromatin
H	0005198	molecular_function	structural molecule activity
H	0005515	molecular_function	protein binding
H	0005634	cellular_component	nucleus
H	0005829	cellular_component	cytosol
H	0006338	biological_process	chromatin remodeling
H	0006357	biological_process	regulation of transcription by RNA polymerase II
H	0016514	cellular_component	SWI/SNF complex
H	0034198	biological_process	cellular response to amino acid starvation
H	0045944	biological_process	positive regulation of transcription by RNA polymerase II
P	0000785	cellular_component	chromatin
P	0003674	molecular_function	molecular_function
P	0003682	molecular_function	chromatin binding
P	0005198	molecular_function	structural molecule activity
P	0005515	molecular_function	protein binding
P	0005634	cellular_component	nucleus
P	0006325	biological_process	chromatin organization
P	0006337	biological_process	nucleosome disassembly
P	0006338	biological_process	chromatin remodeling
P	0006355	biological_process	regulation of DNA-templated transcription
P	0006357	biological_process	regulation of transcription by RNA polymerase II
P	0006368	biological_process	transcription elongation by RNA polymerase II
P	0016514	cellular_component	SWI/SNF complex
P	0016586	cellular_component	RSC-type complex
P	0045944	biological_process	positive regulation of transcription by RNA polymerase II
Q	0000785	cellular_component	chromatin
Q	0005198	molecular_function	structural molecule activity
Q	0005515	molecular_function	protein binding
Q	0005634	cellular_component	nucleus
Q	0006325	biological_process	chromatin organization
Q	0006337	biological_process	nucleosome disassembly
Q	0006338	biological_process	chromatin remodeling
Q	0006355	biological_process	regulation of DNA-templated transcription
Q	0006357	biological_process	regulation of transcription by RNA polymerase II
Q	0006368	biological_process	transcription elongation by RNA polymerase II
Q	0016514	cellular_component	SWI/SNF complex
Q	0016586	cellular_component	RSC-type complex
Q	0045944	biological_process	positive regulation of transcription by RNA polymerase II
R	0000786	cellular_component	nucleosome
R	0003677	molecular_function	DNA binding
R	0005515	molecular_function	protein binding
R	0005634	cellular_component	nucleus
R	0005654	cellular_component	nucleoplasm
R	0005694	cellular_component	chromosome
R	0030527	molecular_function	structural constituent of chromatin
R	0031492	molecular_function	nucleosomal DNA binding
R	0031507	biological_process	heterochromatin formation
R	0046982	molecular_function	protein heterodimerization activity
S	0000786	cellular_component	nucleosome
S	0003677	molecular_function	DNA binding
S	0005515	molecular_function	protein binding
S	0005634	cellular_component	nucleus
S	0005694	cellular_component	chromosome
S	0006334	biological_process	nucleosome assembly
S	0030527	molecular_function	structural constituent of chromatin
S	0031507	biological_process	heterochromatin formation
S	0046982	molecular_function	protein heterodimerization activity
T	0000786	cellular_component	nucleosome
T	0003677	molecular_function	DNA binding
T	0005634	cellular_component	nucleus
T	0005694	cellular_component	chromosome
T	0030527	molecular_function	structural constituent of chromatin
T	0031507	biological_process	heterochromatin formation
T	0046982	molecular_function	protein heterodimerization activity
U	0000786	cellular_component	nucleosome
U	0002227	biological_process	innate immune response in mucosa
U	0003677	molecular_function	DNA binding
U	0005515	molecular_function	protein binding
U	0005634	cellular_component	nucleus
U	0005694	cellular_component	chromosome
U	0006325	biological_process	chromatin organization
U	0019731	biological_process	antibacterial humoral response
U	0030527	molecular_function	structural constituent of chromatin
U	0031507	biological_process	heterochromatin formation
U	0046982	molecular_function	protein heterodimerization activity
U	0061844	biological_process	antimicrobial humoral immune response mediated by antimicrobial peptide
V	0000786	cellular_component	nucleosome
V	0003677	molecular_function	DNA binding
V	0005515	molecular_function	protein binding
V	0005634	cellular_component	nucleus
V	0005654	cellular_component	nucleoplasm
V	0005694	cellular_component	chromosome
V	0030527	molecular_function	structural constituent of chromatin
V	0031492	molecular_function	nucleosomal DNA binding
V	0031507	biological_process	heterochromatin formation
V	0046982	molecular_function	protein heterodimerization activity
W	0000786	cellular_component	nucleosome
W	0003677	molecular_function	DNA binding
W	0005515	molecular_function	protein binding
W	0005634	cellular_component	nucleus
W	0005694	cellular_component	chromosome
W	0006334	biological_process	nucleosome assembly
W	0030527	molecular_function	structural constituent of chromatin
W	0031507	biological_process	heterochromatin formation
W	0046982	molecular_function	protein heterodimerization activity
X	0000786	cellular_component	nucleosome
X	0003677	molecular_function	DNA binding
X	0005634	cellular_component	nucleus
X	0005694	cellular_component	chromosome
X	0030527	molecular_function	structural constituent of chromatin
X	0031507	biological_process	heterochromatin formation
X	0046982	molecular_function	protein heterodimerization activity
Y	0000786	cellular_component	nucleosome
Y	0002227	biological_process	innate immune response in mucosa
Y	0003677	molecular_function	DNA binding
Y	0005515	molecular_function	protein binding
Y	0005634	cellular_component	nucleus
Y	0005694	cellular_component	chromosome
Y	0006325	biological_process	chromatin organization
Y	0019731	biological_process	antibacterial humoral response
Y	0030527	molecular_function	structural constituent of chromatin
Y	0031507	biological_process	heterochromatin formation
Y	0046982	molecular_function	protein heterodimerization activity
Y	0061844	biological_process	antimicrobial humoral immune response mediated by antimicrobial peptide
Z	0000785	cellular_component	chromatin
Z	0005515	molecular_function	protein binding
Z	0005634	cellular_component	nucleus
Z	0006337	biological_process	nucleosome disassembly
Z	0006338	biological_process	chromatin remodeling
Z	0006357	biological_process	regulation of transcription by RNA polymerase II
Z	0006368	biological_process	transcription elongation by RNA polymerase II
Z	0007059	biological_process	chromosome segregation
Z	0015616	molecular_function	DNA translocase activity
Z	0016514	cellular_component	SWI/SNF complex
Z	0016586	cellular_component	RSC-type complex

