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6BOR

Human APE1 substrate complex with an G/G mismatch adjacent the THF

Functional Information from GO Data
ChainGOidnamespacecontents
A0000723biological_processtelomere maintenance
A0000781cellular_componentchromosome, telomeric region
A0003677molecular_functionDNA binding
A0003684molecular_functiondamaged DNA binding
A0003691molecular_functiondouble-stranded telomeric DNA binding
A0003713molecular_functiontranscription coactivator activity
A0003714molecular_functiontranscription corepressor activity
A0003723molecular_functionRNA binding
A0003824molecular_functioncatalytic activity
A0003906molecular_functionDNA-(apurinic or apyrimidinic site) endonuclease activity
A0004518molecular_functionnuclease activity
A0004519molecular_functionendonuclease activity
A0004520molecular_functionDNA endonuclease activity
A0004523molecular_functionRNA-DNA hybrid ribonuclease activity
A0004527molecular_functionexonuclease activity
A0004528molecular_functionphosphodiesterase I activity
A0004844molecular_functionuracil DNA N-glycosylase activity
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005730cellular_componentnucleolus
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0005783cellular_componentendoplasmic reticulum
A0005813cellular_componentcentrosome
A0005840cellular_componentribosome
A0006281biological_processDNA repair
A0006284biological_processbase-excision repair
A0006287biological_processbase-excision repair, gap-filling
A0006308biological_processDNA catabolic process
A0006310biological_processDNA recombination
A0008081molecular_functionphosphoric diester hydrolase activity
A0008296molecular_function3'-5'-DNA exonuclease activity
A0008309molecular_functiondouble-stranded DNA exodeoxyribonuclease activity
A0008311molecular_functiondouble-stranded DNA 3'-5' DNA exonuclease activity
A0008408molecular_function3'-5' exonuclease activity
A0016491molecular_functionoxidoreductase activity
A0016607cellular_componentnuclear speck
A0016890molecular_functionsite-specific endodeoxyribonuclease activity, specific for altered base
A0031490molecular_functionchromatin DNA binding
A0042981biological_processregulation of apoptotic process
A0043488biological_processregulation of mRNA stability
A0044029biological_processpositive regulation of gene expression via chromosomal CpG island demethylation
A0045454biological_processcell redox homeostasis
A0045892biological_processnegative regulation of DNA-templated transcription
A0045944biological_processpositive regulation of transcription by RNA polymerase II
A0046872molecular_functionmetal ion binding
A0048471cellular_componentperinuclear region of cytoplasm
A0052720molecular_functionclass II DNA-(apurinic or apyrimidinic site) endonuclease activity
A0090580molecular_functionphosphodiesterase activity, acting on 3'-phosphoglycolate-terminated DNA strands
A0097698biological_processtelomere maintenance via base-excision repair
A0140431molecular_functionDNA-(abasic site) binding
B0000723biological_processtelomere maintenance
B0000781cellular_componentchromosome, telomeric region
B0003677molecular_functionDNA binding
B0003684molecular_functiondamaged DNA binding
B0003691molecular_functiondouble-stranded telomeric DNA binding
B0003713molecular_functiontranscription coactivator activity
B0003714molecular_functiontranscription corepressor activity
B0003723molecular_functionRNA binding
B0003824molecular_functioncatalytic activity
B0003906molecular_functionDNA-(apurinic or apyrimidinic site) endonuclease activity
B0004518molecular_functionnuclease activity
B0004519molecular_functionendonuclease activity
B0004520molecular_functionDNA endonuclease activity
B0004523molecular_functionRNA-DNA hybrid ribonuclease activity
B0004527molecular_functionexonuclease activity
B0004528molecular_functionphosphodiesterase I activity
B0004844molecular_functionuracil DNA N-glycosylase activity
B0005515molecular_functionprotein binding
B0005634cellular_componentnucleus
B0005654cellular_componentnucleoplasm
B0005730cellular_componentnucleolus
B0005737cellular_componentcytoplasm
B0005739cellular_componentmitochondrion
B0005783cellular_componentendoplasmic reticulum
B0005813cellular_componentcentrosome
B0005840cellular_componentribosome
B0006281biological_processDNA repair
B0006284biological_processbase-excision repair
B0006287biological_processbase-excision repair, gap-filling
B0006308biological_processDNA catabolic process
B0006310biological_processDNA recombination
B0008081molecular_functionphosphoric diester hydrolase activity
B0008296molecular_function3'-5'-DNA exonuclease activity
B0008309molecular_functiondouble-stranded DNA exodeoxyribonuclease activity
B0008311molecular_functiondouble-stranded DNA 3'-5' DNA exonuclease activity
B0008408molecular_function3'-5' exonuclease activity
B0016491molecular_functionoxidoreductase activity
B0016607cellular_componentnuclear speck
B0016890molecular_functionsite-specific endodeoxyribonuclease activity, specific for altered base
B0031490molecular_functionchromatin DNA binding
B0042981biological_processregulation of apoptotic process
B0043488biological_processregulation of mRNA stability
B0044029biological_processpositive regulation of gene expression via chromosomal CpG island demethylation
B0045454biological_processcell redox homeostasis
B0045892biological_processnegative regulation of DNA-templated transcription
B0045944biological_processpositive regulation of transcription by RNA polymerase II
B0046872molecular_functionmetal ion binding
B0048471cellular_componentperinuclear region of cytoplasm
B0052720molecular_functionclass II DNA-(apurinic or apyrimidinic site) endonuclease activity
B0090580molecular_functionphosphodiesterase activity, acting on 3'-phosphoglycolate-terminated DNA strands
B0097698biological_processtelomere maintenance via base-excision repair
B0140431molecular_functionDNA-(abasic site) binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue EDO A 401
ChainResidue
AASP189
APHE192
APHE240
AHOH552

