2LE0

PARP BRCT Domain

> Summary

Summary for 2LE0

DescriptorPoly [ADP-ribose] polymerase 1 (1 entity in total)
Functional Keywordstransferase
Biological sourceRattus norvegicus (rat)
Cellular locationNucleus (By similarity) P27008
Total number of polymer chains1
Total molecular weight11672.6
Authors
Mueller, G.,Loeffler, P.,Cuneo, M.,Derose, E.,London, R. (deposition date: 2011-06-03, release date: 2011-10-19)
Primary citation
Loeffler, P.A.,Cuneo, M.J.,Mueller, G.A.,Derose, E.F.,Gabel, S.A.,London, R.E.
Structural studies of the PARP-1 BRCT domain.
Bmc Struct.Biol., 11:37-37, 2011
PubMed: 21967661 (PDB entries with the same primary citation)
DOI: 10.1186/1472-6807-11-37
MImport into Mendeley
Experimental method
SOLUTION NMR
NMR Information
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Structure validation

ClashscoreRamachandran outliersSidechain outliers144.9%4.3%MetricValuePercentile RanksWorseBetterPercentile relative to all structuresPercentile relative to all NMR structures

More Asymmetric unit images

Molmil generated image of 2le0
no rotation
Molmil generated image of 2le0
rotated about x axis by 90°
Molmil generated image of 2le0
rotated about y axis by 90°

> Structural details

Entity

Chain IDDescriptionTypeChain lengthFormula weightNumber of moleculesDB Name (Accession)Biological sourceDescriptive keywords
APoly [ADP-ribose] polymerase 1polymer10611672.61
UniProt (P27008)
Rattus norvegicus (rat)@PDBjPARP-1, NAD(+) ADP-ribosyltransferase 1, ADPRT 1, Poly[ADP-ribose] synthase 1

Sequence viewer

Contents of the asymmetric unit

PolymersNumber of chains1
Total molecular weight11672.6
Non-Polymers*Number of molecules0
Total molecular weight0.0
All*Total molecular weight11672.6
*Water molecules are not included.

> Experimental details

Spectrometer

Experimental method:SOLUTION NMR

Spectrometer IDSpectrometer makerSpectrometer modelSpectrometer typeSpectrometer field strength
1VarianINOVAVarian INOVA600

Experiment

experiment idconditions idsolution idExperiment type
1112D 1H-15N HSQC
2113D HNCA
3113D HNCACB
4113D CBCA(CO)NH
5113D C(CO)NH
6113D H(CCO)NH
711(HB)CB(CGCD)HD
811(HB)CB(CGCDCE)HE
9113D 1H-15N NOESY
10113D 1H-13C NOESY

NMR Sample

conditions idNMR sample pHNMR sample pressureNMR sample temperature
17.5ambient298

Conformers

Conformers Calculated Total Number100
Conformers Submitted Total Number10

> Functional details

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Functional Information from GO Data

ChainGOidnamespacecontents
A0005737cellular_componentcytoplasm
A0016020cellular_componentmembrane
A0005739cellular_componentmitochondrion
A0000784cellular_componentnuclear chromosome, telomeric region
A0005635cellular_componentnuclear envelope
A0005730cellular_componentnucleolus
A0005634cellular_componentnucleus
A0032993cellular_componentprotein-DNA complex
A0005667cellular_componenttranscription factor complex
A0003910molecular_functionDNA ligase (ATP) activity
A0019899molecular_functionenzyme binding
A0030331molecular_functionestrogen receptor binding
A0042826molecular_functionhistone deacetylase binding
A0042802molecular_functionidentical protein binding
A0051287molecular_functionNAD binding
A0003950molecular_functionNAD+ ADP-ribosyltransferase activity
A1990404molecular_functionprotein ADP-ribosylase activity
A0019901molecular_functionprotein kinase binding
A0047485molecular_functionprotein N-terminus binding
A0070412molecular_functionR-SMAD binding
A0003723molecular_functionRNA binding
A0000977molecular_functionRNA polymerase II regulatory region sequence-specific DNA binding
A0046332molecular_functionSMAD binding
A0008134molecular_functiontranscription factor binding
A0001228molecular_functiontranscriptional activator activity, RNA polymerase II transcription regulatory region sequence-specific binding
A0016763molecular_functiontransferase activity, transferring pentosyl groups
A0008270molecular_functionzinc ion binding
A1990966biological_processATP generation from poly-ADP-D-ribose
A1904646biological_processcellular response to amyloid-beta
A0032869biological_processcellular response to insulin stimulus
A0034599biological_processcellular response to oxidative stress
A0071560biological_processcellular response to transforming growth factor beta stimulus
A0071294biological_processcellular response to zinc ion
A0042769biological_processDNA damage response, detection of DNA damage
A0051103biological_processDNA ligation involved in DNA repair
A0006302biological_processdouble-strand break repair
A0006273biological_processlagging strand elongation
A0043504biological_processmitochondrial DNA repair
A2001170biological_processnegative regulation of ATP biosynthetic process
A0018312biological_processpeptidyl-serine ADP-ribosylation
A0010613biological_processpositive regulation of cardiac muscle hypertrophy
A0033148biological_processpositive regulation of intracellular estrogen receptor signaling pathway
A0051901biological_processpositive regulation of mitochondrial depolarization
A1904762biological_processpositive regulation of myofibroblast differentiation
A1901216biological_processpositive regulation of neuron death
A1900182biological_processpositive regulation of protein localization to nucleus
A0060391biological_processpositive regulation of SMAD protein import into nucleus
A0045944biological_processpositive regulation of transcription from RNA polymerase II promoter
A2000679biological_processpositive regulation of transcription regulatory region DNA binding
A0006471biological_processprotein ADP-ribosylation
A0016540biological_processprotein autoprocessing
A0070212biological_processprotein poly-ADP-ribosylation
A0050790biological_processregulation of catalytic activity
A0044030biological_processregulation of DNA methylation
A1903376biological_processregulation of oxidative stress-induced neuron intrinsic apoptotic signaling pathway
A0010990biological_processregulation of SMAD protein complex assembly
A1904044biological_processresponse to aldosterone
A0010332biological_processresponse to gamma radiation
A0023019biological_processsignal transduction involved in regulation of gene expression
A0007179biological_processtransforming growth factor beta receptor signaling pathway
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Functional Information from PDB Data

site_idNumber of ResiduesDetails
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Functional Information from PDB atom coordinates for the "HETATM" binding sites

site_idNumber of ResiduesDetails
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Functional Information from PROSITE/UniProt

site_idNumber of ResiduesDetails
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Functional Information from SwissProt/UniProt

site_idNumber of ResiduesDetails
SWS_FT_FI1372
ChainResidueDetails
ANA*

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Catalytic Information from CSA

site_idNumber of ResiduesDetails

> Sequence Neighbor

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