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7LPH

APE1 Mn-bound product complex with abasic ribonucleotide DNA

Functional Information from GO Data
ChainGOidnamespacecontents
B0003677molecular_functionDNA binding
B0003824molecular_functioncatalytic activity
B0004518molecular_functionnuclease activity
B0004519molecular_functionendonuclease activity
B0006281biological_processDNA repair
D0003677molecular_functionDNA binding
D0003824molecular_functioncatalytic activity
D0004518molecular_functionnuclease activity
D0004519molecular_functionendonuclease activity
D0006281biological_processDNA repair
Functional Information from PROSITE/UniProt
site_idPS00726
Number of Residues10
DetailsAP_NUCLEASE_F1_1 AP endonucleases family 1 signature 1. PDILCLQETK
ChainResidueDetails
BPRO89-LYS98

site_idPS00727
Number of Residues17
DetailsAP_NUCLEASE_F1_2 AP endonucleases family 1 signature 2. DSFRHlypntpyaYTFW
ChainResidueDetails
BASP251-TRP267

site_idPS00728
Number of Residues12
DetailsAP_NUCLEASE_F1_3 AP endonucleases family 1 signature 3. NvGwRLDYfLlS
ChainResidueDetails
BASN277-SER288

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: ACT_SITE => ECO:0000269|PubMed:15380100
ChainResidueDetails
BTYR171
DTYR171

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton donor/acceptor => ECO:0000269|PubMed:9351835, ECO:0007744|PDB:1BIX
ChainResidueDetails
BASP210
DASP210

site_idSWS_FT_FI3
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00764
ChainResidueDetails
BHIS309
DHIS309

site_idSWS_FT_FI4
Number of Residues12
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00764
ChainResidueDetails
BASN68
DASN212
DASP308
DHIS309
BGLU96
BASP210
BASN212
BASP308
BHIS309
DASN68
DGLU96
DASP210

site_idSWS_FT_FI5
Number of Residues2
DetailsSITE: Transition state stabilizer => ECO:0000269|PubMed:8932375
ChainResidueDetails
BASN212
DASN212

site_idSWS_FT_FI6
Number of Residues2
DetailsSITE: Important for catalytic activity => ECO:0000269|PubMed:21762700, ECO:0000269|PubMed:9804799
ChainResidueDetails
BASP283
DASP283

site_idSWS_FT_FI7
Number of Residues2
DetailsSITE: Interaction with DNA substrate
ChainResidueDetails
BHIS309
DHIS309

site_idSWS_FT_FI8
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
BSER54
DSER54

site_idSWS_FT_FI9
Number of Residues4
DetailsMOD_RES: S-nitrosocysteine; alternate => ECO:0000269|PubMed:17403694
ChainResidueDetails
BCYS65
BCYS93
DCYS65
DCYS93

site_idSWS_FT_FI10
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
BLYS197
DLYS197

site_idSWS_FT_FI11
Number of Residues2
DetailsMOD_RES: Phosphothreonine; by CDK5 => ECO:0000250|UniProtKB:P28352
ChainResidueDetails
BTHR233
DTHR233

site_idSWS_FT_FI12
Number of Residues2
DetailsMOD_RES: S-nitrosocysteine => ECO:0000269|PubMed:17403694
ChainResidueDetails
BCYS310
DCYS310

Catalytic Information from CSA
site_idMCSA1
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

site_idMCSA2
Number of Residues8
DetailsM-CSA 510
ChainResidueDetails
DASP70metal ligand
DGLU96metal ligand
DTYR171electrostatic stabiliser, metal ligand
DASP210increase nucleophilicity, metal ligand, proton acceptor
DASN212
DASP283electrostatic stabiliser
DASP308metal ligand
DHIS309electrostatic stabiliser, metal ligand

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PDB entries from 2024-11-13

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