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Open data
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Basic information
Entry | Database: PDB / ID: 1w5h | ||||||
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Title | An anti-parallel four helix bundle. | ||||||
![]() | GENERAL CONTROL PROTEIN GCN4 | ||||||
![]() | FOUR HELIX BUNDLE / ANTIPARALLEL FOUR HELIX BUNDLE | ||||||
Function / homology | ![]() protein localization to nuclear periphery / FCERI mediated MAPK activation / Activation of the AP-1 family of transcription factors / response to amino acid starvation / mediator complex binding / negative regulation of ribosomal protein gene transcription by RNA polymerase II / positive regulation of cellular response to amino acid starvation / nitrogen catabolite activation of transcription from RNA polymerase II promoter / Oxidative Stress Induced Senescence / TFIID-class transcription factor complex binding ...protein localization to nuclear periphery / FCERI mediated MAPK activation / Activation of the AP-1 family of transcription factors / response to amino acid starvation / mediator complex binding / negative regulation of ribosomal protein gene transcription by RNA polymerase II / positive regulation of cellular response to amino acid starvation / nitrogen catabolite activation of transcription from RNA polymerase II promoter / Oxidative Stress Induced Senescence / TFIID-class transcription factor complex binding / positive regulation of transcription initiation by RNA polymerase II / positive regulation of RNA polymerase II transcription preinitiation complex assembly / amino acid biosynthetic process / cellular response to amino acid starvation / RNA polymerase II transcription regulator complex / : / DNA-binding transcription activator activity, RNA polymerase II-specific / RNA polymerase II-specific DNA-binding transcription factor binding / transcription regulator complex / sequence-specific DNA binding / DNA-binding transcription factor activity, RNA polymerase II-specific / regulation of cell cycle / intracellular signal transduction / RNA polymerase II cis-regulatory region sequence-specific DNA binding / DNA-binding transcription factor activity / chromatin binding / negative regulation of transcription by RNA polymerase II / positive regulation of transcription by RNA polymerase II / identical protein binding / nucleus Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Yadav, M.K. / Leman, L.J. / Stout, C.D. / Ghadiri, M.R. | ||||||
![]() | ![]() Title: Coiled Coils at the Edge of Configurational Heterogeneity. Structural Analyses of Parallel and Antiparallel Homotetrameric Coiled Coils Reveal Configurational Sensitivity to a Single Solvent- ...Title: Coiled Coils at the Edge of Configurational Heterogeneity. Structural Analyses of Parallel and Antiparallel Homotetrameric Coiled Coils Reveal Configurational Sensitivity to a Single Solvent-Exposed Amino Acid Substitution. Authors: Yadav, M.K. / Leman, L.J. / Price, D.J. / Brooks, C.L. / Stout, C.D. / Ghadiri, M.R. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 22.9 KB | Display | ![]() |
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PDB format | ![]() | 15.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 435.4 KB | Display | ![]() |
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Full document | ![]() | 438.9 KB | Display | |
Data in XML | ![]() | 5.2 KB | Display | |
Data in CIF | ![]() | 6 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1w5jC ![]() 1w5kC ![]() 1w5lC ![]() 2cceC ![]() 2ccfC ![]() 2ccnC C: citing same article ( |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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1 | ![]()
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Unit cell |
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Components
#1: Protein/peptide | Mass: 3995.802 Da / Num. of mol.: 2 / Mutation: YES / Source method: obtained synthetically Details: PEPTIDE IS CAPPED WITH PARA ACETAMIDO BENZOIC ACID. Source: (synth.) ![]() ![]() Compound details | CHAIN A, B ENGINEERED MUTATION TYR 265 HIS, GLU 268 CYS THE N-TERMINUS OF THIS PEPTIDE IS CAPPED ...CHAIN A, B ENGINEERED | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2 Å3/Da / Density % sol: 38.9 % |
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Crystal grow | Method: vapor diffusion, hanging drop / pH: 10.5 Details: HANGING DROP, 1UL OF 1MG/ML PEPTIDE IN WATER, 1UL 100MM CAPS, 30% PEG 400, PH 10.5. |
-Data collection
Diffraction | Mean temperature: 93 K |
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Diffraction source | Source: ![]() |
Detector | Date: Jun 26, 2004 |
Radiation | Monochromator: NI FILTER / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.2→35.41 Å / Num. obs: 3786 / % possible obs: 100 % / Observed criterion σ(I): 2 / Redundancy: 7.06 % / Rmerge(I) obs: 0.05 / Net I/σ(I): 17.2 |
Reflection shell | Resolution: 2.2→2.28 Å / Redundancy: 7.11 % / Rmerge(I) obs: 0.36 / Mean I/σ(I) obs: 4.7 / % possible all: 100 |
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Processing
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Refinement | Method to determine structure: ![]() Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. N TERMINUS IS CAPPED WITH ABA.
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: BABINET MODEL WITH MASK | ||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.5→35.41 Å
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LS refinement shell | Resolution: 2.5→2.57 Å / Total num. of bins used: 20 /
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