2LE0

PARP BRCT Domain

> Summary

Summary for 2LE0

DescriptorPoly [ADP-ribose] polymerase 1 (E.C.2.4.2.30)
Functional Keywordstransferase
Biological sourceRattus norvegicus (rat)
Cellular locationNucleus (By similarity) P27008
Total number of polymer chains1
Total molecular weight11672.69
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
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 1polymer10611672.71
UniProt (P27008)
Pfam (PF00533)
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 weight11672.7
Non-Polymers*Number of molecules0
Total molecular weight0.0
All*Total molecular weight11672.7
*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
A0005667cellular_componenttranscription factor complex
A0003677molecular_functionDNA binding
A0003910molecular_functionDNA ligase (ATP) activity
A0019899molecular_functionenzyme binding
A0030331molecular_functionestrogen receptor binding
A0042826molecular_functionhistone deacetylase binding
A0051287molecular_functionNAD binding
A0003950molecular_functionNAD+ ADP-ribosyltransferase activity
A0044822molecular_functionpoly(A) RNA binding
A0070412molecular_functionR-SMAD binding
A0046332molecular_functionSMAD binding
A0016763molecular_functiontransferase activity, transferring pentosyl groups
A0008270molecular_functionzinc ion binding
A1904646biological_processcellular response to beta-amyloid
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
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
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
A0006351biological_processtranscription, DNA-templated
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

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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_FI11
ChainResidueDetails
ANA*

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Catalytic Information from CSA

site_idNumber of ResiduesDetails
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Catalytic Information from CATRES

site_idNumber of ResiduesDetails

> Sequence Neighbor

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