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6G0L

Structure of two molecules of the chromatin remodelling enzyme Chd1 bound to a nucleosome

Functional Information from GO Data
ChainGOidnamespacecontents
A0000786cellular_componentnucleosome
A0003677molecular_functionDNA binding
A0005634cellular_componentnucleus
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
D0030527molecular_functionstructural constituent of chromatin
D0046982molecular_functionprotein heterodimerization activity
E0000786cellular_componentnucleosome
E0003677molecular_functionDNA binding
E0005634cellular_componentnucleus
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
H0030527molecular_functionstructural constituent of chromatin
H0046982molecular_functionprotein heterodimerization activity
M0000123cellular_componenthistone acetyltransferase complex
M0000124cellular_componentSAGA complex
M0000166molecular_functionnucleotide binding
M0000182molecular_functionrDNA binding
M0000724biological_processdouble-strand break repair via homologous recombination
M0000729biological_processDNA double-strand break processing
M0000785cellular_componentchromatin
M0000976molecular_functiontranscription cis-regulatory region binding
M0001178biological_processregulation of transcriptional start site selection at RNA polymerase II promoter
M0003677molecular_functionDNA binding
M0003682molecular_functionchromatin binding
M0005524molecular_functionATP binding
M0005634cellular_componentnucleus
M0005739cellular_componentmitochondrion
M0006325biological_processchromatin organization
M0006338biological_processchromatin remodeling
M0006357biological_processregulation of transcription by RNA polymerase II
M0006363biological_processtermination of RNA polymerase I transcription
M0006366biological_processtranscription by RNA polymerase II
M0006368biological_processtranscription elongation by RNA polymerase II
M0006369biological_processtermination of RNA polymerase II transcription
M0007062biological_processsister chromatid cohesion
M0008094molecular_functionATP-dependent activity, acting on DNA
M0010468biological_processregulation of gene expression
M0016787molecular_functionhydrolase activity
M0016887molecular_functionATP hydrolysis activity
M0030874cellular_componentnucleolar chromatin
M0031490molecular_functionchromatin DNA binding
M0034728biological_processnucleosome organization
M0035861cellular_componentsite of double-strand break
M0042393molecular_functionhistone binding
M0046695cellular_componentSLIK (SAGA-like) complex
M0140002molecular_functionhistone H3K4me3 reader activity
M0140658molecular_functionATP-dependent chromatin remodeler activity
M1902275biological_processregulation of chromatin organization
M2000104biological_processnegative regulation of DNA-templated DNA replication
W0000123cellular_componenthistone acetyltransferase complex
W0000124cellular_componentSAGA complex
W0000166molecular_functionnucleotide binding
W0000182molecular_functionrDNA binding
W0000724biological_processdouble-strand break repair via homologous recombination
W0000729biological_processDNA double-strand break processing
W0000785cellular_componentchromatin
W0000976molecular_functiontranscription cis-regulatory region binding
W0001178biological_processregulation of transcriptional start site selection at RNA polymerase II promoter
W0003677molecular_functionDNA binding
W0003682molecular_functionchromatin binding
W0005524molecular_functionATP binding
W0005634cellular_componentnucleus
W0005739cellular_componentmitochondrion
W0006325biological_processchromatin organization
W0006338biological_processchromatin remodeling
W0006357biological_processregulation of transcription by RNA polymerase II
W0006363biological_processtermination of RNA polymerase I transcription
W0006366biological_processtranscription by RNA polymerase II
W0006368biological_processtranscription elongation by RNA polymerase II
W0006369biological_processtermination of RNA polymerase II transcription
W0007062biological_processsister chromatid cohesion
W0008094molecular_functionATP-dependent activity, acting on DNA
W0010468biological_processregulation of gene expression
W0016787molecular_functionhydrolase activity
W0016887molecular_functionATP hydrolysis activity
W0030874cellular_componentnucleolar chromatin
W0031490molecular_functionchromatin DNA binding
W0034728biological_processnucleosome organization
W0035861cellular_componentsite of double-strand break
W0042393molecular_functionhistone binding
W0046695cellular_componentSLIK (SAGA-like) complex
W0140002molecular_functionhistone H3K4me3 reader activity
W0140658molecular_functionATP-dependent chromatin remodeler activity
W1902275biological_processregulation of chromatin organization
W2000104biological_processnegative regulation of DNA-templated DNA replication
Functional Information from PDB Data
site_idAC1
Number of Residues12
Detailsbinding site for residue ADP M 1501
ChainResidue
MGLU375
MMET781
MARG807
MBEF1502
MLEU376
MARG377
MGLY406
MLYS407
MTHR408
MVAL409
MTRP447
MASN779

site_idAC2
Number of Residues6
Detailsbinding site for residue BEF M 1502
ChainResidue
MMET403
MLYS407
MGLU514
MARG804
MARG807
MADP1501

site_idAC3
Number of Residues3
Detailsbinding site for residue BEF W 1501
ChainResidue
WTHR436
WARG804
WADP1502

site_idAC4
Number of Residues8
Detailsbinding site for residue ADP W 1502
ChainResidue
WLEU376
WGLN380
WGLY404
WGLY406
WASN779
WMET781
WARG807
WBEF1501

