|Entry||Database: PDB / ID: 1y02|
|Title||Crystal Structure of a FYVE-type domain from caspase regulator CARP2|
|Components||FYVE-RING finger protein SAKURA|
|Keywords||METAL BINDING PROTEIN / CARP2 / FYVE / zinc-binding module / phosphoinositide binding / caspase regulation|
|Function / homology|
Function and homology information
negative regulation of cysteine-type endopeptidase activity involved in execution phase of apoptosis / regulation of fibroblast migration / regulation of TOR signaling / negative regulation of signal transduction by p53 class mediator / protein K48-linked ubiquitination / negative regulation of tumor necrosis factor-mediated signaling pathway / negative regulation of extrinsic apoptotic signaling pathway via death domain receptors / regulation of signal transduction by p53 class mediator / RING-type E3 ubiquitin transferase / ubiquitin protein ligase activity ...negative regulation of cysteine-type endopeptidase activity involved in execution phase of apoptosis / regulation of fibroblast migration / regulation of TOR signaling / negative regulation of signal transduction by p53 class mediator / protein K48-linked ubiquitination / negative regulation of tumor necrosis factor-mediated signaling pathway / negative regulation of extrinsic apoptotic signaling pathway via death domain receptors / regulation of signal transduction by p53 class mediator / RING-type E3 ubiquitin transferase / ubiquitin protein ligase activity / recycling endosome membrane / Regulation of TP53 Degradation / p53 binding / ubiquitin-dependent protein catabolic process / proteasome-mediated ubiquitin-dependent protein catabolic process / protease binding / endosome membrane / ubiquitin protein ligase binding / apoptotic process / protein kinase binding / membrane / nucleoplasm / metal ion binding / plasma membrane / cytosol / cytoplasm
Similarity search - Function
Transcription Termination Factor Rho, Rna-binding Domain; Chain A, Domain 1 - #140 / Transcription Termination Factor Rho, Rna-binding Domain; Chain A, Domain 1 / SAP domain superfamily / Ring finger / Zinc finger RING-type profile. / Zinc finger, RING-type / Zinc finger, FYVE/PHD-type / Zinc finger, RING/FYVE/PHD-type / Orthogonal Bundle / Mainly Alpha
Similarity search - Domain/homology
E3 ubiquitin-protein ligase rififylin
Similarity search - Component
|Biological species||Homo sapiens (human)|
|Method||X-RAY DIFFRACTION / SYNCHROTRON / MAD / Resolution: 1.8 Å|
|Authors||Tibbetts, M.D. / Gu, L. / Shiozaki, E.N. / Shi, Y.|
|Citation||Journal: STRUCTURE / Year: 2004|
Title: Crystal structure of a FYVE-type zinc finger domain from the caspase regulator CARP2.
Authors: Tibbetts, M.D. / Shiozaki, E.N. / Gu, L. / McDonald, E.R. / El-Deiry, W.S. / Shi, Y.
|Structure viewer||Molecule: |
Downloads & links
A: FYVE-RING finger protein SAKURA
|#1: Protein|| |
Mass: 13593.707 Da / Num. of mol.: 1 / Fragment: CARP2 fragment (residues 26-145)
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Production host: Escherichia coli (E. coli) / References: UniProt: Q8WZ73
|#2: Chemical||#3: Water|| ChemComp-HOH / |
|Experiment||Method: X-RAY DIFFRACTION / Number of used crystals: 1|
|Crystal||Density Matthews: 2.4 Å3/Da / Density % sol: 50 %|
|Crystal grow||Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 7.5 |
Details: HEPES, Na, K, Tartrate, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K
|Diffraction||Mean temperature: 100 K|
|Diffraction source||Source: SYNCHROTRON / Site: NSLS / Beamline: X25 / Wavelength: 1.28 Å|
|Detector||Type: ADSC QUANTUM 4 / Detector: CCD / Date: Feb 20, 2004|
|Radiation||Monochromator: Ni MIRROR + Ni FILTER / Protocol: MAD / Monochromatic (M) / Laue (L): M / Scattering type: x-ray|
|Radiation wavelength||Wavelength: 1.28 Å / Relative weight: 1|
|Reflection||Resolution: 1.7→99 Å / Num. all: 12581 / Num. obs: 12241 / % possible obs: 97.3 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 6 % / Rsym value: 0.071|
|Reflection shell||Resolution: 1.7→1.76 Å / Rsym value: 0.446 / % possible all: 85.2|
|Refinement||Method to determine structure: MAD / Resolution: 1.8→20 Å / σ(F): 0 / Stereochemistry target values: Engh & Huber|
|Refinement step||Cycle: LAST / Resolution: 1.8→20 Å|
|Refine LS restraints|
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