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Open data
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Basic information
Entry | Database: PDB / ID: 1ekr | ||||||
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Title | MOAC PROTEIN FROM E. COLI | ||||||
![]() | MOLYBDENUM COFACTOR BIOSYNTHESIS PROTEIN C | ||||||
![]() | TRANSLATION / MoaC / Molybdenum cofactor (Moco) / Moco biosynthesis / Moco deficiency | ||||||
Function / homology | ![]() cyclic pyranopterin monophosphate synthase / cyclic pyranopterin monophosphate synthase activity / Mo-molybdopterin cofactor biosynthetic process / protein-containing complex / identical protein binding Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Schindelin, H. / Liu, M.T.W. / Wuebbens, M.M. / Rajagopalan, K.V. | ||||||
![]() | ![]() Title: Insights into molybdenum cofactor deficiency provided by the crystal structure of the molybdenum cofactor biosynthesis protein MoaC. Authors: Wuebbens, M.M. / Liu, M.T. / Rajagopalan, K. / Schindelin, H. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 40.8 KB | Display | ![]() |
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PDB format | ![]() | 28.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 367.7 KB | Display | ![]() |
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Full document | ![]() | 371.7 KB | Display | |
Data in XML | ![]() | 5 KB | Display | |
Data in CIF | ![]() | 7 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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Links
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Assembly
Deposited unit | ![]()
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1 | ![]()
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Unit cell |
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Details | The biological assembly is a hexamer with 32 symmetry generated from chain A by crystallographic symmetry operations |
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Components
#1: Protein | Mass: 17477.277 Da / Num. of mol.: 1 / Mutation: S2A Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
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#2: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.15 Å3/Da / Density % sol: 42.78 % | ||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 295 K / Method: vapor diffusion, sitting drop / pH: 7.5 Details: PEG 400, CALCIUM CHLORIDE, HEPES, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 22K | ||||||||||||||||||||||||||||||
Crystal | *PLUS Density % sol: 42 % | ||||||||||||||||||||||||||||||
Crystal grow | *PLUS Method: vapor diffusion | ||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 95 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC QUANTUM 4 / Detector: CCD / Date: Mar 15, 1998 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.1 Å / Relative weight: 1 |
Reflection | Resolution: 1.95→20 Å / Num. all: 57577 / Num. obs: 11190 / % possible obs: 95.7 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 5.1 % / Biso Wilson estimate: 48 Å2 / Rmerge(I) obs: 0.063 / Net I/σ(I): 29.1 |
Reflection shell | Resolution: 1.95→2.02 Å / Redundancy: 3.9 % / Rmerge(I) obs: 0.497 / Num. unique all: 1083 / % possible all: 95.7 |
Reflection | *PLUS Highest resolution: 2 Å / Lowest resolution: 50 Å / Redundancy: 5.2 % |
Reflection shell | *PLUS % possible obs: 97.9 % / Rmerge(I) obs: 0.365 / Mean I/σ(I) obs: 3.5 |
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Processing
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Refinement | Resolution: 2→20 Å / σ(F): 0 / σ(I): 0 / Stereochemistry target values: Lamzin Details: Partial structure factors for bulk solvent were calculated in XPLOR and incorporated into REFMAC
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Refinement step | Cycle: LAST / Resolution: 2→20 Å
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Refine LS restraints |
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Software | *PLUS Name: REFMAC / Classification: refinement | |||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Rfactor Rfree: 0.252 / Rfactor Rwork: 0.219 | |||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | |||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | |||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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