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Open data
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Basic information
Entry | Database: PDB / ID: 6a3z | ||||||
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Title | Zinc finger domain from the HRD1 Protein | ||||||
![]() | E3 ubiquitin-protein ligase synoviolin | ||||||
![]() | METAL BINDING PROTEIN / HRD1 | ||||||
Function / homology | ![]() Hrd1p ubiquitin ligase complex / endoplasmic reticulum mannose trimming / Hrd1p ubiquitin ligase ERAD-L complex / endoplasmic reticulum quality control compartment / immature B cell differentiation / XBP1(S) activates chaperone genes / Derlin-1 retrotranslocation complex / retrograde protein transport, ER to cytosol / ubiquitin-specific protease binding / smooth endoplasmic reticulum ...Hrd1p ubiquitin ligase complex / endoplasmic reticulum mannose trimming / Hrd1p ubiquitin ligase ERAD-L complex / endoplasmic reticulum quality control compartment / immature B cell differentiation / XBP1(S) activates chaperone genes / Derlin-1 retrotranslocation complex / retrograde protein transport, ER to cytosol / ubiquitin-specific protease binding / smooth endoplasmic reticulum / protein K48-linked ubiquitination / negative regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway / ERAD pathway / ER Quality Control Compartment (ERQC) / endomembrane system / Hh mutants are degraded by ERAD / Hedgehog ligand biogenesis / RING-type E3 ubiquitin transferase / ubiquitin protein ligase activity / unfolded protein binding / protein-folding chaperone binding / ATPase binding / ubiquitin-dependent protein catabolic process / proteasome-mediated ubiquitin-dependent protein catabolic process / protein stabilization / protein ubiquitination / endoplasmic reticulum membrane / endoplasmic reticulum / zinc ion binding / nucleoplasm / membrane Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | SOLUTION NMR / torsion angle dynamics | ||||||
![]() | Miyamoto, K. | ||||||
![]() | ![]() Title: The structure of the zinc finger from the HRD1 protein Authors: Miyamoto, K. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 346.1 KB | Display | ![]() |
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PDB format | ![]() | 288.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Similar structure data | |
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Other databases |
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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: 6520.612 Da / Num. of mol.: 1 / Fragment: Zinc finger domain / Source method: obtained synthetically / Source: (synth.) ![]() References: UniProt: Q86TM6, RING-type E3 ubiquitin transferase |
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#2: Chemical |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR |
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NMR experiment | Sample state: isotropic / Type: NOESY |
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Sample preparation
Details | Type: solution / Contents: 1 mM U 13C; 15N hrd1, 90% H2O/10% D2O / Label: 15N 13C / Solvent system: 90% H2O/10% D2O |
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Sample | Conc.: 1 mM / Component: hrd1 / Isotopic labeling: U 13C; 15N |
Sample conditions | Ionic strength: 20 mM / Label: conditions_1 / pH: 6.8 / Pressure: 1 atm / Temperature: 298 K |
-NMR measurement
NMR spectrometer | Type: Bruker AVANCE / Manufacturer: Bruker / Model: AVANCE / Field strength: 800 MHz |
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Processing
NMR software |
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Refinement | Method: torsion angle dynamics / Software ordinal: 1 | ||||||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 100 / Conformers submitted total number: 20 |