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

> Summary

Summary for 2HTF

DescriptorDNA polymerase mu (1 entity in total)
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
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, Last 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 (PDB entries with the same primary citation)
DOI: 10.1021/bi7007728
MImport into Mendeley
Experimental method
NMR Information

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


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


Experimental method:SOLUTION NMR

Spectrometer IDSpectrometer makerSpectrometer modelSpectrometer typeSpectrometer field strength


experiment idconditions idsolution idExperiment type

NMR Sample

conditions idNMR sample pHNMR sample pressureNMR sample temperature


Conformers Calculated Total Number100
Conformers Submitted Total Number11

> Functional details


Functional Information from GO Data

A0003677molecular_functionDNA binding
A0003887molecular_functionDNA-directed DNA polymerase activity
A0046872molecular_functionmetal ion binding
A0030183biological_processB cell differentiation
A0006310biological_processDNA recombination
A0006303biological_processdouble-strand break repair via nonhomologous end joining
A0016446biological_processsomatic hypermutation of immunoglobulin genes

Functional Information from PDB Data

site_idNumber of ResiduesDetails

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

site_idNumber of ResiduesDetails

Functional Information from PROSITE/UniProt

site_idNumber of ResiduesDetails

Functional Information from SwissProt/UniProt

site_idNumber of ResiduesDetails

Catalytic Information from CSA

site_idNumber of ResiduesDetails

> Sequence Neighbor

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