Loading
PDBj
English日本語简体中文繁體中文한국어
✖
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help
SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

8IQF

Cryo-EM structure of the dimeric human CAF1-H3-H4 complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0000785cellular_componentchromatin
A0003682molecular_functionchromatin binding
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0006260biological_processDNA replication
A0006281biological_processDNA repair
A0006325biological_processchromatin organization
A0006334biological_processnucleosome assembly
A0006335biological_processDNA replication-dependent chromatin assembly
A0006974biological_processDNA damage response
A0032991cellular_componentprotein-containing complex
A0033186cellular_componentCAF-1 complex
A0042802molecular_functionidentical protein binding
A0051082molecular_functionunfolded protein binding
A0070087molecular_functionchromo shadow domain binding
B0000785cellular_componentchromatin
B0003682molecular_functionchromatin binding
B0005515molecular_functionprotein binding
B0005634cellular_componentnucleus
B0005654cellular_componentnucleoplasm
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006260biological_processDNA replication
B0006281biological_processDNA repair
B0006325biological_processchromatin organization
B0006334biological_processnucleosome assembly
B0006335biological_processDNA replication-dependent chromatin assembly
B0006974biological_processDNA damage response
B0032991cellular_componentprotein-containing complex
B0033186cellular_componentCAF-1 complex
B0042393molecular_functionhistone binding
B0051082molecular_functionunfolded protein binding
C0000118cellular_componenthistone deacetylase complex
C0000122biological_processnegative regulation of transcription by RNA polymerase II
C0000781cellular_componentchromosome, telomeric region
C0000785cellular_componentchromatin
C0000978molecular_functionRNA polymerase II cis-regulatory region sequence-specific DNA binding
C0005515molecular_functionprotein binding
C0005634cellular_componentnucleus
C0005654cellular_componentnucleoplasm
C0006260biological_processDNA replication
C0006281biological_processDNA repair
C0006325biological_processchromatin organization
C0006334biological_processnucleosome assembly
C0006335biological_processDNA replication-dependent chromatin assembly
C0006338biological_processchromatin remodeling
C0006351biological_processDNA-templated transcription
C0006355biological_processregulation of DNA-templated transcription
C0006974biological_processDNA damage response
C0007420biological_processbrain development
C0008094molecular_functionATP-dependent activity, acting on DNA
C0008285biological_processnegative regulation of cell population proliferation
C0016581cellular_componentNuRD complex
C0016589cellular_componentNURF complex
C0030336biological_processnegative regulation of cell migration
C0030512biological_processnegative regulation of transforming growth factor beta receptor signaling pathway
C0031492molecular_functionnucleosomal DNA binding
C0031507biological_processheterochromatin formation
C0032991cellular_componentprotein-containing complex
C0033186cellular_componentCAF-1 complex
C0035098cellular_componentESC/E(Z) complex
C0042393molecular_functionhistone binding
C0042659biological_processregulation of cell fate specification
C0042826molecular_functionhistone deacetylase binding
C0045892biological_processnegative regulation of DNA-templated transcription
C0045893biological_processpositive regulation of DNA-templated transcription
C0045944biological_processpositive regulation of transcription by RNA polymerase II
C0070822cellular_componentSin3-type complex
C1902455biological_processnegative regulation of stem cell population maintenance
C1902459biological_processpositive regulation of stem cell population maintenance
C2000736biological_processregulation of stem cell differentiation
D0000786cellular_componentnucleosome
D0003677molecular_functionDNA binding
D0005515molecular_functionprotein binding
D0005576cellular_componentextracellular region
D0005634cellular_componentnucleus
D0005654cellular_componentnucleoplasm
D0005694cellular_componentchromosome
D0006325biological_processchromatin organization
D0006334biological_processnucleosome assembly
D0016020cellular_componentmembrane
D0030527molecular_functionstructural constituent of chromatin
D0031492molecular_functionnucleosomal DNA binding
D0031507biological_processheterochromatin formation
D0032200biological_processtelomere organization
D0032991cellular_componentprotein-containing complex
D0040029biological_processepigenetic regulation of gene expression
D0045296molecular_functioncadherin binding
D0046982molecular_functionprotein heterodimerization activity
D0070062cellular_componentextracellular exosome
E0000781cellular_componentchromosome, telomeric region
E0000786cellular_componentnucleosome
E0003677molecular_functionDNA binding
E0003723molecular_functionRNA binding
E0005515molecular_functionprotein binding
E0005576cellular_componentextracellular region
E0005634cellular_componentnucleus
E0005654cellular_componentnucleoplasm
E0005694cellular_componentchromosome
E0006325biological_processchromatin organization
E0006334biological_processnucleosome assembly
E0016020cellular_componentmembrane
E0030527molecular_functionstructural constituent of chromatin
