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9QEE

Cryo-EM structure of a DNA-bound XPF-ERCC1-SLX4(330-555)-SLX4IP complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0000109cellular_componentnucleotide-excision repair complex
A0000110cellular_componentnucleotide-excision repair factor 1 complex
A0000712biological_processresolution of meiotic recombination intermediates
A0000723biological_processtelomere maintenance
A0000724biological_processdouble-strand break repair via homologous recombination
A0000781cellular_componentchromosome, telomeric region
A0001094molecular_functionTFIID-class transcription factor complex binding
A0003677molecular_functionDNA binding
A0003684molecular_functiondamaged DNA binding
A0003697molecular_functionsingle-stranded DNA binding
A0004520molecular_functionDNA endonuclease activity
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005694cellular_componentchromosome
A0006281biological_processDNA repair
A0006289biological_processnucleotide-excision repair
A0006303biological_processdouble-strand break repair via nonhomologous end joining
A0006312biological_processmitotic recombination
A0009411biological_processresponse to UV
A0010521molecular_functiontelomerase inhibitor activity
A0016604cellular_componentnuclear body
A0032205biological_processnegative regulation of telomere maintenance
A0034644biological_processcellular response to UV
A0042802molecular_functionidentical protein binding
A0061819biological_processtelomeric DNA-containing double minutes formation
A0070522cellular_componentERCC4-ERCC1 complex
A1901255biological_processnucleotide-excision repair involved in interstrand cross-link repair
A1904357biological_processnegative regulation of telomere maintenance via telomere lengthening
A1905765biological_processnegative regulation of protection from non-homologous end joining at telomere
A1990599molecular_function3' overhang single-stranded DNA endodeoxyribonuclease activity
A1990841molecular_functionpromoter-specific chromatin binding
B0000014molecular_functionsingle-stranded DNA endodeoxyribonuclease activity
B0000109cellular_componentnucleotide-excision repair complex
B0000110cellular_componentnucleotide-excision repair factor 1 complex
B0000723biological_processtelomere maintenance
B0000781cellular_componentchromosome, telomeric region
B0001094molecular_functionTFIID-class transcription factor complex binding
B0003677molecular_functionDNA binding
B0003684molecular_functiondamaged DNA binding
B0003697molecular_functionsingle-stranded DNA binding
B0005515molecular_functionprotein binding
B0005634cellular_componentnucleus
B0005654cellular_componentnucleoplasm
B0005737cellular_componentcytoplasm
B0006281biological_processDNA repair
B0006289biological_processnucleotide-excision repair
B0006302biological_processdouble-strand break repair
B0006303biological_processdouble-strand break repair via nonhomologous end joining
B0006310biological_processDNA recombination
B0006312biological_processmitotic recombination
B0006979biological_processresponse to oxidative stress
B0032204biological_processregulation of telomere maintenance
B0032205biological_processnegative regulation of telomere maintenance
B0061819biological_processtelomeric DNA-containing double minutes formation
B0070522cellular_componentERCC4-ERCC1 complex
B0070914biological_processUV-damage excision repair
B0090656biological_processt-circle formation
B1904431biological_processpositive regulation of t-circle formation
B1905765biological_processnegative regulation of protection from non-homologous end joining at telomere
B1990599molecular_function3' overhang single-stranded DNA endodeoxyribonuclease activity
B1990841molecular_functionpromoter-specific chromatin binding
C0005515molecular_functionprotein binding
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues22
DetailsDNA binding: {"evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues3
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)","evidences":[{"source":"PubMed","id":"28112733","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)","evidences":[{"source":"PubMed","id":"25755297","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"28112733","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues80
DetailsDomain: {"description":"ERCC4"}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues21
DetailsRegion: {"description":"Leucine-zipper 1","evidences":[{"source":"PubMed","id":"8887684","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues28
DetailsRegion: {"description":"Leucine-zipper 2","evidences":[{"source":"PubMed","id":"8887684","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues68
DetailsRegion: {"description":"HhH2, dimerization with ERCC1","evidences":[{"source":"PubMed","id":"16076955","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q9QZD4","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

251422

PDB entries from 2026-04-01

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