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- PDB-2pia: PHTHALATE DIOXYGENASE REDUCTASE: A MODULAR STRUCTURE FOR ELECTRON... -
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Open data
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Basic information
Entry | Database: PDB / ID: 2pia | ||||||
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Title | PHTHALATE DIOXYGENASE REDUCTASE: A MODULAR STRUCTURE FOR ELECTRON TRANSFER FROM PYRIDINE NUCLEOTIDES TO [2FE-2S] | ||||||
![]() | PHTHALATE DIOXYGENASE REDUCTASE | ||||||
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Function / homology | ![]() ![]() ![]() ![]() Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Correll, C.C. / Batie, C.J. / Ballou, D.P. / Ludwig, M.L. | ||||||
![]() | ![]() Title: Phthalate dioxygenase reductase: a modular structure for electron transfer from pyridine nucleotides to [2Fe-2S]. Authors: Correll, C.C. / Batie, C.J. / Ballou, D.P. / Ludwig, M.L. #1: ![]() Title: Crystallographic Characterization of Phthalate Oxygenase Reductase, an Iron-Sulfur Flavoprotein from Pseudomonas Cepacia Authors: Correll, C.C. / Batie, C.J. / Ballou, D.P. / Ludwig, M.L. #2: ![]() Title: Structure Determination of an Iron-Sulfur Flavoprotein Authors: Correll, C.C. / Ludwig, M.L. #3: ![]() Title: Phthalate Dioxygenase Reductase and Related Flavin-Iron-Sulfur Containing Electron Transferases Authors: Batie, C.J. / Ballou, D.P. / Correll, C.C. | ||||||
History |
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Remark 700 | SHEET ASSIGNMENTS OF SECONDARY STRUCTURE ARE BASED ON THE ALGORITHM OF KABSCH AND SANDER. ...SHEET ASSIGNMENTS OF SECONDARY STRUCTURE ARE BASED ON THE ALGORITHM OF KABSCH AND SANDER. EXCEPTIONS: STRANDS 3 AND 4 OF BETA SHEET 2 IN WHICH THE KABSCH AND SANDER ALGORITHM INDICATED BREAKS. THE CLOSED SHEET (BETA BARREL) IS INDICATED BY HAVING THE FIRST AND LAST STRANDS IDENTICAL -THE FIRST STRAND APPEARS FIRST AND LAST. THE FMN HYDROGEN BONDS BETWEEN STRANDS 3 AND 4 TO CLOSE THE BARREL. |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 79.3 KB | Display | ![]() |
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PDB format | ![]() | 59.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
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: 35579.844 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() References: UniProt: P33164, ![]() |
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#2: Chemical | ChemComp-FMN / ![]() |
#3: Chemical | ChemComp-FES / ![]() |
#4: Water | ChemComp-HOH / ![]() |
Sequence details | THE SEQUENCE IS DEDUCED FROM THE DNA SEQUENCE DETERMINED BY R. LIU AND G. ZYLSTRA, ABS. ANN. ...THE SEQUENCE IS DEDUCED FROM THE DNA SEQUENCE DETERMINED |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.75 Å3/Da / Density % sol: 55.31 % |
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Crystal grow![]() | *PLUS Method: other / Details: Correll, C.C., (1985) J. Biol. Chem., 260, 14633. |
-Data collection
Reflection | *PLUS Highest resolution: 2 Å / Num. obs: 23943 / % possible obs: 93 % / Rmerge(I) obs: 0.062 |
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Processing
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Refinement | Resolution: 2→10 Å /
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Refinement step | Cycle: LAST / Resolution: 2→10 Å
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Refinement | *PLUS Rfactor obs: 0.186 | ||||||||||||
Solvent computation | *PLUS | ||||||||||||
Displacement parameters | *PLUS | ||||||||||||
Refine LS restraints | *PLUS
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