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- PDB-2nu2: Accommodation of positively-charged residues in a hydrophobic spe... -
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Open data
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Basic information
Entry | Database: PDB / ID: 2nu2 | ||||||
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Title | Accommodation of positively-charged residues in a hydrophobic specificity pocket: Crystal structures of SGPB in complex with OMTKY3 variants Lys18I and Arg18I | ||||||
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![]() | HYDROLASE / ENZYME-INHIBITOR COMPLEX / CHARGED P1 RESIDUE | ||||||
Function / homology | ![]() streptogrisin B / molecular function inhibitor activity / serine-type endopeptidase inhibitor activity / serine-type endopeptidase activity / proteolysis / extracellular region Similarity search - Function | ||||||
Biological species | ![]() ![]() ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Bateman, K.S. / Anderson, S. / Lu, W. / Qasim, M.A. / Laskowski Jr., M. / James, M.N.G. | ||||||
![]() | ![]() Title: Accommodation of positively-charged residues in a hydrophobic specificity pocket: Crystal structures of SGPB in complex with OMTKY3 variants Lys18I and Arg18I Authors: Bateman, K.S. / Anderson, S. / Lu, W. / Qasim, M.A. / Laskowski Jr., M. / James, M.N.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 | ![]() | 60.4 KB | Display | ![]() |
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PDB format | ![]() | 42.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 414.7 KB | Display | ![]() |
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Full document | ![]() | 415.4 KB | Display | |
Data in XML | ![]() | 12.3 KB | Display | |
Data in CIF | ![]() | 17.5 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 2nu3C ![]() 2nu4C ![]() 3sgbS 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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Components
#1: Protein | Mass: 18653.232 Da / Num. of mol.: 1 / Fragment: residues 115-299 / Source method: isolated from a natural source / Source: (natural) ![]() |
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#2: Protein | Mass: 5629.325 Da / Num. of mol.: 1 / Fragment: third domain, residues 135-185 / Mutation: L18R Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
#3: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.03 Å3/Da / Density % sol: 39.46 % |
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, hanging drop / pH: 7.1 Details: PEG 4000, SODIUM POTASSIUM PHOSPHATE, pH 7.1, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
-Data collection
Diffraction | Mean temperature: 298 K |
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Diffraction source | Source: ![]() |
Detector | Type: MAC Science DIP-2030 / Detector: IMAGE PLATE / Date: Jan 6, 1998 / Details: mirrors |
Radiation | Monochromator: mirrors / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.54178 Å / Relative weight: 1 |
Reflection | Resolution: 1.65→20 Å / Num. all: 23447 / Num. obs: 22171 / % possible obs: 94.6 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 5 / Redundancy: 3.5 % / Rmerge(I) obs: 0.118 / Net I/σ(I): 8.09 |
Reflection shell | Resolution: 1.65→1.68 Å / Rmerge(I) obs: 0.288 / Mean I/σ(I) obs: 2.86 / % possible all: 55.1 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 3SGB Resolution: 1.65→20 Å / σ(F): 0 / σ(I): 0 / Stereochemistry target values: Engh & Huber /
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Refine analyze | Luzzati coordinate error obs: 0.18 Å / Luzzati sigma a obs: 0.206 Å | |||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.65→20 Å
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Refine LS restraints |
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