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6SXA

XPF-ERCC1 Cryo-EM Structure, Apo-form

Functional Information from GO Data
ChainGOidnamespacecontents
F0000014molecular_functionsingle-stranded DNA endodeoxyribonuclease activity
F0000109cellular_componentnucleotide-excision repair complex
F0000110cellular_componentnucleotide-excision repair factor 1 complex
F0000712biological_processresolution of meiotic recombination intermediates
F0000723biological_processtelomere maintenance
F0000724biological_processdouble-strand break repair via homologous recombination
F0000781cellular_componentchromosome, telomeric region
F0001094molecular_functionTFIID-class transcription factor complex binding
F0003677molecular_functionDNA binding
F0003684molecular_functiondamaged DNA binding
F0003697molecular_functionsingle-stranded DNA binding
F0004518molecular_functionnuclease activity
F0004519molecular_functionendonuclease activity
F0004520molecular_functionDNA endonuclease activity
F0005515molecular_functionprotein binding
F0005634cellular_componentnucleus
F0005654cellular_componentnucleoplasm
F0005694cellular_componentchromosome
F0006281biological_processDNA repair
F0006289biological_processnucleotide-excision repair
F0006303biological_processdouble-strand break repair via nonhomologous end joining
F0006974biological_processDNA damage response
F0009411biological_processresponse to UV
F0010521molecular_functiontelomerase inhibitor activity
F0016604cellular_componentnuclear body
F0016787molecular_functionhydrolase activity
F0032205biological_processnegative regulation of telomere maintenance
F0034644biological_processcellular response to UV
F0042802molecular_functionidentical protein binding
F0061819biological_processtelomeric DNA-containing double minutes formation
F0070522cellular_componentERCC4-ERCC1 complex
F1901255biological_processnucleotide-excision repair involved in interstrand cross-link repair
F1904357biological_processnegative regulation of telomere maintenance via telomere lengthening
F1905765biological_processnegative regulation of protection from non-homologous end joining at telomere
F1990599molecular_function3' overhang single-stranded DNA endodeoxyribonuclease activity
F1990841molecular_functionpromoter-specific chromatin binding
G0000014molecular_functionsingle-stranded DNA endodeoxyribonuclease activity
G0000109cellular_componentnucleotide-excision repair complex
G0000110cellular_componentnucleotide-excision repair factor 1 complex
G0000723biological_processtelomere maintenance
G0000781cellular_componentchromosome, telomeric region
G0001094molecular_functionTFIID-class transcription factor complex binding
G0003677molecular_functionDNA binding
G0003684molecular_functiondamaged DNA binding
G0003697molecular_functionsingle-stranded DNA binding
G0005515molecular_functionprotein binding
G0005634cellular_componentnucleus
G0005654cellular_componentnucleoplasm
G0005737cellular_componentcytoplasm
G0006281biological_processDNA repair
G0006289biological_processnucleotide-excision repair
G0006302biological_processdouble-strand break repair
G0006303biological_processdouble-strand break repair via nonhomologous end joining
G0006310biological_processDNA recombination
G0006312biological_processmitotic recombination
G0006974biological_processDNA damage response
G0006979biological_processresponse to oxidative stress
G0032204biological_processregulation of telomere maintenance
G0032205biological_processnegative regulation of telomere maintenance
G0061819biological_processtelomeric DNA-containing double minutes formation
G0070522cellular_componentERCC4-ERCC1 complex
G0070914biological_processUV-damage excision repair
G0090656biological_processt-circle formation
G1904431biological_processpositive regulation of t-circle formation
G1905765biological_processnegative regulation of protection from non-homologous end joining at telomere
G1990599molecular_function3' overhang single-stranded DNA endodeoxyribonuclease activity
G1990841molecular_functionpromoter-specific chromatin binding
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues80
DetailsDomain: {"description":"ERCC4"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues21
DetailsRegion: {"description":"Leucine-zipper 1","evidences":[{"source":"PubMed","id":"8887684","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues28
DetailsRegion: {"description":"Leucine-zipper 2","evidences":[{"source":"PubMed","id":"8887684","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues68
DetailsRegion: {"description":"HhH2, dimerization with ERCC1","evidences":[{"source":"PubMed","id":"16076955","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q9QZD4","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues22
DetailsDNA binding: {"evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues2
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)","evidences":[{"source":"PubMed","id":"28112733","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

247536

PDB entries from 2026-01-14

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