[English] 日本語
![](img/lk-miru.gif)
- PDB-2qwk: THE X-RAY STRUCTURE OF A COMPLEX OF 5-N-ACETYL-5-AMINO-3-(1-ETHYL... -
+
Open data
-
Basic information
Entry | Database: PDB / ID: 2qwk | |||||||||
---|---|---|---|---|---|---|---|---|---|---|
Title | THE X-RAY STRUCTURE OF A COMPLEX OF 5-N-ACETYL-5-AMINO-3-(1-ETHYLPROPOXY)-1-CYCLOHEXENE-1-CARBOXYLIC ACID (GS4071) AND WILDTYPE TERN N9 INFLUENZA VIRUS NEURAMINIDASE | |||||||||
![]() | NEURAMINIDASE | |||||||||
![]() | HYDROLASE / NEURAMINIDASE / INFLUENZA PROTEIN / SIALIC ACID ANALOGUES / DANA ANOLOGUES / GS4071. NEURAMINIDASE / DRUG RESISTANT VARIANT / GLYCOSYLATED PROTEIN / GS4071 | |||||||||
Function / homology | ![]() exo-alpha-(2->3)-sialidase activity / exo-alpha-(2->6)-sialidase activity / exo-alpha-(2->8)-sialidase activity / exo-alpha-sialidase / viral budding from plasma membrane / carbohydrate metabolic process / host cell plasma membrane / virion membrane / membrane / metal ion binding Similarity search - Function | |||||||||
Biological species | ![]() ![]() | |||||||||
Method | ![]() ![]() | |||||||||
![]() | Varghese, J.N. | |||||||||
![]() | ![]() Title: Drug design against a shifting target: a structural basis for resistance to inhibitors in a variant of influenza virus neuraminidase. Authors: Varghese, J.N. / Smith, P.W. / Sollis, S.L. / Blick, T.J. / Sahasrabudhe, A. / McKimm-Breschkin, J.L. / Colman, P.M. #1: ![]() Title: Mutations in a Conserved Residue in the Influenza Virus Neuraminidase Active Site Decreases Sensitivity to Neu5Ac2En-Derived Inhibitors Authors: Mckimm-Breschkin, J.L. / Sahasrabudhe, A. / Blick, T.J. / Mcdonald, M. / Colman, P.M. / Hart, G.J. / Bethell, R.C. / Varghese, J.N. | |||||||||
History |
|
-
Structure visualization
Structure viewer | Molecule: ![]() ![]() |
---|
-
Downloads & links
-
Download
PDBx/mmCIF format | ![]() | 104.9 KB | Display | ![]() |
---|---|---|---|---|
PDB format | ![]() | 78.4 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
---|
-Related structure data
Related structure data | ![]() 2qwaC ![]() 2qwbC ![]() 2qwcC ![]() 2qwdC ![]() 2qweC ![]() 2qwfC ![]() 2qwgC ![]() 2qwhC ![]() 2qwiC ![]() 2qwjC C: citing same article ( |
---|---|
Similar structure data |
-
Links
-
Assembly
Deposited unit | ![]()
| |||||||||
---|---|---|---|---|---|---|---|---|---|---|
1 | ![]()
| |||||||||
Unit cell |
| |||||||||
Components on special symmetry positions |
|
-
Components
-Protein , 1 types, 1 molecules A
#1: Protein | Mass: 43723.770 Da / Num. of mol.: 1 / Fragment: RESIDUES 82 - 468 Source method: isolated from a genetically manipulated source Details: INTEGRAL MEMBRANE PROTEIN, MEMBRANE BOUND STALK CLEAVED BY PRONASE, RELEASING FULLY ACTIVE HEAD WITH RESIDUES 82 - 468 (TOKYO/3/67 NUMBERING) Source: (gene. exp.) ![]() ![]() ![]() ![]() |
---|
-Sugars , 3 types, 3 molecules ![](data/chem/img/NAG.gif)
#2: Polysaccharide | alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-[alpha-D- ...alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose Source method: isolated from a genetically manipulated source |
---|---|
#3: Polysaccharide | 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose Source method: isolated from a genetically manipulated source |
#4: Sugar | ChemComp-NAG / |
-Non-polymers , 3 types, 353 molecules ![](data/chem/img/G39.gif)
![](data/chem/img/CA.gif)
![](data/chem/img/HOH.gif)
![](data/chem/img/CA.gif)
![](data/chem/img/HOH.gif)
#5: Chemical | ChemComp-G39 / ( | ||
---|---|---|---|
#6: Chemical | #7: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
---|
-
Sample preparation
Crystal | Density Matthews: 2.82 Å3/Da / Density % sol: 54 % Description: THIS EXPERIMENT WAS CARRIED OUT TO DETERMINE THE STRUCTURE OF COMPLEX OF 5-N-ACETYL-5-AMINO-3- (1-ETHYLPROPOXY)-1-CYCLOHEXENE-1-CARBOXYLIC ACID (GS4071) AND WILDTYPE TERN N9 NEURAMINIDASE. | ||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Crystal grow | pH: 5.9 / Details: 1.9M PHOSPHATE (PH 5.9) | ||||||||||||||||||||
Crystal | *PLUS | ||||||||||||||||||||
Crystal grow | *PLUS pH: 6.6 / Method: vapor diffusion / Details: Laver, W.G., (1984) Virology, 137, 314. | ||||||||||||||||||||
Components of the solutions | *PLUS
|
-Data collection
Diffraction | Mean temperature: 107 K |
---|---|
Diffraction source | Source: ![]() |
Detector | Type: RIGAKU RAXIS II / Detector: IMAGE PLATE / Date: Jan 13, 1997 / Details: YALE MIRRORS |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 1.8→100 Å / Num. obs: 37216 / % possible obs: 79.6 % / Observed criterion σ(I): 1 / Redundancy: 4.15 % / Rmerge(I) obs: 0.092 / Rsym value: 0.088 |
Reflection shell | Resolution: 1.8→1.863 Å / % possible all: 29.5 |
Reflection | *PLUS Num. measured all: 154336 |
-
Processing
Software |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method to determine structure: ![]() Starting model: TERN N9 NEURAMINIDASE Resolution: 1.8→6 Å / σ(F): 1 / Details: 2 METAL IONS
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine analyze | Luzzati coordinate error obs: 0.01 Å / Luzzati d res low obs: 6 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.8→6 Å
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
LS refinement shell | Resolution: 1.8→1.83 Å / Total num. of bins used: 20
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Xplor file |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Highest resolution: 2 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS |