+Open data
-Basic information
Entry | Database: PDB / ID: 4gm5 | ||||||
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Title | Carboxypeptidase T with Sulphamoil Arginine | ||||||
Components | Carboxypeptidase T | ||||||
Keywords | HYDROLASE/HYDROLASE inhibitor / Zinc carboxypeptidase / HYDROLASE-HYDROLASE inhibitor complex | ||||||
Function / homology | Function and homology information carboxypeptidase T / metallocarboxypeptidase activity / proteolysis / extracellular space / zinc ion binding Similarity search - Function | ||||||
Biological species | Thermoactinomyces vulgaris (bacteria) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.39 Å | ||||||
Authors | Kuznetsov, S.A. / Timofeev, V.I. / Akparov, V.K. / Kuranova, I.P. | ||||||
Citation | Journal: To be Published Title: Carboxypeptidase T with Sulphamoil Arginine Authors: Kuznetsov, S.A. / Timofeev, V.I. / Akparov, V.K. / Kuranova, I.P. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 4gm5.cif.gz | 175.5 KB | Display | PDBx/mmCIF format |
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PDB format | pdb4gm5.ent.gz | 148.3 KB | Display | PDB format |
PDBx/mmJSON format | 4gm5.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 4gm5_validation.pdf.gz | 796.1 KB | Display | wwPDB validaton report |
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Full document | 4gm5_full_validation.pdf.gz | 802.2 KB | Display | |
Data in XML | 4gm5_validation.xml.gz | 21.2 KB | Display | |
Data in CIF | 4gm5_validation.cif.gz | 31.8 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/gm/4gm5 ftp://data.pdbj.org/pub/pdb/validation_reports/gm/4gm5 | HTTPS FTP |
-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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2 |
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Unit cell |
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Components on special symmetry positions |
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-Components
-Protein , 1 types, 1 molecules A
#1: Protein | Mass: 36641.277 Da / Num. of mol.: 1 / Fragment: unp residues 99-421 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Thermoactinomyces vulgaris (bacteria) / Gene: cpt / Production host: Escherichia coli (E. coli) / References: UniProt: P29068, carboxypeptidase T |
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-Non-polymers , 6 types, 435 molecules
#2: Chemical | ChemComp-ZN / | ||||||||
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#3: Chemical | ChemComp-CA / #4: Chemical | ChemComp-SO4 / #5: Chemical | ChemComp-0X9 / | #6: Chemical | ChemComp-GOL / #7: 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: 5.17 Å3/Da / Density % sol: 76.19 % |
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: SPring-8 / Beamline: BL41XU / Wavelength: 0.8 Å |
Detector | Type: MARMOSAIC 225 mm CCD / Detector: CCD |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.8 Å / Relative weight: 1 |
Reflection | Resolution: 1.388→26.95 Å / Num. all: 152576 / Num. obs: 151202 / % possible obs: 99.1 % / Redundancy: 4.97 % / Rmerge(I) obs: 0.067 / Net I/σ(I): 15.7916 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 1.39→20 Å / Cor.coef. Fo:Fc: 0.977 / Cor.coef. Fo:Fc free: 0.972 / SU B: 1.35 / SU ML: 0.023 / Cross valid method: THROUGHOUT / ESU R: 0.035 / ESU R Free: 0.035 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN USED IF PRESENT IN THE INPUT
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 17.129 Å2
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Refinement step | Cycle: LAST / Resolution: 1.39→20 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.388→1.424 Å / Total num. of bins used: 20
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