site_idAC2
Number of Residues8
Detailsbinding site for residue EDO A 402
ChainResidue
AHOH517
AHOH541
AHOH655
ALYS63
AGLU86
AGLU87
AGLY178
ALEU179

site_idAC3
Number of Residues7
Detailsbinding site for residue EDO A 403
ChainResidue
ALEU44
ATYR45
AASN277
AHOH509
AHOH548
AHOH612
AHOH641

site_idAC4
Number of Residues4
Detailsbinding site for residue CL A 404
ChainResidue
AGLN96
ASER129
ATYR171
PDG10

site_idAC5
Number of Residues6
Detailsbinding site for residue EDO B 401
ChainResidue
BASP189
BPHE192
BGLY239
BPHE240
BHOH534
BHOH618

Functional Information from PROSITE/UniProt
site_idPS00727
Number of Residues17
DetailsAP_NUCLEASE_F1_2 AP endonucleases family 1 signature 2. DSFRHlypntpyaYTFW
ChainResidueDetails
AASP251-TRP267

site_idPS00728
Number of Residues12
DetailsAP_NUCLEASE_F1_3 AP endonucleases family 1 signature 3. NvGwRLDYfLlS
ChainResidueDetails
AASN277-SER288

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: ACT_SITE => ECO:0000269|PubMed:15380100
ChainResidueDetails
ATYR171
BTYR171

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton donor/acceptor => ECO:0000269|PubMed:9351835, ECO:0007744|PDB:1BIX
ChainResidueDetails
AASN210
BASN210

site_idSWS_FT_FI3
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00764
ChainResidueDetails
AHIS309
BHIS309

site_idSWS_FT_FI4
Number of Residues12
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00764
ChainResidueDetails
AASN210
AASN212
AASP308
AHIS309
BASN68
BGLN96
BASN210
BASN212
BASP308
BHIS309
AGLN96
AASN68

site_idSWS_FT_FI5
Number of Residues2
DetailsSITE: Cleavage; by granzyme A
ChainResidueDetails
BLYS31
ALYS31

site_idSWS_FT_FI6
Number of Residues2
DetailsSITE: Transition state stabilizer => ECO:0000269|PubMed:8932375
ChainResidueDetails
BASN212
AASN212

site_idSWS_FT_FI7
Number of Residues2
DetailsSITE: Important for catalytic activity => ECO:0000269|PubMed:21762700, ECO:0000269|PubMed:9804799
ChainResidueDetails
BASP283
AASP283

site_idSWS_FT_FI8
Number of Residues2
DetailsSITE: Interaction with DNA substrate
ChainResidueDetails
AHIS309
BHIS309

site_idSWS_FT_FI9
Number of Residues4
DetailsMOD_RES: N6-acetyllysine; by EP300 => ECO:0000269|PubMed:14633989
ChainResidueDetails
ALYS7
BLYS6
BLYS7
ALYS6

site_idSWS_FT_FI10
Number of Residues8
DetailsMOD_RES: N6-acetyllysine => ECO:0000269|PubMed:20699270
ChainResidueDetails
ALYS32
ALYS35
BLYS27
BLYS31
BLYS32
BLYS35
ALYS27
ALYS31

site_idSWS_FT_FI11
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER54
BSER54

site_idSWS_FT_FI12
Number of Residues4
DetailsMOD_RES: S-nitrosocysteine; alternate => ECO:0000269|PubMed:17403694
ChainResidueDetails
BCYS65
BCYS93
ACYS65
ACYS93

site_idSWS_FT_FI13
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
ALYS197
BLYS197

site_idSWS_FT_FI14
Number of Residues2
DetailsMOD_RES: Phosphothreonine; by CDK5 => ECO:0000250|UniProtKB:P28352
ChainResidueDetails
ATHR233
BTHR233

site_idSWS_FT_FI15
Number of Residues2
DetailsMOD_RES: S-nitrosocysteine => ECO:0000269|PubMed:17403694
ChainResidueDetails
ACYS310
BCYS310

Catalytic Information from CSA
site_idMCSA1
Number of Residues8
DetailsM-CSA 510
ChainResidueDetails
AASP70metal ligand
AGLN96metal ligand
ATYR171electrostatic stabiliser, metal ligand
AASN210increase nucleophilicity, metal ligand, proton acceptor
AASN212
AASP283electrostatic stabiliser
AASP308metal ligand
AHIS309electrostatic stabiliser, metal ligand

site_idMCSA2
Number of Residues8
DetailsM-CSA 510
ChainResidueDetails
BASP70metal ligand
BGLN96metal ligand
BTYR171electrostatic stabiliser, metal ligand
BASN210increase nucleophilicity, metal ligand, proton acceptor
BASN212
BASP283electrostatic stabiliser
BASP308metal ligand
BHIS309electrostatic stabiliser, metal ligand

221051

PDB entries from 2024-06-12

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