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- PDB-1o8o: The active site of the molybdenum cofactor biosynthetic protein d... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1o8o | ||||||
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Title | The active site of the molybdenum cofactor biosynthetic protein domain Cnx1G | ||||||
![]() | MOLYBDOPTERIN BIOSYNTHESIS CNX1 PROTEIN | ||||||
![]() | MOLYBDENUM COFACTOR BIOSYNTHESIS / CNX1G / MUTANTS | ||||||
Function / homology | ![]() glycine receptor clustering / molybdopterin adenylyltransferase / molybdopterin adenylyltransferase activity / establishment of synaptic specificity at neuromuscular junction / molybdopterin molybdotransferase / molybdopterin molybdotransferase activity / gamma-aminobutyric acid receptor clustering / nitrate reductase activity / auxin-activated signaling pathway / Mo-molybdopterin cofactor biosynthetic process ...glycine receptor clustering / molybdopterin adenylyltransferase / molybdopterin adenylyltransferase activity / establishment of synaptic specificity at neuromuscular junction / molybdopterin molybdotransferase / molybdopterin molybdotransferase activity / gamma-aminobutyric acid receptor clustering / nitrate reductase activity / auxin-activated signaling pathway / Mo-molybdopterin cofactor biosynthetic process / molybdenum ion binding / postsynaptic neurotransmitter receptor diffusion trapping / response to metal ion / dendrite / ATP binding / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Kuper, J. / Winking, J. / Hecht, H.J. / Schwarz, G. / Mendel, R.R. | ||||||
![]() | ![]() Title: The Active Site of the Molybdenum Cofactor Biosynthetic Protein Domain Cnx1G Authors: Kuper, J. / Winking, J. / Hecht, H.J. / Mendel, R.R. / Schwarz, G. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 100.2 KB | Display | ![]() |
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PDB format | ![]() | 78.3 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 441.8 KB | Display | ![]() |
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Full document | ![]() | 446.9 KB | Display | |
Data in XML | ![]() | 19.3 KB | Display | |
Data in CIF | ![]() | 26.5 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1o8nC ![]() 1o8qC ![]() 1eavS S: Starting model for refinement C: citing same article ( |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS domain:
NCS domain segments: Ens-ID: 1 / Refine code: 4
NCS oper:
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Components
#1: Protein | Mass: 17729.502 Da / Num. of mol.: 3 / Fragment: CNX1 G-DOMAIN, RESIDUES 462-623 / Mutation: YES Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() #2: Water | ChemComp-HOH / | Compound details | THE MOLECULE CNX1G IS INVOLVED IN MOLYBDENUM COFACTOR BIOSYNTHESIS ENGINEERED MUTATION IN CHAIN A, ...THE MOLECULE CNX1G IS INVOLVED IN MOLYBDENUM | Sequence details | DOMAIN DEFINITION | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.8 Å3/Da / Density % sol: 56.4 % |
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Crystal grow | pH: 6.5 Details: 1.4 M SODIUM ACETATE, 0.1 M SODIUM CACODYLATE, PH 6.5 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() |
Detector | Type: RIGAKU IMAGE PLATE / Detector: IMAGE PLATE / Date: Jul 23, 2001 / Details: OSMIX MIRROR |
Radiation | Monochromator: MIRROR / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.7→26.57 Å / Num. obs: 18549 / % possible obs: 99.9 % / Redundancy: 2.7 % / Rmerge(I) obs: 0.031 / Net I/σ(I): 17.7 |
Reflection shell | Resolution: 2.7→2.85 Å / Redundancy: 5.2 % / Rmerge(I) obs: 0.112 / Mean I/σ(I) obs: 6.7 / % possible all: 100 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 1EAV Resolution: 2.7→100 Å / Cor.coef. Fo:Fc: 0.941 / Cor.coef. Fo:Fc free: 0.913 / SU B: 10.281 / SU ML: 0.208 / Cross valid method: THROUGHOUT / ESU R: 0.605 / ESU R Free: 0.305 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
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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: 46.93 Å2
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Refinement step | Cycle: LAST / Resolution: 2.7→100 Å
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Refine LS restraints |
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