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5WN2

APE1 exonuclease substrate complex with phosphoglycolate

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 Residues2
Detailsbinding site for residue NA A 401
ChainResidue
ALYS125
ATYR128

site_idAC2
Number of Residues5
Detailsbinding site for residue EDO B 401
ChainResidue
BGLN137
BALA138
BLEU140
BPHE162
BASP163

site_idAC3
Number of Residues2
Detailsbinding site for residue EDO B 402
ChainResidue
BGLY198
BARG202

site_idAC4
Number of Residues4
Detailsbinding site for residue EDO B 403
ChainResidue
BHIS215
BGLU216
BARG237
BGLY241

site_idAC5
Number of Residues4
Detailsbinding site for residue EDO C 101
ChainResidue
BMET270
CDC11
DDG1
EDG1

site_idAC6
Number of Residues11
Detailsbinding site for residue PGA D 101
ChainResidue
AGLN96
ATYR171
AASN174
AASN210
AASN212
APHE266
ALEU282
AHIS309
AHOH507
DDG9
DHOH202

site_idAC7
Number of Residues6
Detailsbinding site for residue CA E 101
ChainResidue
BTYR171
BASN174
BHOH501
BHOH579
EDC21
EHOH209

site_idAC8
Number of Residues1
Detailsbinding site for residue CA E 102
ChainResidue
BALA230

site_idAC9
Number of Residues3
Detailsbinding site for residue NA E 103
ChainResidue
BMET270
EDG1
EDG2

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

238582

PDB entries from 2025-07-09

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