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8V6V

Cryo-EM structure of doubly-bound SNF2h-nucleosome complex

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
B0030527molecular_functionstructural constituent of chromatin
B0046982molecular_functionprotein heterodimerization activity
C0000786cellular_componentnucleosome
C0003677molecular_functionDNA binding
C0005634cellular_componentnucleus
C0005694cellular_componentchromosome
C0030527molecular_functionstructural constituent of chromatin
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
F0030527molecular_functionstructural constituent of chromatin
F0046982molecular_functionprotein heterodimerization activity
G0000786cellular_componentnucleosome
G0003677molecular_functionDNA binding
G0005634cellular_componentnucleus
G0005694cellular_componentchromosome
G0030527molecular_functionstructural constituent of chromatin
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
W0000183biological_processrDNA heterochromatin formation
W0000785cellular_componentchromatin
W0000793cellular_componentcondensed chromosome
W0001650cellular_componentfibrillar center
W0003677molecular_functionDNA binding
W0003682molecular_functionchromatin binding
W0004386molecular_functionhelicase activity
W0005515molecular_functionprotein binding
W0005524molecular_functionATP binding
W0005634cellular_componentnucleus
W0005654cellular_componentnucleoplasm
W0005677cellular_componentchromatin silencing complex
W0005694cellular_componentchromosome
W0005721cellular_componentpericentric heterochromatin
W0005730cellular_componentnucleolus
W0006275biological_processregulation of DNA replication
W0006281biological_processDNA repair
W0006325biological_processchromatin organization
W0006334biological_processnucleosome assembly
W0006338biological_processchromatin remodeling
W0006346biological_processDNA methylation-dependent heterochromatin formation
W0006352biological_processDNA-templated transcription initiation
W0006355biological_processregulation of DNA-templated transcription
W0006357biological_processregulation of transcription by RNA polymerase II
W0006974biological_processDNA damage response
W0008623cellular_componentCHRAC
W0016479biological_processnegative regulation of transcription by RNA polymerase I
W0016589cellular_componentNURF complex
W0016590cellular_componentACF complex
W0016787molecular_functionhydrolase activity
W0016887molecular_functionATP hydrolysis activity
W0031010cellular_componentISWI-type complex
W0031213cellular_componentRSF complex
W0031491molecular_functionnucleosome binding
W0031507biological_processheterochromatin formation
W0035861cellular_componentsite of double-strand break
W0042393molecular_functionhistone binding
W0043596cellular_componentnuclear replication fork
W0045740biological_processpositive regulation of DNA replication
W0045893biological_processpositive regulation of DNA-templated transcription
W0045943biological_processpositive regulation of transcription by RNA polymerase I
W0045944biological_processpositive regulation of transcription by RNA polymerase II
W0045945biological_processpositive regulation of transcription by RNA polymerase III
W0090535cellular_componentWICH complex
W0090536cellular_componentNoRC complex
W0110016cellular_componentB-WICH complex
W0140374biological_processantiviral innate immune response
W0140658molecular_functionATP-dependent chromatin remodeler activity
W0140750molecular_functionnucleosome array spacer activity
W0140751molecular_functionhistone octamer slider activity
W1905213biological_processnegative regulation of mitotic chromosome condensation
W1990830biological_processcellular response to leukemia inhibitory factor
X0000183biological_processrDNA heterochromatin formation
X0000785cellular_componentchromatin
X0000793cellular_componentcondensed chromosome
X0001650cellular_componentfibrillar center
X0003677molecular_functionDNA binding
X0003682molecular_functionchromatin binding
X0004386molecular_functionhelicase activity
X0005515molecular_functionprotein binding
X0005524molecular_functionATP binding
X0005634cellular_componentnucleus
X0005654cellular_componentnucleoplasm
X0005677cellular_componentchromatin silencing complex
X0005694cellular_componentchromosome
X0005721cellular_componentpericentric heterochromatin
X0005730cellular_componentnucleolus
X0006275biological_processregulation of DNA replication
X0006281biological_processDNA repair
X0006325biological_processchromatin organization
X0006334biological_processnucleosome assembly
X0006338biological_processchromatin remodeling
X0006346biological_processDNA methylation-dependent heterochromatin formation
X0006352biological_processDNA-templated transcription initiation
X0006355biological_processregulation of DNA-templated transcription
X0006357biological_processregulation of transcription by RNA polymerase II
X0006974biological_processDNA damage response
X0008623cellular_componentCHRAC
X0016479biological_processnegative regulation of transcription by RNA polymerase I
X0016589cellular_componentNURF complex
X0016590cellular_componentACF complex
X0016787molecular_functionhydrolase activity
X0016887molecular_functionATP hydrolysis activity
X0031010cellular_componentISWI-type complex
X0031213cellular_componentRSF complex
X0031491molecular_functionnucleosome binding
X0031507biological_processheterochromatin formation
X0035861cellular_componentsite of double-strand break
X0042393molecular_functionhistone binding
X0043596cellular_componentnuclear replication fork
X0045740biological_processpositive regulation of DNA replication
X0045893biological_processpositive regulation of DNA-templated transcription
X0045943biological_processpositive regulation of transcription by RNA polymerase I
X0045944biological_processpositive regulation of transcription by RNA polymerase II
X0045945biological_processpositive regulation of transcription by RNA polymerase III
X0090535cellular_componentWICH complex
X0090536cellular_componentNoRC complex
X0110016cellular_componentB-WICH complex
X0140374biological_processantiviral innate immune response
X0140658molecular_functionATP-dependent chromatin remodeler activity
X0140750molecular_functionnucleosome array spacer activity
X0140751molecular_functionhistone octamer slider activity
X1905213biological_processnegative regulation of mitotic chromosome condensation
X1990830biological_processcellular response to leukemia inhibitory factor
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_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
DetailsBINDING: BINDING => ECO:0000305
ChainResidueDetails
WASP205
XASP205
DLYS12
DLYS17
HLYS2
HLYS9
HLYS12
HLYS17

