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- PDB-1hv2: SOLUTION STRUCTURE OF YEAST ELONGIN C IN COMPLEX WITH A VON HIPPE... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1hv2 | ||||||
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Title | SOLUTION STRUCTURE OF YEAST ELONGIN C IN COMPLEX WITH A VON HIPPEL-LINDAU PEPTIDE | ||||||
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![]() | SIGNALING PROTEIN / protein-peptide complex | ||||||
Function / homology | ![]() regulation of catecholamine metabolic process / homeostasis of number of retina cells / : / negative regulation of hypoxia-inducible factor-1alpha signaling pathway / regulation of protein localization => GO:0032880 / nucleotide-excision repair factor 4 complex / pancreatic A cell differentiation / SUMOylation of ubiquitinylation proteins / type B pancreatic cell differentiation / regulation of thymocyte apoptotic process ...regulation of catecholamine metabolic process / homeostasis of number of retina cells / : / negative regulation of hypoxia-inducible factor-1alpha signaling pathway / regulation of protein localization => GO:0032880 / nucleotide-excision repair factor 4 complex / pancreatic A cell differentiation / SUMOylation of ubiquitinylation proteins / type B pancreatic cell differentiation / regulation of thymocyte apoptotic process / ciliary body morphogenesis / iris morphogenesis / negative regulation of endothelial cell differentiation / melanin metabolic process / eye pigmentation / Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha / global genome nucleotide-excision repair / regulation of protein catabolic process at postsynapse, modulating synaptic transmission / blood vessel endothelial cell migration / Neddylation / camera-type eye morphogenesis / Antigen processing: Ubiquitination & Proteasome degradation / negative regulation of receptor signaling pathway via JAK-STAT / regulation of apoptotic signaling pathway / elongin complex / VCB complex / negative regulation of thymocyte apoptotic process / Cul2-RING ubiquitin ligase complex / Cul3-RING ubiquitin ligase complex / TP53 Regulates Transcription of DNA Repair Genes / Antigen processing: Ubiquitination & Proteasome degradation / transcription factor binding / ubiquitin-like ligase-substrate adaptor activity / proteasomal protein catabolic process / response to UV / extracellular matrix organization / positive regulation of epithelial cell proliferation / nucleotide-excision repair / protein catabolic process / neuron differentiation / cilium / protein transport / protein-macromolecule adaptor activity / ubiquitin-dependent protein catabolic process / postsynapse / regulation of gene expression / angiogenesis / response to ethanol / response to hypoxia / protein ubiquitination / negative regulation of cell population proliferation / negative regulation of gene expression / glutamatergic synapse / protein-containing complex binding / regulation of DNA-templated transcription / nucleolus / positive regulation of DNA-templated transcription / enzyme binding / negative regulation of transcription by RNA polymerase II / mitochondrion / nucleoplasm / membrane / nucleus / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | SOLUTION NMR / distance geometry, simulating annealing | ||||||
![]() | Botuyan, M.V. / Mer, G. / Yi, G.-S. / Koth, C.M. / Case, D.A. / Edwards, A.M. / Chazin, W.J. / Arrowsmith, C.H. | ||||||
![]() | ![]() Title: Solution structure and dynamics of yeast elongin C in complex with a von Hippel-Lindau peptide. Authors: Botuyan, M.V. / Mer, G. / Yi, G.S. / Koth, C.M. / Case, D.A. / Edwards, A.M. / Chazin, W.J. / Arrowsmith, C.H. #1: ![]() Title: Binding of Elongin A or a von Hippel-Lindau Peptide Stabilizes the Structure of Yeast Elongin C Authors: Botuyan, M.V. / Koth, C.M. / Mer, G. / Chakrabartty, A. / Conaway, J.W. / Conaway, R.C. / Edwards, A.M. / Arrowsmith, C.H. / Chazin, W.J. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 712.3 KB | Display | ![]() |
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PDB format | ![]() | 602.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 365 KB | Display | ![]() |
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Full document | ![]() | 539.5 KB | Display | |
Data in XML | ![]() | 31 KB | Display | |
Data in CIF | ![]() | 55.9 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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NMR ensembles |
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Components
#1: Protein | Mass: 11338.760 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Production host: ![]() ![]() |
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#2: Protein/peptide | Mass: 1776.195 Da / Num. of mol.: 1 / Fragment: RESIDUES 157-171 / Source method: obtained synthetically / Details: This peptide was chemically synthesized / References: UniProt: P40338 |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||||||||||||||
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NMR experiment |
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NMR details | Text: The structure was determined using triple-resonance NMR spectroscopy |
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Sample preparation
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Sample conditions | pH: 7.5 / Pressure: ambient / Temperature: 303 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: distance geometry, simulating annealing / Software ordinal: 1 | ||||||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||||||
NMR ensemble | Conformer selection criteria: The submitted conformer models are the 20 structures with the lowest energy Conformers calculated total number: 100 / Conformers submitted total number: 20 |