Functional Information from PDB Data

site_id	AC1
Number of Residues	7
Details	binding site for residue PO4 P 501

Chain	Residue
P	HIS15
P	ASP190
P	ALA224
P	GLN229
P	LYS232
P	PO4503
P	HOH608

site_id	AC2
Number of Residues	2
Details	binding site for residue PO4 P 502

Chain	Residue
P	ASN53
P	TYR89

site_id	AC3
Number of Residues	11
Details	binding site for residue PO4 P 503

Chain	Residue
P	HIS15
P	ARG16
P	ALA161
P	GLY186
P	LYS232
P	SER397
P	THR398
P	PO4501
P	HOH602
P	HOH603
P	HOH608

site_id	AC4
Number of Residues	7
Details	binding site for residue PO4 P 504

Chain	Residue
P	HIS11
P	GLY13
P	GLU141
P	PO4505
P	HOH601
P	HOH602
P	HOH612

site_id	AC5
Number of Residues	6
Details	binding site for residue PO4 P 505

Chain	Residue
P	SER14
P	ASP158
P	SER162
P	ASN165
P	ARG181
P	PO4504

site_id	AC6
Number of Residues	7
Details	binding site for residue PO4 Q 501

Chain	Residue
Q	SER16
Q	GLN17
Q	ASN70
Q	GLY71
Q	THR166
Q	HIS167
Q	HIS168

site_id	AC7
Number of Residues	4
Details	binding site for residue PO4 Q 502

Chain	Residue
Q	ARG15
Q	GLY338
Q	SER425
Q	GLU426

site_id	AC8
Number of Residues	4
Details	binding site for residue PO4 Q 503

Chain	Residue
Q	GLY344
Q	LYS346
Q	HOH605
Q	HOH616

site_id	AC9
Number of Residues	4
Details	binding site for residue PO4 Q 504

Chain	Residue
Q	ARG15
Q	ASP163
Q	GLY338
Q	HOH601

site_id	AD1
Number of Residues	4
Details	binding site for residue PO4 Q 505

Chain	Residue
Q	ASP206
Q	ASP208
Q	ASP286
Q	LYS288

site_id	AD2
Number of Residues	5
Details	binding site for residue PO4 Q 506

Chain	Residue
P	LYS293
Q	GLY314
Q	ASP318
Q	ASP356
Q	HIS357

site_id	AD3
Number of Residues	2
Details	binding site for residue PO4 A 1801

Chain	Residue
A	ARG619
P	ASP431

site_id	AD4
Number of Residues	14
Details	binding site for residue ADP A 1802

Chain	Residue
A	THR766
A	LYS768
A	TYR770
A	GLY795
A	GLY797
A	LYS798
A	THR799
A	ILE800
A	TRP838
A	ASN1171
A	GLN1173
A	ILE1200
A	BEF1803
A	MG1804

