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Open data
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Basic information
Entry | Database: PDB / ID: 1h8c | ||||||
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Title | UBX domain from human faf1 | ||||||
![]() | FAS-ASSOCIATED FACTOR 1 | ||||||
![]() | APOPTOSIS / FAF1 UBX DOMAIN UBIQUITIN-LIKE | ||||||
Function / homology | ![]() ooplasm / positive regulation of extrinsic apoptotic signaling pathway via death domain receptors / CD95 death-inducing signaling complex / protein kinase regulator activity / VCP-NPL4-UFD1 AAA ATPase complex / regulation of protein catabolic process / NF-kappaB binding / regulation of cell adhesion / ERAD pathway / heat shock protein binding ...ooplasm / positive regulation of extrinsic apoptotic signaling pathway via death domain receptors / CD95 death-inducing signaling complex / protein kinase regulator activity / VCP-NPL4-UFD1 AAA ATPase complex / regulation of protein catabolic process / NF-kappaB binding / regulation of cell adhesion / ERAD pathway / heat shock protein binding / ubiquitin binding / positive regulation of DNA replication / positive regulation of protein-containing complex assembly / positive regulation of protein catabolic process / nuclear envelope / proteasome-mediated ubiquitin-dependent protein catabolic process / positive regulation of apoptotic process / protein domain specific binding / apoptotic process / ubiquitin protein ligase binding / protein kinase binding / perinuclear region of cytoplasm / endoplasmic reticulum / nucleoplasm / nucleus / cytosol Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | SOLUTION NMR | ||||||
![]() | Bycroft, M.M. | ||||||
![]() | ![]() Title: The Ubx Domain: A Widespread Ubiquitin-Like Module Authors: Buchberger, A. / Howard, M.J. / Proctor, M. / Bycroft, M.M. #1: Journal: Biochem.Biophys.Res.Commun. / Year: 1999 Title: Identification and Characterization of Human Fas Associated Factor 1, Hfaf1 Authors: Ryu, S.W. / Chae, S.K. / Lee, K.J. / Kim, E. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 534.9 KB | Display | ![]() |
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PDB format | ![]() | 445.4 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 344.3 KB | Display | ![]() |
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Full document | ![]() | 522.1 KB | Display | |
Data in XML | ![]() | 75.5 KB | Display | |
Data in CIF | ![]() | 100.7 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: 9600.015 Da / Num. of mol.: 1 / Fragment: UBX DOMAIN Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR |
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Sample preparation
Sample conditions | pH: 5.8 / Temperature: 310 K |
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Crystal grow | *PLUS Method: other / Details: NMR |
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Processing
NMR software | Name: ![]() |
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NMR ensemble | Conformer selection criteria: LOWEST VIOLATIONS / Conformers calculated total number: 100 / Conformers submitted total number: 20 |