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- PDB-1k0p: NMR Structures of the Zinc Finger Domain of Human DNA Polymerase-alpha -
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Open data
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Basic information
Entry | Database: PDB / ID: 1k0p | ||||||
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Title | NMR Structures of the Zinc Finger Domain of Human DNA Polymerase-alpha | ||||||
![]() | DNA polymerase alpha catalytic subunit | ||||||
![]() | TRANSFERASE / zinc finger protein / DNA binding domain / polymerase-alpha | ||||||
Function / homology | ![]() DNA replication initiation / Telomere C-strand synthesis initiation / Inhibition of replication initiation of damaged DNA by RB1/E2F1 / alpha DNA polymerase:primase complex / Polymerase switching / regulation of type I interferon production / Processive synthesis on the lagging strand / Removal of the Flap Intermediate / Polymerase switching on the C-strand of the telomere / lagging strand elongation ...DNA replication initiation / Telomere C-strand synthesis initiation / Inhibition of replication initiation of damaged DNA by RB1/E2F1 / alpha DNA polymerase:primase complex / Polymerase switching / regulation of type I interferon production / Processive synthesis on the lagging strand / Removal of the Flap Intermediate / Polymerase switching on the C-strand of the telomere / lagging strand elongation / DNA replication, synthesis of primer / mitotic DNA replication initiation / DNA strand elongation involved in DNA replication / DNA synthesis involved in DNA repair / G1/S-Specific Transcription / leading strand elongation / DNA replication origin binding / Activation of the pre-replicative complex / DNA replication initiation / Defective pyroptosis / nuclear matrix / double-strand break repair via nonhomologous end joining / nuclear envelope / single-stranded DNA binding / DNA replication / DNA-directed DNA polymerase / DNA-directed DNA polymerase activity / DNA repair / nucleotide binding / chromatin binding / chromatin / nucleolus / protein kinase binding / DNA binding / zinc ion binding / nucleoplasm / nucleus / cytosol Similarity search - Function | ||||||
Method | SOLUTION NMR / simulated annealing | ||||||
![]() | Yang, W.W. / Evanics, F. / Basu, S. / Bose, R.N. | ||||||
![]() | ![]() Title: Nuclear magnetic resonance structures of the zinc finger domain of human DNA polymerase-alpha. Authors: Evanics, F. / Maurmann, L. / Yang, W.W. / Bose, R.N. #1: ![]() Title: Unwinding of DNA polymerases by the antitumor drug, cis-diamminedichloroplatinum(II) Authors: Volckova, E. / Evanics, F. / Yang, W.W. / Bose, R.N. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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PDBx/mmCIF format | ![]() | 151 KB | Display | ![]() |
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PDB format | ![]() | 122.2 KB | Display | ![]() |
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-Validation report
Summary document | ![]() | 352.5 KB | Display | ![]() |
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Full document | ![]() | 458.8 KB | Display | |
Data in XML | ![]() | 26.1 KB | Display | |
Data in CIF | ![]() | 37.4 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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Links
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Assembly
Deposited unit | ![]()
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1 |
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NMR ensembles |
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Components
#1: Protein/peptide | Mass: 3536.204 Da / Num. of mol.: 1 / Fragment: zinc finger domain (residues 1347-1377) / Source method: obtained synthetically Details: The peptide was chemically synthesized. The sequence occurs naturally in Homo sapiens (human). References: UniProt: P09884, DNA-directed DNA polymerase |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||
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NMR experiment |
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NMR details | Text: This structure was determined using standard 2D homonuclear techniques. The NOESY mixing time was 200 ms. |
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Sample preparation
Details | Contents: 3mM Zinc Finger Domain; 3.6mM Zn(II)nitrate / Solvent system: 90% H2O/10% D2O |
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Sample conditions | pH: 6.8 / Pressure: ambient / Temperature: 296 K |
Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M | |||||||||||||||
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Radiation wavelength | Relative weight: 1 | |||||||||||||||
NMR spectrometer |
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Processing
NMR software |
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Refinement | Method: simulated annealing / Software ordinal: 1 Details: The structures are based on 206 NOE-derived distance constraints and 4 dihedral angle restraints | ||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with lowest RMSD compared to the average structure Conformers calculated total number: 75 / Conformers submitted total number: 15 |