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- PDB-6fcy: Catalytic subunit HisG from Psychrobacter arcticus ATP phosphorib... -
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Open data
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Basic information
Entry | Database: PDB / ID: 6fcy | ||||||
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Title | Catalytic subunit HisG from Psychrobacter arcticus ATP phosphoribosyltransferase (HisZG ATPPRT) in complex with PRPP and ADP | ||||||
![]() | ATP phosphoribosyltransferase | ||||||
![]() | TRANSFERASE / phosphoribosyltransferase / HisG / catalytic / cold-adapted | ||||||
Function / homology | ![]() ATP phosphoribosyltransferase / ATP phosphoribosyltransferase activity / L-histidine biosynthetic process / ATP binding / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Alphey, M.S. / Ge, Y. / Fisher, G. / Czekster, C.M. / Naismith, J.H. / da Silva, R.G. | ||||||
Funding support | ![]()
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![]() | ![]() Title: Catalytic and Anticatalytic Snapshots of a Short-Form ATP Phosphoribosyltransferase Authors: Alphey, M.S. / Fisher, G. / Hirschi, J.S. / Stroek, R. / Ge, Y. / Gould, E.R. / Czekster, C.M. / Liu, H. / Florence, G.J. / Vetticatt, M.J. / Naismith, J.H. / da Silva, R.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 | ![]() | 60.3 KB | Display | ![]() |
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PDB format | ![]() | 41.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 1 MB | Display | ![]() |
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Full document | ![]() | 1 MB | Display | |
Data in XML | ![]() | 11 KB | Display | |
Data in CIF | ![]() | 15 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 6fcaC ![]() 6fccC ![]() 6fctC ![]() 6fcwC ![]() 6fd9C ![]() 6fttC ![]() 6fu2C ![]() 6fu7C ![]() 6fuaC ![]() 5m8hS 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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1 | ![]()
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Unit cell |
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Components on special symmetry positions |
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Components
#1: Protein | Mass: 25240.965 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Details: Residues from N- and C-termini are missing from coordinate sequence due to flexibility - electron density missing. Initial glycine remains after affinity-tag cleavage. Source: (gene. exp.) ![]() ![]() ![]() |
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#2: Sugar | ChemComp-PRP / |
#3: Chemical | ChemComp-ADP / |
#4: Chemical | ChemComp-MG / |
#5: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.23 Å3/Da / Density % sol: 44.91 % |
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Crystal grow | Temperature: 277 K / Method: vapor diffusion / pH: 6.5 Details: 10mg/ml protein in 20mM Tris HCl pH8.0, 50mM KCl, 10mM MgCl2, 2mM DTT mixed 1:1 with 32% PEG 3350, 0.1M MOPS pH6.5, 0.1M K/Na tartrate |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() |
Detector | Type: RIGAKU SATURN 944+ / Detector: CCD / Date: Mar 8, 2017 / Details: mirrors |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 1.96→23.03 Å / Num. obs: 16164 / % possible obs: 99.1 % / Redundancy: 3.9 % / CC1/2: 0.996 / Rmerge(I) obs: 0.094 / Rpim(I) all: 0.054 / Rrim(I) all: 0.109 / Net I/σ(I): 9 / Num. measured all: 63590 / Scaling rejects: 44 |
Reflection shell | Resolution: 1.96→2.01 Å / Redundancy: 3 % / Rmerge(I) obs: 0.477 / Num. unique obs: 1029 / CC1/2: 0.762 / Rpim(I) all: 0.325 / Rrim(I) all: 0.583 / % possible all: 90.1 |
-Phasing
Phasing | Method: ![]() |
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Processing
Software |
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Refinement | Method to determine structure: ![]() Starting model: 5M8H chain E Resolution: 1.96→23.03 Å / Cor.coef. Fo:Fc: 0.957 / Cor.coef. Fo:Fc free: 0.943 / SU B: 4.605 / SU ML: 0.12 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.171 / ESU R Free: 0.152 Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS U VALUES : REFINED INDIVIDUALLY
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso max: 81.72 Å2 / Biso mean: 27.018 Å2 / Biso min: 14.7 Å2
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Refinement step | Cycle: final / Resolution: 1.96→23.03 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.961→2.012 Å / Rfactor Rfree error: 0 / Total num. of bins used: 20
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