E0032200biological_processtelomere organization
E0032991cellular_componentprotein-containing complex
E0045653biological_processnegative regulation of megakaryocyte differentiation
E0046982molecular_functionprotein heterodimerization activity
E0061644biological_processprotein localization to CENP-A containing chromatin
E0070062cellular_componentextracellular exosome
F0000785cellular_componentchromatin
F0003682molecular_functionchromatin binding
F0005515molecular_functionprotein binding
F0005634cellular_componentnucleus
F0005654cellular_componentnucleoplasm
F0006260biological_processDNA replication
F0006281biological_processDNA repair
F0006325biological_processchromatin organization
F0006334biological_processnucleosome assembly
F0006335biological_processDNA replication-dependent chromatin assembly
F0006974biological_processDNA damage response
F0032991cellular_componentprotein-containing complex
F0033186cellular_componentCAF-1 complex
F0042802molecular_functionidentical protein binding
F0051082molecular_functionunfolded protein binding
F0070087molecular_functionchromo shadow domain binding
G0000785cellular_componentchromatin
G0003682molecular_functionchromatin binding
G0005515molecular_functionprotein binding
G0005634cellular_componentnucleus
G0005654cellular_componentnucleoplasm
G0005737cellular_componentcytoplasm
G0005829cellular_componentcytosol
G0006260biological_processDNA replication
G0006281biological_processDNA repair
G0006325biological_processchromatin organization
G0006334biological_processnucleosome assembly
G0006335biological_processDNA replication-dependent chromatin assembly
G0006974biological_processDNA damage response
G0032991cellular_componentprotein-containing complex
G0033186cellular_componentCAF-1 complex
G0042393molecular_functionhistone binding
G0051082molecular_functionunfolded protein binding
H0000118cellular_componenthistone deacetylase complex
H0000122biological_processnegative regulation of transcription by RNA polymerase II
H0000781cellular_componentchromosome, telomeric region
H0000785cellular_componentchromatin
H0000978molecular_functionRNA polymerase II cis-regulatory region sequence-specific DNA binding
H0005515molecular_functionprotein binding
H0005634cellular_componentnucleus
H0005654cellular_componentnucleoplasm
H0006260biological_processDNA replication
H0006281biological_processDNA repair
H0006325biological_processchromatin organization
H0006334biological_processnucleosome assembly
H0006335biological_processDNA replication-dependent chromatin assembly
H0006338biological_processchromatin remodeling
H0006351biological_processDNA-templated transcription
H0006355biological_processregulation of DNA-templated transcription
H0006974biological_processDNA damage response
H0007420biological_processbrain development
H0008094molecular_functionATP-dependent activity, acting on DNA
H0008285biological_processnegative regulation of cell population proliferation
H0016581cellular_componentNuRD complex
H0016589cellular_componentNURF complex
H0030336biological_processnegative regulation of cell migration
H0030512biological_processnegative regulation of transforming growth factor beta receptor signaling pathway
H0031492molecular_functionnucleosomal DNA binding
H0031507biological_processheterochromatin formation
H0032991cellular_componentprotein-containing complex
H0033186cellular_componentCAF-1 complex
H0035098cellular_componentESC/E(Z) complex
H0042393molecular_functionhistone binding
H0042659biological_processregulation of cell fate specification
H0042826molecular_functionhistone deacetylase binding
H0045892biological_processnegative regulation of DNA-templated transcription
H0045893biological_processpositive regulation of DNA-templated transcription
H0045944biological_processpositive regulation of transcription by RNA polymerase II
H0070822cellular_componentSin3-type complex
H1902455biological_processnegative regulation of stem cell population maintenance
H1902459biological_processpositive regulation of stem cell population maintenance
H2000736biological_processregulation of stem cell differentiation
I0000786cellular_componentnucleosome
I0003677molecular_functionDNA binding
I0005515molecular_functionprotein binding
I0005576cellular_componentextracellular region
I0005634cellular_componentnucleus
I0005654cellular_componentnucleoplasm
I0005694cellular_componentchromosome
I0006325biological_processchromatin organization
I0006334biological_processnucleosome assembly
I0016020cellular_componentmembrane
I0030527molecular_functionstructural constituent of chromatin
I0031492molecular_functionnucleosomal DNA binding
I0031507biological_processheterochromatin formation
I0032200biological_processtelomere organization
I0032991cellular_componentprotein-containing complex
I0040029biological_processepigenetic regulation of gene expression
I0045296molecular_functioncadherin binding
I0046982molecular_functionprotein heterodimerization activity
I0070062cellular_componentextracellular exosome
J0000781cellular_componentchromosome, telomeric region
J0000786cellular_componentnucleosome
J0003677molecular_functionDNA binding
J0003723molecular_functionRNA binding
J0005515molecular_functionprotein binding
J0005576cellular_componentextracellular region
J0005634cellular_componentnucleus
J0005654cellular_componentnucleoplasm
J0005694cellular_componentchromosome
J0006325biological_processchromatin organization
J0006334biological_processnucleosome assembly
J0016020cellular_componentmembrane
J0030527molecular_functionstructural constituent of chromatin
J0032200biological_processtelomere organization
J0032991cellular_componentprotein-containing complex
J0045653biological_processnegative regulation of megakaryocyte differentiation
J0046982molecular_functionprotein heterodimerization activity
J0061644biological_processprotein localization to CENP-A containing chromatin
J0070062cellular_componentextracellular exosome
Functional Information from PROSITE/UniProt
site_idPS00047
Number of Residues5
DetailsHISTONE_H4 Histone H4 signature. GAKRH
ChainResidueDetails
EGLY14-HIS18
site_idPS00322
Number of Residues7
DetailsHISTONE_H3_1 Histone H3 signature 1. KAPRKQL
ChainResidueDetails
DLYS14-LEU20
site_idPS00678
Number of Residues15
DetailsWD_REPEATS_1 Trp-Asp (WD) repeats signature. MASAsvDnTAIIWDV
ChainResidueDetails
BMET144-VAL158
CLEU193-ILE207
CLEU289-LEU303
CLEU333-LEU347
site_idPS00959
Number of Residues9
DetailsHISTONE_H3_2 Histone H3 signature 2. PFqRLVREI
ChainResidueDetails
DPRO66-ILE74
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues80
DetailsRegion: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues72
DetailsRegion: {"description":"Necessary for homodimerization and competence for chromatin assembly"}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues52
DetailsCompositional bias: {"description":"Acidic residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues2
DetailsModified residue: {"description":"Citrulline; alternate","evidences":[{"source":"PubMed","id":"16567635","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues2
DetailsModified residue: {"description":"Phosphothreonine; by HASPIN and VRK1","evidences":[{"source":"PubMed","id":"15681610","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16185088","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"31527692","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues2
DetailsModified residue: {"description":"N6-methyllysine; alternate","evidences":[{"source":"PubMed","id":"16267050","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16457588","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17194708","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues2
DetailsModified residue: {"description":"5-glutamyl serotonin; alternate","evidences":[{"source":"PubMed","id":"30867594","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues2
DetailsModified residue: {"description":"Phosphothreonine; by PKC","evidences":[{"source":"PubMed","id":"20228790","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues2
DetailsModified residue: {"description":"Symmetric dimethylarginine; by PRMT5; alternate","evidences":[{"source":"UniProtKB","id":"P68433","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues2
DetailsModified residue: {"description":"N6-methyllysine; alternate","evidences":[{"source":"PubMed","id":"11242053","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16185088","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16267050","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16457588","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17194708","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine; alternate; by AURKB, AURKC, RPS6KA3, RPS6KA4 and RPS6KA5","evidences":[{"source":"PubMed","id":"10464286","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11856369","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12560483","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15681610","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16185088","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16457588","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues2
DetailsModified residue: {"description":"Phosphothreonine; by PKC and CHEK1","evidences":[{"source":"PubMed","id":"12560483","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18066052","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18243098","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22901803","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues2
DetailsModified residue: {"description":"N6-methyllysine; alternate","evidences":[{"source":"PubMed","id":"15983376","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16185088","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16267050","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16627869","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17194708","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues2
DetailsModified residue: {"description":"N6-methyllysine","evidences":[{"source":"PubMed","id":"15983376","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues2
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"19783980","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI16
Number of Residues8
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"PubMed","id":"22389435","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI17
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"20850016","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI18
Number of Residues2
DetailsModified residue: {"description":"N6-methyllysine; alternate","evidences":[{"source":"PubMed","id":"16267050","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17194708","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI19
