Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

6W4I

APE1 Y269A product complex with abasic DNA

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 Residues6
Detailsbinding site for residue MN A 401
ChainResidue
AGLU96
AHOH513
AHOH520
AHOH555
D3DR1
PDC10

site_idAC2
Number of Residues6
Detailsbinding site for residue MN B 401
ChainResidue
BHOH533
C3DR1
EDC10
BGLU96
BHOH526
BHOH527

site_idAC3
Number of Residues21
Detailsbinding site for Di-nucleotide 3DR C 1 and DC C 2
ChainResidue
BASN68
BGLU96
BTYR171
BASN174
BARG177
BASP210
BASN212
BASN226
BASN229
BALA230
BPHE266
BLEU282
BHIS309
BMN401
BHOH526
CDG3
CHOH101
CHOH105
EDC10
FDC9
FDG10

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
BTYR171
ATYR171

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton donor/acceptor => ECO:0000269|PubMed:9351835, ECO:0007744|PDB:1BIX
ChainResidueDetails
BASP210
AASP210

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

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

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

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

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

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

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

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

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

220472

PDB entries from 2024-05-29

PDB statisticsPDBj update infoContact PDBjnumon