+
Open data
-
Basic information
Entry | Database: PDB / ID: 1fp4 | ||||||
---|---|---|---|---|---|---|---|
Title | CRYSTAL STRUCTURE OF THE ALPHA-H195Q MUTANT OF NITROGENASE | ||||||
![]() | (NITROGENASE MOLYBDENUM-IRON PROTEIN ...) x 2 | ||||||
![]() | OXIDOREDUCTASE / Iron-Sulfur-Molybdenum protein | ||||||
Function / homology | ![]() molybdenum-iron nitrogenase complex / nitrogenase / : / nitrogenase activity / nitrogen fixation / iron-sulfur cluster binding / ATP binding / metal ion binding Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() | ||||||
![]() | Sorlie, M. / Christiansen, J. / Lemon, B.J. / Peters, J.W. / Dean, D.R. / Hales, B.J. | ||||||
![]() | ![]() Title: Mechanistic features and structure of the nitrogenase alpha-Gln195 MoFe protein Authors: Sorlie, M. / Christiansen, J. / Lemon, B.J. / Peters, J.W. / Dean, D.R. / Hales, B.J. | ||||||
History |
|
-
Structure visualization
Structure viewer | Molecule: ![]() ![]() |
---|
-
Downloads & links
-
Download
PDBx/mmCIF format | ![]() | 410.3 KB | Display | ![]() |
---|---|---|---|---|
PDB format | ![]() | 328.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 456.7 KB | Display | ![]() |
---|---|---|---|---|
Full document | ![]() | 507.3 KB | Display | |
Data in XML | ![]() | 43.1 KB | Display | |
Data in CIF | ![]() | 66.1 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | |
---|---|
Similar structure data |
-
Links
-
Assembly
Deposited unit | ![]()
| ||||||||
---|---|---|---|---|---|---|---|---|---|
1 |
| ||||||||
Unit cell |
|
-
Components
-NITROGENASE MOLYBDENUM-IRON PROTEIN ... , 2 types, 4 molecules ACBD
#1: Protein | Mass: 55353.027 Da / Num. of mol.: 2 / Mutation: H195Q Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() #2: Protein | Mass: 59535.879 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() |
---|
-Non-polymers , 5 types, 441 molecules ![](data/chem/img/HCA.gif)
![](data/chem/img/CFM.gif)
![](data/chem/img/CLP.gif)
![](data/chem/img/CA.gif)
![](data/chem/img/HOH.gif)
![](data/chem/img/CFM.gif)
![](data/chem/img/CLP.gif)
![](data/chem/img/CA.gif)
![](data/chem/img/HOH.gif)
#3: Chemical | #4: Chemical | #5: Chemical | #6: Chemical | #7: Water | ChemComp-HOH / | |
---|
-Experimental details
-Experiment
Experiment | Method: ![]() |
---|
-
Sample preparation
Crystal | Density Matthews: 2.28 Å3/Da / Density % sol: 45.95 % | ||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Crystal grow | Temperature: 298 K / Method: microcapillary batch diffusion / pH: 8 Details: PEG 4000, TRIS pH 8.0, sodium molybdate, microcapillary batch diffusion, temperature 298K | ||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Method: batch method | ||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
|
-Data collection
Diffraction | Mean temperature: 100 K |
---|---|
Diffraction source | Source: ![]() |
Detector | Type: RIGAKU RAXIS IIC / Detector: IMAGE PLATE / Date: Oct 13, 1999 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.5→20 Å / Num. all: 63058 / Num. obs: 59345 / % possible obs: 93 % / Observed criterion σ(F): 1 / Observed criterion σ(I): 1 / Redundancy: 6.4 % / Rmerge(I) obs: 0.082 / Net I/σ(I): 7.9 |
Reflection shell | Resolution: 2.5→20 Å / Redundancy: 6.4 % / Rmerge(I) obs: 0.082 / % possible all: 70.9 |
Reflection | *PLUS Num. obs: 63058 / % possible obs: 88.8 % / Num. measured all: 403283 |
Reflection shell | *PLUS % possible obs: 60 % / Rmerge(I) obs: 0.252 |
-
Processing
Software |
| ||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Resolution: 2.5→20 Å / σ(F): 1 / σ(I): 1
| ||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.5→20 Å
| ||||||||||||||||||||
Refine LS restraints |
| ||||||||||||||||||||
Refinement | *PLUS Num. reflection Rfree: 2988 / Rfactor Rfree: 0.239 / Rfactor Rwork: 0.182 | ||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||
Refine LS restraints | *PLUS Type: x_angle_deg / Dev ideal: 2.5 |