site_idAC5
Number of Residues8
Detailsbinding site for Di-nucleotide DG I -3 and DC I -2
ChainResidue
AARG116
AVAL117
ATHR118
IDC-4
IDG-1
JDG2
JDC3
JDG4

site_idAC6
Number of Residues8
Detailsbinding site for Di-nucleotide DC I 21 and SER W 524
ChainResidue
IDG20
IDC22
JDG-21
WGLU522
WSER523
WLEU525
WTYR526
WSER528

site_idAC7
Number of Residues10
Detailsbinding site for Di-nucleotide DC I 22 and ASN W 520
ChainResidue
IDC21
IDA23
JDG-21
JDG-22
WLEU518
WLYS519
WALA521
WGLU522
WSER523
WLYS550

site_idAC8
Number of Residues6
Detailsbinding site for Di-nucleotide DC I 45 and DA I 46
ChainResidue
GLYS15
IDC44
IDG47
JDG-44
JDT-46
JDG-45

site_idAC9
Number of Residues6
Detailsbinding site for Di-nucleotide DC I 45 and DA I 46
ChainResidue
GLYS15
IDC44
IDG47
JDG-44
JDT-46
JDG-45

site_idAD1
Number of Residues6
Detailsbinding site for Di-nucleotide DC I 45 and DA I 46
ChainResidue
GLYS15
IDC44
IDG47
JDG-44
JDT-46
JDG-45

site_idAD2
Number of Residues6
Detailsbinding site for Di-nucleotide DC I 45 and DA I 46
ChainResidue
GLYS15
IDC44
IDG47
JDG-44
JDT-46
JDG-45

site_idAD3
Number of Residues6
Detailsbinding site for Di-nucleotide DC I 45 and DA I 46
ChainResidue
GLYS15
IDC44
IDG47
JDG-44
JDT-46
JDG-45

site_idAD4
Number of Residues6
Detailsbinding site for Di-nucleotide DC I 45 and DA I 46
ChainResidue
GLYS15
IDC44
IDG47
JDG-44
JDT-46
JDG-45

site_idAD5
Number of Residues6
Detailsbinding site for Di-nucleotide DC I 45 and DA I 46
ChainResidue
GLYS15
IDC44
IDG47
JDG-44
JDT-46
JDG-45

site_idAD6
Number of Residues6
Detailsbinding site for Di-nucleotide DC I 45 and DA I 46
ChainResidue
IDG47
JDG-44
JDT-46
JDG-45
GLYS15
IDC44

site_idAD7
Number of Residues9
Detailsbinding site for Di-nucleotide DG I -53 and DT J 54
ChainResidue
DLYS43
IDA-54
IDG-52
IDT53
IDT55
JDC-52
JDC-54
JDC53
JDT55

site_idAD8
Number of Residues10
Detailsbinding site for Di-nucleotide DT J -17 and GLU W 493
ChainResidue
IDA16
JDT-16
JDG-18
WLEU434
WTHR491
WTYR492
WTYR494
WILE495
WLEU496
WLYS497

site_idAD9
Number of Residues12
Detailsbinding site for Di-nucleotide DG J -18 and GLU W 493
ChainResidue
IDA17
IDC18
IDC19
JDT-17
JDG-19
JDT-16
WTHR491
WTYR492
WTYR494
WILE495
WLEU496
WLYS497

Functional Information from PROSITE/UniProt
site_idPS00046
Number of Residues7
DetailsHISTONE_H2A Histone H2A signature. AGLqFPV
ChainResidueDetails
CALA21-VAL27
GALA21-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_idPS00598
Number of Residues21
DetailsCHROMO_1 Chromo domain signature. FlIKWtDEshlhn.TWETyesI
ChainResidueDetails
MPHE213-ILE233
MTYR307-ILE327

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 Residues3
DetailsModified residue: {"description":"N6-methyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues5
DetailsModified residue: {"description":"N6-propionyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine; by PAK2","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues4
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues2
DetailsModified residue: {"description":"N6-glutaryllysine; alternate","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues2
DetailsModified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P62805","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI8
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_FI9
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_FI10
Number of Residues4
DetailsDNA binding: {}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues2
DetailsModified residue: {"description":"N6-(2-hydroxyisobutyryl)lysine; alternate","evidences":[{"source":"UniProtKB","id":"P0C0S8","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues4
DetailsModified residue: {"description":"N6-(2-hydroxyisobutyryl)lysine","evidences":[{"source":"UniProtKB","id":"P0C0S8","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI13
Number of Residues2
DetailsModified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P0C0S8","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI14
Number of Residues2
DetailsModified residue: {"description":"N5-methylglutamine","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI15
Number of Residues2
DetailsModified residue: {"description":"N6-glutaryllysine; alternate","evidences":[{"source":"UniProtKB","id":"P0C0S8","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI16
Number of Residues2
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI17
Number of Residues130
DetailsDomain: {"description":"Chromo 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00053","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI18
Number of Residues6
DetailsMotif: {"description":"DEAH box"}
ChainResidueDetails

site_idSWS_FT_FI19
Number of Residues14
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00541","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI20
Number of Residues4
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"12872131","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI21
Number of Residues174
DetailsDomain: {"description":"Helicase ATP-binding","evidences":[{"source":"PROSITE-ProRule","id":"PRU00541","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

239492

PDB entries from 2025-07-30

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