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Yorodumi- PDB-3azu: X-RAY CRYSTAL STRUCTURE OF THE TWO SITE-SPECIFIC MUTANTS HIS35GLN... -
+Open data
-Basic information
Entry | Database: PDB / ID: 3azu | ||||||
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Title | X-RAY CRYSTAL STRUCTURE OF THE TWO SITE-SPECIFIC MUTANTS HIS35GLN AND HIS35LEU OF AZURIN FROM PSEUDOMONAS AERUGINOSA | ||||||
Components | AZURIN | ||||||
Keywords | ELECTRON TRANSFER(CUPROPROTEIN) | ||||||
Function / homology | Function and homology information transition metal ion binding / periplasmic space / electron transfer activity / copper ion binding / zinc ion binding / identical protein binding Similarity search - Function | ||||||
Biological species | Pseudomonas aeruginosa (bacteria) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 2.1 Å | ||||||
Authors | Messerschmidt, A. / Nar, H. / Huber, R. | ||||||
Citation | Journal: J.Mol.Biol. / Year: 1991 Title: X-ray crystal structure of the two site-specific mutants His35Gln and His35Leu of azurin from Pseudomonas aeruginosa. Authors: Nar, H. / Messerschmidt, A. / Huber, R. / van de Kamp, M. / Canters, G.W. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 3azu.cif.gz | 113.6 KB | Display | PDBx/mmCIF format |
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PDB format | pdb3azu.ent.gz | 88.5 KB | Display | PDB format |
PDBx/mmJSON format | 3azu.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 3azu_validation.pdf.gz | 383.4 KB | Display | wwPDB validaton report |
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Full document | 3azu_full_validation.pdf.gz | 389.6 KB | Display | |
Data in XML | 3azu_validation.xml.gz | 10.9 KB | Display | |
Data in CIF | 3azu_validation.cif.gz | 18.6 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/az/3azu ftp://data.pdbj.org/pub/pdb/validation_reports/az/3azu | HTTPS FTP |
-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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Details | THERE ARE FOUR MOLECULES IN THE ASYMMETRIC UNIT WHICH ARE ARRANGED AS A DIMER OF DIMERS. |
-Components
#1: Protein | Mass: 13950.796 Da / Num. of mol.: 4 / Mutation: H35Q Source method: isolated from a genetically manipulated source Source: (gene. exp.) Pseudomonas aeruginosa (bacteria) / References: UniProt: P00282 #2: Chemical | ChemComp-CU / #3: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 2.33 Å3/Da / Density % sol: 47.22 % | ||||||||||||||||||||||||||||||
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Crystal grow | *PLUS Method: vapor diffusion / PH range low: 5.7 / PH range high: 5.5 | ||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Radiation | Scattering type: x-ray |
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Radiation wavelength | Relative weight: 1 |
Reflection | *PLUS Highest resolution: 2.09 Å / Lowest resolution: 9999 Å / Num. obs: 22537 / % possible obs: 66.6 % / Num. measured all: 99146 / Rmerge(I) obs: 0.097 |
Reflection shell | *PLUS Highest resolution: 2.09 Å / Lowest resolution: 2.14 Å / % possible obs: 21.6 % |
-Processing
Software |
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Refinement | Rfactor Rwork: 0.163 / Highest resolution: 2.1 Å | ||||||||||||
Refinement step | Cycle: LAST / Highest resolution: 2.1 Å
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Refine LS restraints |
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Refinement | *PLUS Highest resolution: 2.1 Å / Num. reflection obs: 20747 / Rfactor obs: 0.163 / Lowest resolution: 8 Å | ||||||||||||
Solvent computation | *PLUS | ||||||||||||
Displacement parameters | *PLUS | ||||||||||||
Refine LS restraints | *PLUS
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