[English] 日本語
![](img/lk-miru.gif)
- PDB-1unb: Deacetoxycephalosporin C synthase complexed with 2-oxoglutarate a... -
+
Open data
-
Basic information
Entry | Database: PDB / ID: 1unb | ||||||
---|---|---|---|---|---|---|---|
Title | Deacetoxycephalosporin C synthase complexed with 2-oxoglutarate and ampicillin | ||||||
![]() | DEACETOXYCEPHALOSPORIN C SYNTHETASE | ||||||
![]() | OXIDOREDUCTASE / ANTIBIOTIC BIOSYNTHESIS | ||||||
Function / homology | ![]() deacetoxycephalosporin-C synthase / deacetoxycephalosporin-C synthase activity / L-ascorbic acid binding / antibiotic biosynthetic process / iron ion binding Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Valegard, K. / Terwisscha van Scheltinga, A.C. / Dubus, A. / Oster, L.M. / Rhangino, G. / Hajdu, J. / Andersson, I. | ||||||
![]() | ![]() Title: The Structural Basis of Cephalosporin Formation in a Mononuclear Ferrous Enzyme Authors: Valegard, K. / Terwisscha van Scheltinga, A.C. / Dubus, A. / Ranghino, G. / Oster, L.M. / Hajdu, J. / Andersson, I. | ||||||
History |
|
-
Structure visualization
Structure viewer | Molecule: ![]() ![]() |
---|
-
Downloads & links
-
Download
PDBx/mmCIF format | ![]() | 79.8 KB | Display | ![]() |
---|---|---|---|---|
PDB format | ![]() | 57.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 740.5 KB | Display | ![]() |
---|---|---|---|---|
Full document | ![]() | 752.5 KB | Display | |
Data in XML | ![]() | 16.9 KB | Display | |
Data in CIF | ![]() | 23.8 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1uo9C ![]() 1uobC ![]() 1uofC ![]() 1uogC ![]() 1rxfS 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: 34591.641 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() References: UniProt: P18548, deacetoxycephalosporin-C synthase |
---|---|
#2: Chemical | ChemComp-FE2 / |
#3: Chemical | ChemComp-AKG / |
#4: Chemical | ChemComp-PN1 / ( |
#5: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
---|
-
Sample preparation
Crystal | Density Matthews: 2.26 Å3/Da / Density % sol: 45.7 % | ||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Crystal grow | pH: 7.5 Details: 1.75M AMMONIUM SULPHATE, 5MM 2-OXOGLUTARATE,0.1M HEPESPH7.5, pH 7.50 | ||||||||||||||||||||
Crystal grow | *PLUS Method: unknown / Details: Valegard, K., (1998) Nature, 394, 805. / PH range low: 7.5 / PH range high: 7 | ||||||||||||||||||||
Components of the solutions | *PLUS
|
-Data collection
Diffraction | Mean temperature: 100 K |
---|---|
Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARRESEARCH / Detector: CCD / Date: Feb 15, 2002 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.076 Å / Relative weight: 1 |
Reflection | Resolution: 1.5→31.4 Å / Num. obs: 45847 / % possible obs: 94 % / Redundancy: 5.5 % / Rmerge(I) obs: 0.064 |
Reflection shell | Resolution: 1.5→1.55 Å / Rmerge(I) obs: 0.295 / % possible all: 100 |
Reflection | *PLUS Highest resolution: 1.5 Å / Num. obs: 45862 / % possible obs: 94.2 % / Num. measured all: 299664 / Rmerge(I) obs: 0.064 |
Reflection shell | *PLUS % possible obs: 99.9 % / Rmerge(I) obs: 0.312 |
-
Processing
Software |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 1RXF Resolution: 1.5→31.5 Å / Cor.coef. Fo:Fc: 0.962 / Cor.coef. Fo:Fc free: 0.941 / SU B: 1.76 / SU ML: 0.06 / Cross valid method: THROUGHOUT / ESU R Free: 0.09 / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: THE RESIDUES MISSING IN THE PDB ENTRY (81-90,167-177 AND 310-311) ARE DISORDERED, AND THEREFORE OMITTED FROM THE MODEL
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: BABINET MODEL WITH MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 22.3 Å2
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.5→31.5 Å
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints |
|