Number of Residues2
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"PubMed","id":"22389435","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"29211711","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI20
Number of Residues2
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"20850016","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI21
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P84243","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI22
Number of Residues2
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"Q71DI3","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI23
Number of Residues4
DetailsModified residue: {"description":"N6-glutaryllysine; alternate","evidences":[{"source":"PubMed","id":"31542297","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI24
Number of Residues2
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"PubMed","id":"22389435","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27436229","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI25
Number of Residues2
DetailsModified residue: {"description":"N6-propionyllysine; alternate","evidences":[{"source":"PubMed","id":"17267393","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI26
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine; by PAK2","evidences":[{"source":"PubMed","id":"21724829","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17081983","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"21406692","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI27
Number of Residues2
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"15592455","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI28
Number of Residues2
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P62806","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI29
Number of Residues2
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P62806","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI30
Number of Residues2
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI31
Number of Residues2
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in UFM1); alternate","evidences":[{"source":"PubMed","id":"30886146","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI32
Number of Residues4
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate","evidences":[{"source":"PubMed","id":"19818714","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI33
Number of Residues4
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate","evidences":[{"source":"PubMed","id":"28112733","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI34
Number of Residues186
DetailsRepeat: {"description":"WD 1","evidences":[{"source":"PubMed","id":"39460621","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"8TX8","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI35
Number of Residues98
DetailsRepeat: {"description":"WD 2","evidences":[{"source":"PubMed","id":"39460621","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"8TX8","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI36
Number of Residues94
DetailsRepeat: {"description":"WD 3","evidences":[{"source":"PubMed","id":"39460621","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"8TX8","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI37
Number of Residues90
DetailsRepeat: {"description":"WD 4","evidences":[{"source":"PubMed","id":"39460621","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"8TX8","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI38
Number of Residues86
DetailsRepeat: {"description":"WD 5","evidences":[{"source":"PubMed","id":"39460621","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"8TX8","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI39
Number of Residues112
DetailsRepeat: {"description":"WD 6","evidences":[{"source":"PubMed","id":"39460621","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"8TX8","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI40
Number of Residues64
DetailsRepeat: {"description":"WD 7","evidences":[{"source":"PubMed","id":"39460621","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"8TX8","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI41
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI42
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q60972","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI43
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI44
Number of Residues4
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate","evidences":[{"source":"PubMed","id":"25755297","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"28112733","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI45
Number of Residues86
DetailsRepeat: {"description":"WD 1"}
ChainResidueDetails
site_idSWS_FT_FI46
Number of Residues78
DetailsRepeat: {"description":"WD 3"}
ChainResidueDetails
site_idSWS_FT_FI47
Number of Residues78
DetailsRepeat: {"description":"WD 4"}
ChainResidueDetails
site_idSWS_FT_FI48
Number of Residues102
DetailsRepeat: {"description":"WD 5"}
ChainResidueDetails
site_idSWS_FT_FI49
Number of Residues82
DetailsRepeat: {"description":"WD 6"}
ChainResidueDetails
site_idSWS_FT_FI50
Number of Residues82
DetailsRepeat: {"description":"WD 7"}
ChainResidueDetails

247536

PDB entries from 2026-01-14

PDB statisticsPDBj update infoContact PDBjnumon