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6TDA

Structure of SWI/SNF chromatin remodeler RSC bound to a nucleosome

Functional Information from GO Data
ChainGOidnamespacecontents
A0000786cellular_componentnucleosome
A0003677molecular_functionDNA binding
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005694cellular_componentchromosome
A0030527molecular_functionstructural constituent of chromatin
A0046982molecular_functionprotein heterodimerization activity
B0000786cellular_componentnucleosome
B0003677molecular_functionDNA binding
B0005515molecular_functionprotein binding
B0005634cellular_componentnucleus
B0005694cellular_componentchromosome
B0006334biological_processnucleosome assembly
B0030527molecular_functionstructural constituent of chromatin
B0046982molecular_functionprotein heterodimerization activity
C0000786cellular_componentnucleosome
C0003677molecular_functionDNA binding
C0005634cellular_componentnucleus
C0005694cellular_componentchromosome
C0030527molecular_functionstructural constituent of chromatin
C0031507biological_processheterochromatin formation
C0046982molecular_functionprotein heterodimerization activity
D0000786cellular_componentnucleosome
D0003677molecular_functionDNA binding
D0005515molecular_functionprotein binding
D0005634cellular_componentnucleus
D0005694cellular_componentchromosome
D0030527molecular_functionstructural constituent of chromatin
D0046982molecular_functionprotein heterodimerization activity
E0000786cellular_componentnucleosome
E0003677molecular_functionDNA binding
E0005515molecular_functionprotein binding
E0005634cellular_componentnucleus
E0005654cellular_componentnucleoplasm
E0005694cellular_componentchromosome
E0030527molecular_functionstructural constituent of chromatin
E0046982molecular_functionprotein heterodimerization activity
F0000786cellular_componentnucleosome
F0003677molecular_functionDNA binding
F0005515molecular_functionprotein binding
F0005634cellular_componentnucleus
F0005694cellular_componentchromosome
F0006334biological_processnucleosome assembly
F0030527molecular_functionstructural constituent of chromatin
F0046982molecular_functionprotein heterodimerization activity
G0000786cellular_componentnucleosome
G0003677molecular_functionDNA binding
G0005634cellular_componentnucleus
G0005694cellular_componentchromosome
G0030527molecular_functionstructural constituent of chromatin
G0031507biological_processheterochromatin formation
G0046982molecular_functionprotein heterodimerization activity
H0000786cellular_componentnucleosome
H0003677molecular_functionDNA binding
H0005515molecular_functionprotein binding
H0005634cellular_componentnucleus
H0005694cellular_componentchromosome
H0030527molecular_functionstructural constituent of chromatin
H0046982molecular_functionprotein heterodimerization activity
K0000086biological_processG2/M transition of mitotic cell cycle
K0000228cellular_componentnuclear chromosome
K0000785cellular_componentchromatin
K0003712molecular_functiontranscription coregulator activity
K0005515molecular_functionprotein binding
K0005634cellular_componentnucleus
K0006302biological_processdouble-strand break repair
K0006325biological_processchromatin organization
K0006337biological_processnucleosome disassembly
K0006338biological_processchromatin remodeling
K0006357biological_processregulation of transcription by RNA polymerase II
K0006368biological_processtranscription elongation by RNA polymerase II
K0007059biological_processchromosome segregation
K0016586cellular_componentRSC-type complex
K0031055biological_processchromatin remodeling at centromere
K0031491molecular_functionnucleosome binding
K0033262biological_processregulation of nuclear cell cycle DNA replication
L0008270molecular_functionzinc ion binding
M0000785cellular_componentchromatin
M0003674molecular_functionmolecular_function
M0005515molecular_functionprotein binding
M0005634cellular_componentnucleus
M0006325biological_processchromatin organization
M0006337biological_processnucleosome disassembly
M0006338biological_processchromatin remodeling
M0006368biological_processtranscription elongation by RNA polymerase II
M0016586cellular_componentRSC-type complex
M0031490molecular_functionchromatin DNA binding
N0000785cellular_componentchromatin
N0003677molecular_functionDNA binding
N0005634cellular_componentnucleus
N0006325biological_processchromatin organization
N0006337biological_processnucleosome disassembly
N0006338biological_processchromatin remodeling
N0006355biological_processregulation of DNA-templated transcription
N0006357biological_processregulation of transcription by RNA polymerase II
N0006368biological_processtranscription elongation by RNA polymerase II
N0009303biological_processrRNA transcription
N0016586cellular_componentRSC-type complex
O0000785cellular_componentchromatin
O0005198molecular_functionstructural molecule activity
O0005515molecular_functionprotein binding
O0005634cellular_componentnucleus
O0006325biological_processchromatin organization
O0006337biological_processnucleosome disassembly
O0006338biological_processchromatin remodeling
O0016586cellular_componentRSC-type complex
O0032968biological_processpositive regulation of transcription elongation by RNA polymerase II
P0000785cellular_componentchromatin
P0003674molecular_functionmolecular_function
P0005515molecular_functionprotein binding
