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9JNP

Structure of isw1-nucleosome complex in ATP state

Functional Information from GO Data
ChainGOidnamespacecontents
A0000786cellular_componentnucleosome
A0003677molecular_functionDNA binding
A0005634cellular_componentnucleus
A0005694cellular_componentchromosome
C0000786cellular_componentnucleosome
C0003677molecular_functionDNA binding
C0005634cellular_componentnucleus
C0005694cellular_componentchromosome
C0030527molecular_functionstructural constituent of chromatin
C0031507biological_processheterochromatin formation
D0000786cellular_componentnucleosome
D0003677molecular_functionDNA binding
D0005634cellular_componentnucleus
D0005694cellular_componentchromosome
E0000786cellular_componentnucleosome
E0003677molecular_functionDNA binding
E0005634cellular_componentnucleus
E0005694cellular_componentchromosome
G0000786cellular_componentnucleosome
G0003677molecular_functionDNA binding
G0005634cellular_componentnucleus
G0005694cellular_componentchromosome
G0030527molecular_functionstructural constituent of chromatin
G0031507biological_processheterochromatin formation
H0000786cellular_componentnucleosome
H0003677molecular_functionDNA binding
H0005634cellular_componentnucleus
H0005694cellular_componentchromosome
K0000166molecular_functionnucleotide binding
K0000182molecular_functionrDNA binding
K0000785cellular_componentchromatin
K0000976molecular_functiontranscription cis-regulatory region binding
K0001178biological_processregulation of transcriptional start site selection at RNA polymerase II promoter
K0003677molecular_functionDNA binding
K0003682molecular_functionchromatin binding
K0003730molecular_functionmRNA 3'-UTR binding
K0004386molecular_functionhelicase activity
K0005515molecular_functionprotein binding
K0005524molecular_functionATP binding
K0005634cellular_componentnucleus
K0006325biological_processchromatin organization
K0006338biological_processchromatin remodeling
K0006354biological_processDNA-templated transcription elongation
K0006355biological_processregulation of DNA-templated transcription
K0006363biological_processtermination of RNA polymerase I transcription
K0006369biological_processtermination of RNA polymerase II transcription
K0007062biological_processsister chromatid cohesion
K0009408biological_processresponse to heat
K0016587cellular_componentIsw1 complex
K0016787molecular_functionhydrolase activity
K0016887molecular_functionATP hydrolysis activity
K0030874cellular_componentnucleolar chromatin
K0031491molecular_functionnucleosome binding
K0031507biological_processheterochromatin formation
K0036436cellular_componentIsw1a complex
K0036437cellular_componentIsw1b complex
K0045944biological_processpositive regulation of transcription by RNA polymerase II
K0046832biological_processnegative regulation of RNA export from nucleus
K0140750molecular_functionnucleosome array spacer activity
K1902275biological_processregulation of chromatin organization
K1903895biological_processnegative regulation of IRE1-mediated unfolded protein response
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_FI2
Number of Residues2
DetailsModified residue: {"description":"N6-(2-hydroxyisobutyryl)lysine; alternate","evidences":[{"source":"UniProtKB","id":"P0C0S8","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues4
DetailsModified residue: {"description":"N6-(2-hydroxyisobutyryl)lysine","evidences":[{"source":"UniProtKB","id":"P0C0S8","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsModified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P0C0S8","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsModified residue: {"description":"N5-methylglutamine","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues2
DetailsModified residue: {"description":"N6-glutaryllysine; alternate","evidences":[{"source":"UniProtKB","id":"P0C0S8","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues6
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues2
DetailsGlycosylation: {"description":"O-linked (GlcNAc) serine","evidences":[{"source":"UniProtKB","id":"P62807","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI9
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_FI10
Number of Residues165
DetailsDomain: {"description":"Helicase ATP-binding","evidences":[{"source":"PROSITE-ProRule","id":"PRU00541","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues3
DetailsMotif: {"description":"DEAH box"}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues7
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00541","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

238895

PDB entries from 2025-07-16

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