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Yorodumi- PDB-2abz: Crystal structure of C19A/C43A mutant of leech carboxypeptidase i... -
+Open data
-Basic information
Entry | Database: PDB / ID: 2abz | ||||||
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Title | Crystal structure of C19A/C43A mutant of leech carboxypeptidase inhibitor in complex with bovine carboxypeptidase A | ||||||
Components |
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Keywords | hydrolase/hydrolase inhibitor / inhibitor-metallocarboxypeptidase complex / LCI mutant / oxidative folding intermediate analog / hydrolase-hydrolase inhibitor COMPLEX | ||||||
Function / homology | Function and homology information carboxypeptidase A / peptidase inhibitor activity / leukotriene metabolic process / metallocarboxypeptidase activity / proteolysis / extracellular space / zinc ion binding Similarity search - Function | ||||||
Biological species | Bos taurus (cattle) Hirudo medicinalis (medicinal leech) | ||||||
Method | X-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 2.16 Å | ||||||
Authors | Arolas, J.L. / Popowicz, G.M. / Bronsoms, S. / Aviles, F.X. / Huber, R. / Holak, T.A. / Ventura, S. | ||||||
Citation | Journal: J.Mol.Biol. / Year: 2005 Title: Study of a major intermediate in the oxidative folding of leech carboxypeptidase inhibitor: contribution of the fourth disulfide bond Authors: Arolas, J.L. / Popowicz, G.M. / Bronsoms, S. / Aviles, F.X. / Huber, R. / Holak, T.A. / Ventura, S. #1: Journal: NAT.STRUCT.MOL.BIOL. / Year: 2000 Title: Structure of a novel leech carboxypeptidase inhibitor determined free in solution and in complex with human carboxypeptidase A2 Authors: Reverter, D. / Fernandez-Catalan, C. / Baumgartner, R. / Pfander, R. / Huber, R. / Bode, W. / Vendrell, J. / Holak, T.A. / Aviles, F.X. #2: Journal: Structure / Year: 2005 Title: NMR structural characterization and computational predictions of the major intermediate in oxidative folding of leech carboxypeptidase inhibitor Authors: Arolas, J.L. / D'Silva, L. / Popowicz, G.M. / Aviles, F.X. / Holak, T.A. / Ventura, S. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2abz.cif.gz | 162.2 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2abz.ent.gz | 135.5 KB | Display | PDB format |
PDBx/mmJSON format | 2abz.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2abz_validation.pdf.gz | 439.6 KB | Display | wwPDB validaton report |
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Full document | 2abz_full_validation.pdf.gz | 456.3 KB | Display | |
Data in XML | 2abz_validation.xml.gz | 19.5 KB | Display | |
Data in CIF | 2abz_validation.cif.gz | 28.7 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ab/2abz ftp://data.pdbj.org/pub/pdb/validation_reports/ab/2abz | HTTPS FTP |
-Related structure data
Related structure data | |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 34721.750 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Bos taurus (cattle) / Plasmid: pPIC9 / Production host: Pichia pastoris (fungus) / Strain (production host): KM71 / References: UniProt: P00730, carboxypeptidase A #2: Protein | Mass: 7333.126 Da / Num. of mol.: 4 / Mutation: C19A/C43A Source method: isolated from a genetically manipulated source Source: (gene. exp.) Hirudo medicinalis (medicinal leech) / Plasmid: pBAT4 / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) / References: UniProt: P81511 #3: Chemical | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 3.1 Å3/Da / Density % sol: 60.02 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, sitting drop / pH: 8.5 Details: 1.5M Lithium Sulfate monohydrate, 100mM Tris, pH 8.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K |
-Data collection
Detector | Date: Jun 21, 2004 |
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Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Relative weight: 1 |
Reflection | Resolution: 2.1→30 Å / Num. obs: 66322 |
-Processing
Software | Name: REFMAC / Version: 5.1.2 / Classification: refinement | ||||||||||||||||||||
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.16→30 Å / σ(F): 2 / Stereochemistry target values: Engh & Huber
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Refinement step | Cycle: LAST / Resolution: 2.16→30 Å
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