P0005634cellular_componentnucleus
P0006325biological_processchromatin organization
P0006337biological_processnucleosome disassembly
P0006338biological_processchromatin remodeling
P0006357biological_processregulation of transcription by RNA polymerase II
P0006368biological_processtranscription elongation by RNA polymerase II
P0016586cellular_componentRSC-type complex
Q0000086biological_processG2/M transition of mitotic cell cycle
Q0000785cellular_componentchromatin
Q0003682molecular_functionchromatin binding
Q0005515molecular_functionprotein binding
Q0005634cellular_componentnucleus
Q0006337biological_processnucleosome disassembly
Q0006338biological_processchromatin remodeling
Q0006368biological_processtranscription elongation by RNA polymerase II
Q0016586cellular_componentRSC-type complex
R0000785cellular_componentchromatin
R0003682molecular_functionchromatin binding
R0005515molecular_functionprotein binding
R0005634cellular_componentnucleus
R0006325biological_processchromatin organization
R0006337biological_processnucleosome disassembly
R0006338biological_processchromatin remodeling
R0006366biological_processtranscription by RNA polymerase II
R0006368biological_processtranscription elongation by RNA polymerase II
R0016586cellular_componentRSC-type complex
R0140006molecular_functionhistone H3 reader activity
R0140008molecular_functionhistone H4 reader activity
S0000166molecular_functionnucleotide binding
S0000775cellular_componentchromosome, centromeric region
S0000785cellular_componentchromatin
S0003677molecular_functionDNA binding
S0003682molecular_functionchromatin binding
S0003824molecular_functioncatalytic activity
S0004386molecular_functionhelicase activity
S0005515molecular_functionprotein binding
S0005524molecular_functionATP binding
S0005634cellular_componentnucleus
S0006284biological_processbase-excision repair
S0006302biological_processdouble-strand break repair
S0006325biological_processchromatin organization
S0006337biological_processnucleosome disassembly
S0006338biological_processchromatin remodeling
S0006355biological_processregulation of DNA-templated transcription
S0006366biological_processtranscription by RNA polymerase II
S0006368biological_processtranscription elongation by RNA polymerase II
S0007010biological_processcytoskeleton organization
S0007059biological_processchromosome segregation
S0010468biological_processregulation of gene expression
S0015616molecular_functionDNA translocase activity
S0016586cellular_componentRSC-type complex
S0016787molecular_functionhydrolase activity
S0016887molecular_functionATP hydrolysis activity
S0031055biological_processchromatin remodeling at centromere
S0031507biological_processheterochromatin formation
S0042393molecular_functionhistone binding
S0045944biological_processpositive regulation of transcription by RNA polymerase II
S0051321biological_processmeiotic cell cycle
S0140008molecular_functionhistone H4 reader activity
S0140015molecular_functionhistone H3K14ac reader activity
S0140054molecular_functionhistone H2A reader activity
S0140658molecular_functionATP-dependent chromatin remodeler activity
S0140750molecular_functionnucleosome array spacer activity
T0000785cellular_componentchromatin
T0003674molecular_functionmolecular_function
T0003682molecular_functionchromatin binding
T0005198molecular_functionstructural molecule activity
T0005515molecular_functionprotein binding
T0005634cellular_componentnucleus
T0006325biological_processchromatin organization
T0006337biological_processnucleosome disassembly
T0006338biological_processchromatin remodeling
T0006355biological_processregulation of DNA-templated transcription
T0006357biological_processregulation of transcription by RNA polymerase II
T0006368biological_processtranscription elongation by RNA polymerase II
T0016514cellular_componentSWI/SNF complex
T0016586cellular_componentRSC-type complex
T0035267cellular_componentNuA4 histone acetyltransferase complex
T0045944biological_processpositive regulation of transcription by RNA polymerase II
U0000785cellular_componentchromatin
U0005198molecular_functionstructural molecule activity
U0005515molecular_functionprotein binding
U0005634cellular_componentnucleus
U0006325biological_processchromatin organization
U0006337biological_processnucleosome disassembly
U0006338biological_processchromatin remodeling
U0006355biological_processregulation of DNA-templated transcription
U0006357biological_processregulation of transcription by RNA polymerase II
U0006368biological_processtranscription elongation by RNA polymerase II
U0016514cellular_componentSWI/SNF complex
U0016586cellular_componentRSC-type complex
U0045944biological_processpositive regulation of transcription by RNA polymerase II
V0000785cellular_componentchromatin
V0005515molecular_functionprotein binding
V0005634cellular_componentnucleus
V0006337biological_processnucleosome disassembly
V0006338biological_processchromatin remodeling
V0006357biological_processregulation of transcription by RNA polymerase II
V0006368biological_processtranscription elongation by RNA polymerase II
V0007059biological_processchromosome segregation
V0015616molecular_functionDNA translocase activity
V0016514cellular_componentSWI/SNF complex
V0016586cellular_componentRSC-type complex
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue ZN L 560
ChainResidue
LCYS260
LCYS263
LCYS283
LCYS286