site_id	AD5
Number of Residues	5
Details	binding site for residue BEF A 1803

Chain	Residue
A	ASN1171
A	ARG1196
A	ARG1199
A	ADP1802
A	MG1804

site_id	AD6
Number of Residues	3
Details	binding site for residue MG A 1804

Chain	Residue
A	GLU895
A	ADP1802
A	BEF1803

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
T	ALA21-VAL27

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

Chain	Residue	Details
S	GLY14-HIS18

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

Chain	Residue	Details
R	LYS14-LEU20

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

Chain	Residue	Details
U	ARG89-GLY111

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

Chain	Residue	Details
R	PRO66-ILE74

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	Modified residue: {"description":"N6-methyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P68431","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	2
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"Q71DI3","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	4
Details	Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P84228","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q71DI3","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	2
Details	Modified residue: {"description":"N6-methyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q71DI3","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	4
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"Q71DI3","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P84243","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	2
Details	Modified residue: {"description":"N6-glutaryllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q71DI3","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	2
Details	Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q71DI3","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	2
Details	Lipidation: {"description":"S-palmitoyl cysteine","evidences":[{"source":"UniProtKB","id":"Q71DI3","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	1
Details	Modified residue: {"description":"N6-methyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI12
Number of Residues	4
Details	Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI13
Number of Residues	4
Details	Modified residue: {"description":"N6-propionyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI14
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine; by PAK2","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI15
Number of Residues	4
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI16
Number of Residues	2
Details	Modified residue: {"description":"N6-methacryllysine; alternate","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI17
Number of Residues	2
Details	Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI18
Number of Residues	2
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in UFM1); alternate","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI19
Number of Residues	4
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI20
Number of Residues	2
Details	Modified residue: {"description":"N6-benzoyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P0C0S8","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI21
Number of Residues	2
Details	Modified residue: {"description":"N6-isonicotinyllysine","evidences":[{"source":"UniProtKB","id":"P0C0S8","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI22
Number of Residues	2
Details	Modified residue: {"description":"N6-benzoyllysine; alternate","evidences":[{"source":"UniProtKB","id":"C0HKE1","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI23
Number of Residues	4
Details	Modified residue: {"description":"N6-(2-hydroxyisobutyryl)lysine","evidences":[{"source":"UniProtKB","id":"P0C0S8","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI24
Number of Residues	2
Details	Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P0C0S8","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI25
Number of Residues	2
Details	Modified residue: {"description":"N5-methylglutamine","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI26
Number of Residues	2
Details	Modified residue: {"description":"N6-glutaryllysine; alternate","evidences":[{"source":"UniProtKB","id":"P0C0S8","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI27
Number of Residues	6
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI28
Number of Residues	4
Details	Modified residue: {"description":"N6-isonicotinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q93079","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI29
Number of Residues	6
Details	Modified residue: {"description":"N6-methacryllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q93079","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI30
Number of Residues	2
Details	Glycosylation: {"description":"O-linked (GlcNAc) serine","evidences":[{"source":"UniProtKB","id":"P62807","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI31
Number of Residues	4
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"UniProtKB","id":"P0C1H4","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI32
Number of Residues	165
Details	Domain: {"description":"Helicase ATP-binding","evidences":[{"source":"PROSITE-ProRule","id":"PRU00541","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI33
Number of Residues	163
Details	Domain: {"description":"Helicase C-terminal","evidences":[{"source":"PROSITE-ProRule","id":"PRU00542","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI34
Number of Residues	3
Details	Motif: {"description":"DEGH box"}

Chain

Residue

Details

site_id	SWS_FT_FI35
Number of Residues	7
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00541","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI36
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18407956","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI37
Number of Residues	2
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"22106047","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI38
Number of Residues	17
Details	Zinc finger: {"description":"C4-type"}

Chain

Residue

Details

site_id	SWS_FT_FI39
Number of Residues	194
Details	Domain: {"description":"SWIRM","evidences":[{"source":"PROSITE-ProRule","id":"PRU00247","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI40
Number of Residues	56
Details	Region: {"description":"Leucine-zipper"}

Chain

Residue

Details

site_id	SWS_FT_FI41
Number of Residues	51
Details	Domain: {"description":"SANT","evidences":[{"source":"PROSITE-ProRule","id":"PRU00624","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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