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5DFJ

Human APE1 E96Q/D210N mismatch substrate complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0003677molecular_functionDNA binding
A0003824molecular_functioncatalytic activity
A0004518molecular_functionnuclease activity
A0004519molecular_functionendonuclease activity
A0006281biological_processDNA repair
B0003677molecular_functionDNA binding
B0003824molecular_functioncatalytic activity
B0004518molecular_functionnuclease activity
B0004519molecular_functionendonuclease activity
B0006281biological_processDNA repair
Functional Information from PDB Data
site_idAC1
Number of Residues3
Detailsbinding site for residue CL A 401
ChainResidue
AGLN96
ASER129
ATYR171

site_idAC2
Number of Residues3
Detailsbinding site for residue CL A 402
ChainResidue
AGLU154
AARG156
ATRP188

site_idAC3
Number of Residues5
Detailsbinding site for residue CL A 403
ChainResidue
AHOH638
AHOH706
APHE253
AARG281
AASP283

site_idAC4
Number of Residues4
Detailsbinding site for residue CL A 404
ChainResidue
AHIS215
AASP251
AHOH583
AHOH800

site_idAC5
Number of Residues4
Detailsbinding site for residue CL A 405
ChainResidue
AASP47
ATYR257
ASER298
ALYS299

site_idAC6
Number of Residues5
Detailsbinding site for residue EDO A 406
ChainResidue
AASP189
APHE192
AGLY239
APHE240
AHOH541

site_idAC7
Number of Residues6
Detailsbinding site for residue EDO A 407
ChainResidue
ALEU44
ATYR45
AASN277
AHOH570
AHOH589
AHOH675

site_idAC8
Number of Residues3
Detailsbinding site for residue CL B 401
ChainResidue
AHOH702
BHIS116
BGLN117

site_idAC9
Number of Residues3
Detailsbinding site for residue CL B 402
ChainResidue
BGLY145
BARG156
BVAL157

site_idAD1
Number of Residues3
Detailsbinding site for residue CL V 101
ChainResidue
AMET271
VDG11
VDG12

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 Residues58
DetailsRegion: {"description":"Mitochondrial targeting sequence (MTS)"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues32
DetailsMotif: {"description":"Nuclear export signal (NES)"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsActive site: {"evidences":[{"source":"PubMed","id":"15380100","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsActive site: {"description":"Proton donor/acceptor","evidences":[{"source":"PubMed","id":"9351835","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1BIX","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00764","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues12
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00764","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues2
DetailsSite: {"description":"Transition state stabilizer","evidences":[{"source":"PubMed","id":"8932375","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues2
DetailsSite: {"description":"Important for catalytic activity","evidences":[{"source":"PubMed","id":"21762700","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9804799","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues2
DetailsSite: {"description":"Interaction with DNA substrate"}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues4
DetailsModified residue: {"description":"S-nitrosocysteine; alternate","evidences":[{"source":"PubMed","id":"17403694","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI13
Number of Residues2
DetailsModified residue: {"description":"Phosphothreonine; by CDK5","evidences":[{"source":"UniProtKB","id":"P28352","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI14
Number of Residues2
DetailsModified residue: {"description":"S-nitrosocysteine","evidences":[{"source":"PubMed","id":"17403694","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

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

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PDB entries from 2025-12-24

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