Functional Information from PROSITE/UniProt
site_idPS00046
Number of Residues7
DetailsHISTONE_H2A Histone H2A signature. AGLqFPV
ChainResidueDetails
CALA21-VAL27

site_idPS00047
Number of Residues5
DetailsHISTONE_H4 Histone H4 signature. GAKRH
ChainResidueDetails
BGLY14-HIS18

site_idPS00322
Number of Residues7
DetailsHISTONE_H3_1 Histone H3 signature 1. KAPRKQL
ChainResidueDetails
ALYS14-LEU20

site_idPS00357
Number of Residues23
DetailsHISTONE_H2B Histone H2B signature. REIQTavRlLLpGELaKHAVSEG
ChainResidueDetails
DARG89-GLY111

site_idPS00633
Number of Residues58
DetailsBROMODOMAIN_1 Bromodomain signature. TsiFeklpSkrdyp..DYFkvIekpMaidiIlknckngt..Yktleevrqalqt.MfeNArfY
ChainResidueDetails
STHR1275-TYR1332
RPHE77-TYR133
RSER210-PHE267

site_idPS00959
Number of Residues9
DetailsHISTONE_H3_2 Histone H3 signature 2. PFqRLVREI
ChainResidueDetails
APRO66-ILE74

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"Q71DI3","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P84228","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q71DI3","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsModified residue: {"description":"N6-methyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q71DI3","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues4
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"Q71DI3","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P84243","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues2
DetailsModified residue: {"description":"N6-glutaryllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q71DI3","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues2
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q71DI3","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues2
DetailsLipidation: {"description":"S-palmitoyl cysteine","evidences":[{"source":"UniProtKB","id":"Q71DI3","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues4
DetailsDNA binding: {}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues5
DetailsModified residue: {"description":"N6-propionyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues1
DetailsModified residue: {"description":"N6-methyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI13
Number of Residues4
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI14
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine; by PAK2","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI15
Number of Residues4
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI16
Number of Residues2
DetailsModified residue: {"description":"N6-glutaryllysine; alternate","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI17
Number of Residues2
DetailsModified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI18
Number of Residues2
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in UFM1); alternate","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI19
Number of Residues4
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI20
Number of Residues2
DetailsModified residue: {"description":"N6-(2-hydroxyisobutyryl)lysine; alternate","evidences":[{"source":"UniProtKB","id":"P0C0S8","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI21
Number of Residues4
DetailsModified residue: {"description":"N6-(2-hydroxyisobutyryl)lysine","evidences":[{"source":"UniProtKB","id":"P0C0S8","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI22
Number of Residues2
DetailsModified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P0C0S8","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI23
Number of Residues2
DetailsModified residue: {"description":"N5-methylglutamine","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI24
Number of Residues4
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI25
Number of Residues2
DetailsGlycosylation: {"description":"O-linked (GlcNAc) serine","evidences":[{"source":"UniProtKB","id":"P62807","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI26
Number of Residues4
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"UniProtKB","id":"P0C1H4","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI27
Number of Residues41
DetailsRegion: {"description":"Interaction with STH1","evidences":[{"source":"PubMed","id":"9154831","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI28
Number of Residues97
DetailsDomain: {"description":"SWIRM","evidences":[{"source":"PROSITE-ProRule","id":"PRU00247","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI29
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00228","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI30
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"19779198","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI31
Number of Residues165
DetailsDomain: {"description":"Helicase ATP-binding","evidences":[{"source":"PROSITE-ProRule","id":"PRU00541","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI32
Number of Residues3
DetailsMotif: {"description":"DEGH box"}
ChainResidueDetails

site_idSWS_FT_FI33
Number of Residues7
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

239492

PDB entries from 2025-07-30

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