Structure of PDB 1lwv Chain A Binding Site BS03

Receptor Information
>1lwv Chain A (length=314) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
GSEGHRTLASTPALWASIPCPRSELRLDLVLPSGQSFRWREQSPAHWSGV
LADQVWTLTQTEEQLHCTVYRSQASRPTPDELEAVRKYFQLDVTLAQLYH
HWGSVDSHFQEVAQKFQGVRLLRQDPIECLFSFICSSNNNIARITGMVER
LCQAFGPRLIQLDDVTYHGFPSLQALAGPEVEAHLRKLGLGYRARYVSAS
ARAILEEQGGLAWLQQLRESSYEEAHKALCILPGVGTKVADCICLMALDK
PQAVPVDVHMWHIAQRDYSWHPTTSQAKGPSPQTNKELGNFFRSLWGPYA
GWAQAVLFSADLRQ
Ligand information
Ligand IDANG
InChIInChI=1S/C5H6N6O/c6-4-8-1-2(9-4)10-5(7)11-3(1)12/h(H6,6,7,8,9,10,11,12)
InChIKeyWYDKPTZGVLTYPG-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.341NC1=Nc2[nH]c(N)nc2C(=O)N1
ACDLabs 10.04O=C1c2nc(nc2N=C(N1)N)N
OpenEye OEToolkits 1.5.0c12c([nH]c(n1)N)N=C(NC2=O)N
FormulaC5 H6 N6 O
Name8-AMINOGUANINE
ChEMBLCHEMBL8040
DrugBank
ZINCZINC000013514984
PDB chain1lwv Chain A Residue 328 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1lwv Product-Assisted Catalysis in Base Excision DNA Repair
Resolution2.3 Å
Binding residue
(original residue number in PDB)		G42 F144 K249 P266 D268 Q315 F319
Binding residue
(residue number reindexed from 1)		G34 F133 K238 P255 D257 Q304 F308
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) K249 D268
Catalytic site (residue number reindexed from 1) K238 D257
Enzyme Commision number 3.2.2.-
4.2.99.18: DNA-(apurinic or apyrimidinic site) lyase.
Gene Ontology
Molecular Function
GO:0000978 RNA polymerase II cis-regulatory region sequence-specific DNA binding
GO:0003677 DNA binding
GO:0003684 damaged DNA binding
GO:0003824 catalytic activity
GO:0004519 endonuclease activity
GO:0005515 protein binding
GO:0008017 microtubule binding
GO:0008534 oxidized purine nucleobase lesion DNA N-glycosylase activity
GO:0016798 hydrolase activity, acting on glycosyl bonds
GO:0016829 lyase activity
GO:0019104 DNA N-glycosylase activity
GO:0019899 enzyme binding
GO:0032357 oxidized purine DNA binding
GO:0034039 8-oxo-7,8-dihydroguanine DNA N-glycosylase activity
GO:0140078 class I DNA-(apurinic or apyrimidinic site) endonuclease activity
GO:0140097 catalytic activity, acting on DNA
Biological Process
GO:0006281 DNA repair
GO:0006284 base-excision repair
GO:0006285 base-excision repair, AP site formation
GO:0006289 nucleotide-excision repair
GO:0006355 regulation of DNA-templated transcription
GO:0006974 DNA damage response
GO:0006979 response to oxidative stress
GO:0009314 response to radiation
GO:0009410 response to xenobiotic stimulus
GO:0009416 response to light stimulus
GO:0032355 response to estradiol
GO:0034614 cellular response to reactive oxygen species
GO:0043066 negative regulation of apoptotic process
GO:0044029 positive regulation of gene expression via chromosomal CpG island demethylation
GO:0045007 depurination
GO:0045008 depyrimidination
GO:0045471 response to ethanol
GO:0045944 positive regulation of transcription by RNA polymerase II
GO:0051593 response to folic acid
GO:0071276 cellular response to cadmium ion
GO:1901291 negative regulation of double-strand break repair via single-strand annealing
Cellular Component
GO:0005634 nucleus
GO:0005654 nucleoplasm
GO:0005739 mitochondrion
GO:0005759 mitochondrial matrix
GO:0005829 cytosol
GO:0016363 nuclear matrix
GO:0016607 nuclear speck
GO:0032991 protein-containing complex

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1lwv, PDBe:1lwv, PDBj:1lwv
PDBsum1lwv
PubMed12592398
UniProtO15527|OGG1_HUMAN N-glycosylase/DNA lyase (Gene Name=OGG1)

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