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: N-acetylserine => ECO:0007744|PubMed:19413330
ChainResidueDetails
WSER2
XSER2

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:17693683, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:24275569
ChainResidueDetails
WSER66
XSER66
GLYS9
GLYS95

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:20068231
ChainResidueDetails
WTHR113
XTHR113
HLYS117

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163
ChainResidueDetails
WSER116
XSER116
GLYS74
GLYS75
FLYS8
FLYS16
FLYS44
FLYS79

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163
ChainResidueDetails
WSER137
XSER137
FLYS12
FLYS20

site_idSWS_FT_FI7
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
WSER171
WSER755
XSER171
XSER755

site_idSWS_FT_FI8
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
WLYS440
XLYS440
CLYS15
CLYS119
GLYS13
GLYS15
GLYS119

site_idSWS_FT_FI9
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692
ChainResidueDetails
WSER825
XSER825
FTYR51
FTYR88

site_idSWS_FT_FI10
Number of Residues16
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733
ChainResidueDetails
WLYS83
ELYS64
XLYS644
XLYS647
XLYS694
XLYS722
XLYS735
XLYS966
FLYS59
WLYS644
WLYS647
WLYS694
WLYS722
WLYS735
WLYS966
XLYS83

site_idSWS_FT_FI11
Number of Residues2
DetailsMOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P62805
ChainResidueDetails
BLYS77
FLYS77

site_idSWS_FT_FI12
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in UFM1); alternate => ECO:0000250|UniProtKB:P62805
ChainResidueDetails
BLYS31
FLYS31

site_idSWS_FT_FI13
Number of Residues4
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000250|UniProtKB:P62805
ChainResidueDetails
ALYS37
BLYS91
FLYS91

site_idSWS_FT_FI14
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:Q71DI3
ChainResidueDetails
ATYR41
ETYR41

site_idSWS_FT_FI15
Number of Residues4
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P84228
ChainResidueDetails
ALYS56
ALYS79
ELYS56
ELYS79

site_idSWS_FT_FI16
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q71DI3
ChainResidueDetails
ASER57
ESER57

site_idSWS_FT_FI17
Number of Residues4
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q71DI3
ChainResidueDetails
ATHR80
ATHR107
ETHR80
ETHR107

site_idSWS_FT_FI18
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P84243
ChainResidueDetails
ASER86
ESER86

site_idSWS_FT_FI19
Number of Residues2
DetailsMOD_RES: N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:Q71DI3
ChainResidueDetails
ALYS115
ELYS115

site_idSWS_FT_FI20
Number of Residues2
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q71DI3
ChainResidueDetails
ALYS122
ELYS122

site_idSWS_FT_FI21
Number of Residues2
DetailsLIPID: S-palmitoyl cysteine => ECO:0000250|UniProtKB:Q71DI3
ChainResidueDetails
AALA110
EALA110

227111

PDB entries from 2024-11-06

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