2HTF

The solution structure of the BRCT domain from human polymerase reveals homology with the TdT BRCT domain

> Summary

Summary for 2HTF

DescriptorDNA polymerase mu (E.C.2.7.7.7)
Functional Keywordsbrct domain, alpha-beta-alpha sandwich, transferase
Biological sourceHomo sapiens (human)
Cellular locationNucleus (By similarity) Q9NP87
Total number of polymer chains1
Total molecular weight11420.11
Authors
DeRose, E.F.,Clarkson, M.W.,Gilmore, S.A.,Ramsden, D.A.,Mueller, G.A.,London, R.E.,Lee, A.L. (deposition date: 2006-07-25, release date: 2007-02-27, modification date: 2009-02-24)
Primary citation
DeRose, E.F.,Clarkson, M.W.,Gilmore, S.A.,Galban, C.J.,Tripathy, A.,Havener, J.M.,Mueller, G.A.,Ramsden, D.A.,London, R.E.,Lee, A.L.
Solution structure of polymerase mu's BRCT Domain reveals an element essential for its role in nonhomologous end joining.
Biochemistry, 46:12100-12110, 2007
PubMed: 17915942
DOI: 10.1021/bi7007728
MImport into Mendeley
Experimental method
SOLUTION NMR
NMR Information
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Structure validation

ClashscoreRamachandran outliersSidechain outliers123.4%8.2%MetricValuePercentile RanksWorseBetterPercentile relative to all structuresPercentile relative to all NMR structures

More Asymmetric unit images

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

> Structural details

Entity

Chain IDDescriptionTypeChain lengthFormula weightNumber of moleculesDB Name (Accession)Biological sourceDescriptive keywords
ADNA polymerase mupolymer10511420.11
UniProt (Q9NP87)
Homo sapiens (human)@PDBjPol Mu

Sequence viewer

Contents of the asymmetric unit

PolymersNumber of chains1
Total molecular weight11420.1
Non-Polymers*Number of molecules0
Total molecular weight0.0
All*Total molecular weight11420.1
*Water molecules are not included.

> Experimental details

Spectrometer

Experimental method:SOLUTION NMR

Spectrometer IDSpectrometer makerSpectrometer modelSpectrometer typeSpectrometer field strength
1VarianINOVA600
2VarianINOVA800

Experiment

experiment idconditions idsolution idExperiment type
1113D_13C-separated_NOESY
2113D_15N-separated_NOESY

NMR Sample

conditions idNMR sample pHNMR sample pressureNMR sample temperature
17.9ambient283

Conformers

Conformers Calculated Total Number100
Conformers Submitted Total Number11

> Functional details

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Functional Information from GO Data

ChainGOidnamespacecontents
A0005654cellular_componentnucleoplasm
A0003677molecular_functionDNA binding
A0003887molecular_functionDNA-directed DNA polymerase activity
A0046872molecular_functionmetal ion binding
A0030183biological_processB cell differentiation
A0071897biological_processDNA biosynthetic process
A0006310biological_processDNA recombination
A0006281biological_processDNA repair
A0006302biological_processdouble-strand break repair
A0006303biological_processdouble-strand break repair via nonhomologous end joining
A0016446biological_processsomatic hypermutation of immunoglobulin genes
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Functional Information from PDB Data

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

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Functional Information from PROSITE/UniProt

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Functional Information from SwissProt/UniProt

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Catalytic Information from CSA

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Catalytic Information from CATRES

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> Sequence Neighbor

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