|Entry||Database: PDB / ID: 2yrc|
|Title||Solution structure of the zf-Sec23_Sec24 from human Sec23A|
|Components||Protein transport protein Sec23AProtein targeting|
|Keywords||PROTEIN TRANSPORT / zinc binding / COPII / coat protein complex-II / endoplasmic reticulum / Golgi / Structural Genomics / NPPSFA / National Project on Protein Structural and Functional Analyses / RIKEN Structural Genomics/Proteomics Initiative / RSGI|
|Function / homology|
Function and homology information
COPII-coated vesicle cargo loading / COPII vesicle coat / Regulation of cholesterol biosynthesis by SREBP (SREBF) / Cargo concentration in the ER / COPII-mediated vesicle transport / extrinsic component of membrane / endoplasmic reticulum exit site / MHC class II antigen presentation / GTPase activator activity / protein localization to plasma membrane ...COPII-coated vesicle cargo loading / COPII vesicle coat / Regulation of cholesterol biosynthesis by SREBP (SREBF) / Cargo concentration in the ER / COPII-mediated vesicle transport / extrinsic component of membrane / endoplasmic reticulum exit site / MHC class II antigen presentation / GTPase activator activity / protein localization to plasma membrane / intracellular protein transport / Antigen Presentation: Folding, assembly and peptide loading of class I MHC / ER to Golgi transport vesicle membrane / Golgi membrane / endoplasmic reticulum membrane / perinuclear region of cytoplasm / zinc ion binding / cytosol
Similarity search - Function
Sec23, C-terminal / Protein transport protein Sec23 / Sec23/Sec24, helical domain / Sec23/Sec24 beta-sandwich / Zinc finger, Sec23/Sec24-type superfamily / Sec23/Sec24 helical domain superfamily / Sec23/Sec24, trunk domain / Sec23/Sec24 zinc finger / Sec23/Sec24 trunk domain / Sec23/Sec24 helical domain ...Sec23, C-terminal / Protein transport protein Sec23 / Sec23/Sec24, helical domain / Sec23/Sec24 beta-sandwich / Zinc finger, Sec23/Sec24-type superfamily / Sec23/Sec24 helical domain superfamily / Sec23/Sec24, trunk domain / Sec23/Sec24 zinc finger / Sec23/Sec24 trunk domain / Sec23/Sec24 helical domain / Sec23/Sec24 beta-sandwich domain / Zn-finger domain of Sec23/24 / Zinc finger, Sec23/Sec24-type / Gelsolin-like domain superfamily / Gelsolin repeat / Gelsolin-like domain / ADF-H/Gelsolin-like domain superfamily / von Willebrand factor A-like domain superfamily / SH3 type barrels. / Roll / Mainly Beta
Similarity search - Domain/homology
Protein transport protein Sec23A
Similarity search - Component
|Biological species||Homo sapiens (human)|
|Method||SOLUTION NMR / torsion angle dynamics|
|Authors||Nagashima, T. / Hayashi, F. / Yokoyama, S. / RIKEN Structural Genomics/Proteomics Initiative (RSGI)|
|Citation||Journal: To be Published|
Title: Solution structure of the zf-Sec23_Sec24 from human Sec23A
Authors: Nagashima, T. / Hayashi, F. / Yokoyama, S.
|Structure viewer||Molecule: |
Downloads & links
A: Protein transport protein Sec23A
|#1: Protein|| |
Mass: 6461.266 Da / Num. of mol.: 1 / Fragment: zf-Sec23_Sec24
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Description: Cell-free protein synthesis / Plasmid: P060613-07 / References: UniProt: Q15436
|#2: Chemical|| ChemComp-ZN / |
|Experiment||Method: SOLUTION NMR|
|Details||Contents: 1.12mM uniformly 13C, 15N-labeled protein; 20mM TrisHCl, 100mM NaCl, 1mM DTT, 0.02%NaN3, 0.05mM ZnCl2, 1mM IDA, 10% D2O, 90% H2O|
Solvent system: 10% D2O / 90% H2O
|Sample conditions||Ionic strength: 120mM / pH: 7.0 / Pressure: ambient / Temperature: 298 K|
|NMR spectrometer||Type: Varian INOVA / Manufacturer: Varian / Model: INOVA / Field strength: 800 MHz|
|Refinement||Method: torsion angle dynamics / Software ordinal: 1|
|NMR representative||Selection criteria: lowest energy|
|NMR ensemble||Conformer selection criteria: structures with the least restraint violations, target function|
Conformers calculated total number: 100 / Conformers submitted total number: 20
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