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5WN0

APE1 exonuclease substrate complex with a C/G match

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 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 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
AASP210
BASP210

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
AASN68
BASN212
BASP308
BHIS309
AGLU96
AASP210
AASN212
AASP308
AHIS309
BASN68
BGLU96
BASP210

site_idSWS_FT_FI5
Number of Residues2
DetailsSITE: Transition state stabilizer => ECO:0000269|PubMed:8932375
ChainResidueDetails
AASN212
BASN212

site_idSWS_FT_FI6
Number of Residues2
DetailsSITE: Important for catalytic activity => ECO:0000269|PubMed:21762700, ECO:0000269|PubMed:9804799
ChainResidueDetails
AASP283
BASP283

site_idSWS_FT_FI7
Number of Residues2
DetailsSITE: Interaction with DNA substrate
ChainResidueDetails
AHIS309
BHIS309

site_idSWS_FT_FI8
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER54
BSER54

site_idSWS_FT_FI9
Number of Residues4
DetailsMOD_RES: S-nitrosocysteine; alternate => ECO:0000269|PubMed:17403694
ChainResidueDetails
ACYS65
ACYS93
BCYS65
BCYS93

site_idSWS_FT_FI10
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
ALYS197
BLYS197

site_idSWS_FT_FI11
Number of Residues2
DetailsMOD_RES: Phosphothreonine; by CDK5 => ECO:0000250|UniProtKB:P28352
ChainResidueDetails
ATHR233
BTHR233

site_idSWS_FT_FI12
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
AGLU96metal ligand
ATYR171electrostatic stabiliser, metal ligand
AASP210increase 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
BGLU96metal ligand
BTYR171electrostatic stabiliser, metal ligand
BASP210increase nucleophilicity, metal ligand, proton acceptor
BASN212
BASP283electrostatic stabiliser
BASP308metal ligand
BHIS309electrostatic stabiliser, metal ligand

229380

PDB entries from 2024-12-25

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