[English] 日本語
![](img/lk-miru.gif)
- PDB-1v39: DC26 MUTANT OF VACCINIA VIRUS PROTEIN VP39 IN COMPLEX WITH S-ADEN... -
+
Open data
-
Basic information
Entry | Database: PDB / ID: 1v39 | ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Title | DC26 MUTANT OF VACCINIA VIRUS PROTEIN VP39 IN COMPLEX WITH S-ADENOSYLHOMOCYSTEINE AND M7G(5')PPPG | ||||||||||||
![]() | VP39 | ||||||||||||
![]() | ![]() ![]() ![]() ![]() ![]() ![]() | ||||||||||||
Function / homology | ![]() regulation of mRNA 3'-end processing / 7-methylguanosine mRNA capping / ![]() ![]() ![]() ![]() Similarity search - Function | ||||||||||||
Biological species | ![]() ![]() ![]() | ||||||||||||
Method | ![]() ![]() | ||||||||||||
![]() | Hodel, A.E. / Gershon, P.D. / Quiocho, F.A. | ||||||||||||
![]() | ![]() Title: Specific protein recognition of an mRNA cap through its alkylated base. Authors: Hodel, A.E. / Gershon, P.D. / Shi, X. / Wang, S.M. / Quiocho, F.A. #1: ![]() Title: The 1.85 A Structure of Vaccinia Protein Vp39: A Bifunctional Enzyme that Participates in the Modification of Both Mrna Ends Authors: Hodel, A.E. / Gershon, P.D. / Shi, X. / Quiocho, F.A. | ||||||||||||
History |
|
-
Structure visualization
Structure viewer | Molecule: ![]() ![]() |
---|
-
Downloads & links
-
Download
PDBx/mmCIF format | ![]() | 80 KB | Display | ![]() |
---|---|---|---|---|
PDB format | ![]() | 57.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
---|
-Related structure data
Related structure data | ![]() 1p39C ![]() 1vp3C ![]() 1vp9C ![]() 2vp3C ![]() 1vptS S: Starting model for refinement C: citing same article ( |
---|---|
Similar structure data |
-
Links
-
Assembly
Deposited unit | ![]()
| |||||||||
---|---|---|---|---|---|---|---|---|---|---|
1 | ![]()
| |||||||||
Unit cell |
| |||||||||
Components on special symmetry positions |
|
-
Components
#1: Protein | Mass: 37133.703 Da / Num. of mol.: 1 / Mutation: 26 C-TERMINAL RESIDUES DELETED Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() ![]() ![]() ![]() References: UniProt: P07617, ![]() |
---|---|
#2: Chemical | ChemComp-SAH / ![]() |
#3: Chemical | ChemComp-M7G / |
#4: Water | ChemComp-HOH / ![]() |
-Experimental details
-Experiment
Experiment | Method: ![]() |
---|
-
Sample preparation
Crystal | Density Matthews: 2.71 Å3/Da / Density % sol: 53 % | ||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Crystal grow![]() | pH: 6.5 Details: DC26/ADOHCY CRYSTAL SOAKED IN 10MM M7GPPPG., pH 6.5 | ||||||||||||||||||||||||
Crystal grow | *PLUS pH: 4.5 Details: macro-seeding, Hodel, A.E., (1996) Cell(Cambridge,Mass.), 85, 247. Method: other | ||||||||||||||||||||||||
Components of the solutions | *PLUS
|
-Data collection
Diffraction | Mean temperature: 103 K |
---|---|
Diffraction source | Source: ![]() |
Detector | Type: MACSCIENCE / Detector: IMAGE PLATE / Date: May 6, 1996 / Details: MIRROR |
Radiation | Monochromator: NI FILTER / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength![]() |
Reflection | Resolution: 1.8→15 Å / Num. obs: 35403 / % possible obs: 95 % / Observed criterion σ(I): 2 / Redundancy: 4 % / Rmerge(I) obs: 0.046 / Net I/σ(I): 35 |
Reflection shell | Resolution: 1.8→1.86 Å / Redundancy: 1 % / Rmerge(I) obs: 0.27 / Mean I/σ(I) obs: 4 / % possible all: 67 |
Reflection shell | *PLUS % possible obs: 67 % |
-
Processing
Software |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method to determine structure![]() ![]() Starting model: PDB ENTRY 1VPT Resolution: 1.8→8 Å / Data cutoff high absF: 100000 / Data cutoff low absF: 0.0001 / Isotropic thermal model: RESTRAINED / σ(F): 2
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 31 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.8→8 Å
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS |