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2O3H

Crystal structure of the human C65A Ape

Functional Information from GO Data
ChainGOidnamespacecontents
A0003677molecular_functionDNA binding
A0003824molecular_functioncatalytic activity
A0004518molecular_functionnuclease activity
A0004519molecular_functionendonuclease activity
A0006281biological_processDNA repair
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SM A 400
ChainResidue
AGLU216
AGLU217
AGLU242
AGLN245
AHOH506
AHOH589
AHOH646

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SM A 401
ChainResidue
AHOH559
AHOH593
AHOH676
AHOH703
AHOH789
AASP70
AGLU96

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE ACT A 500
ChainResidue
ALYS78
ALEU104
AALA106
AGLN109
AHOH652
AHOH697
AHOH784

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ACT A 501
ChainResidue
AASN272
AARG274
ASER275

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE ACT A 502
ChainResidue
AMET37
AALA38
ASER120
ATYR144
AASP152
AHOH523
AHOH530

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ACT A 503
ChainResidue
ASER56
ATYR128
ASER129
ATYR171

Functional Information from PROSITE/UniProt
site_idPS00726
Number of Residues10
DetailsAP_NUCLEASE_F1_1 AP endonucleases family 1 signature 1. PDILCLQETK
ChainResidueDetails
APRO89-LYS98

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 Residues29
DetailsRegion: {"description":"Mitochondrial targeting sequence (MTS)"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues16
DetailsMotif: {"description":"Nuclear export signal (NES)"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsActive site: {"evidences":[{"source":"PubMed","id":"15380100","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
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 Residues1
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00764","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00764","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues1
DetailsSite: {"description":"Transition state stabilizer","evidences":[{"source":"PubMed","id":"8932375","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues1
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 Residues1
DetailsSite: {"description":"Interaction with DNA substrate"}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues2
DetailsModified residue: {"description":"S-nitrosocysteine; alternate","evidences":[{"source":"PubMed","id":"17403694","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI13
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine; by CDK5","evidences":[{"source":"UniProtKB","id":"P28352","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI14
Number of Residues1
DetailsModified residue: {"description":"S-nitrosocysteine","evidences":[{"source":"PubMed","id":"17403694","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues5
DetailsAnnotated By Reference To The Literature 1ako
ChainResidueDetails
AASN212
AHIS309
AASN68
AASP283
AASP210

site_idMCSA1
Number of Residues8
DetailsM-CSA 510
ChainResidueDetails
AASP70metal ligand
AGLU96metal ligand
ATYR171electrostatic stabiliser, metal ligand
AASP210increase nucleophilicity, metal ligand, proton acceptor
AASN212
AASP283electrostatic stabiliser
AASP308metal ligand
AHIS309electrostatic stabiliser, metal ligand

244693

PDB entries from 2025-11-12

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