+Open data
-Basic information
Entry | Database: PDB / ID: 1fma | ||||||
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Title | MOLYBDOPTERIN SYNTHASE (MOAD/MOAE) | ||||||
Components |
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Keywords | TRANSFERASE / Isopeptide bond / Molybdenum cofactor biosynthesis | ||||||
Function / homology | Function and homology information molybdopterin adenylyltransferase complex / molybdopterin synthase complex / molybdopterin synthase / molybdopterin synthase activity / Mo-molybdopterin cofactor biosynthetic process / nucleotide binding / protein homodimerization activity / cytosol Similarity search - Function | ||||||
Biological species | Escherichia coli (E. coli) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / Resolution: 1.58 Å | ||||||
Authors | Rudolph, M.J. / Wuebbens, M.M. / Rajagolpalan, K.V. / Schindelin, H. | ||||||
Citation | Journal: Nat.Struct.Biol. / Year: 2001 Title: Crystal structure of molybdopterin synthase and its evolutionary relationship to ubiquitin activation. Authors: Rudolph, M.J. / Wuebbens, M.M. / Rajagopalan, K.V. / Schindelin, H. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1fma.cif.gz | 61.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1fma.ent.gz | 44.9 KB | Display | PDB format |
PDBx/mmJSON format | 1fma.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/fm/1fma ftp://data.pdbj.org/pub/pdb/validation_reports/fm/1fma | HTTPS FTP |
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-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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2 |
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Unit cell |
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Details | The biological assembly is a heteroteteramer consisting of two alpha subunits and two beta subunits where the alpha-beta heterodimer falls on a crystallographic twofold axis of symmetry to generate the heterotetramer |
-Components
#1: Protein | Mass: 8764.880 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / Plasmid: PET15B / Production host: Escherichia coli (E. coli) / References: UniProt: P30748 | ||
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#2: Protein | Mass: 17003.020 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / Plasmid: PET15B / Production host: Escherichia coli (E. coli) / References: UniProt: P30749 | ||
#3: Chemical | #4: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.11 Å3/Da / Density % sol: 41.75 % | ||||||||||||||||||
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Crystal grow | Temperature: 295 K / Method: vapor diffusion / pH: 7.5 Details: Sodium chloride, Hepes , pH 7.5, VAPOR DIFFUSION, temperature 295K | ||||||||||||||||||
Crystal grow | *PLUS | ||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 95 K |
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Diffraction source | Source: SYNCHROTRON / Site: NSLS / Beamline: X26C / Wavelength: 1.1 |
Detector | Type: ADSC QUANTUM 4 / Detector: CCD / Date: Nov 1, 1999 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.1 Å / Relative weight: 1 |
Reflection | Resolution: 1.58→20 Å / Num. all: 150077 / Num. obs: 29821 / % possible obs: 95.2 % / Observed criterion σ(I): 0 / Redundancy: 5 % / Biso Wilson estimate: 19.32 Å2 / Rmerge(I) obs: 0.066 / Net I/σ(I): 13.5 |
Reflection shell | Resolution: 1.58→1.61 Å / Redundancy: 5 % / Rmerge(I) obs: 0.294 / % possible all: 95.2 |
Reflection | *PLUS Num. measured all: 150077 |
Reflection shell | *PLUS % possible obs: 88.7 % / Mean I/σ(I) obs: 1.8 |
-Processing
Software |
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Refinement | Resolution: 1.58→20 Å / SU B: 2.66084 / SU ML: 0.09354 / σ(F): 0 / ESU R: 0.16872 / ESU R Free: 0.14205 / Stereochemistry target values: Murshudov
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Displacement parameters | Biso mean: 20.03 Å2
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Refinement step | Cycle: LAST / Resolution: 1.58→20 Å
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Refine LS restraints |
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Software | *PLUS Name: REFMAC / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS σ(F): 0 / % reflection Rfree: 4.9 % | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS |