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Open data
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Basic information
Entry | Database: PDB / ID: 3cyt | ||||||||||||
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Title | REDOX CONFORMATION CHANGES IN REFINED TUNA CYTOCHROME C | ||||||||||||
![]() | CYTOCHROME C![]() | ||||||||||||
![]() | ELECTRON TRANSPORT (HEME PROTEIN) | ||||||||||||
Function / homology | ![]() ![]() ![]() ![]() ![]() ![]() Similarity search - Function | ||||||||||||
Biological species | ![]() ![]() | ||||||||||||
Method | ![]() | ||||||||||||
![]() | Takano, T. | ||||||||||||
![]() | ![]() Title: Redox conformation changes in refined tuna cytochrome c. Authors: Takano, T. / Dickerson, R.E. #1: ![]() Title: Conformation Change of Cytochrome C. I. Ferrocytochrome C Structure Refined at 1.5 Angstroms Resolution Authors: Takano, T. / Dickerson, R.E. #2: ![]() Title: Conformation Change of Cytochrome C. II. Ferricytochrome C Refinement at 1.8 Angstroms and Comparison with the Ferrocytochrome Structure Authors: Takano, T. / Dickerson, R.E. #3: ![]() Title: Cytochrome C and the Evolution of Energy Metabolism Authors: Dickerson, R.E. #4: ![]() Title: Internal Mobility of Ferrocytochrome C Authors: Northrup, S.H. / Pear, M.R. / Mccammon, J.A. / Karplus, M. / Takano, T. #5: ![]() Title: Tuna Cytochrome C at 2.0 Angstroms Resolution. II. Ferrocytochrome Structure Analysis Authors: Takano, T. / Trus, B.L. / Mandel, N. / Mandel, G. / Kallai, O.B. / Swanson, R. / Dickerson, R.E. #6: ![]() Title: Tuna Cytochrome C at 2.0 Angstroms Resolution. I. Ferricytochrome Structure Analysis Authors: Swanson, R. / Trus, B.L. / Mandel, N. / Mandel, G. / Kallai, O.B. / Dickerson, R.E. #7: ![]() Title: The Structure of Ferrocytochrome C at 2.45 Angstroms Resolution Authors: Takano, T. / Kallai, O.B. / Swanson, R. / Dickerson, R.E. #8: ![]() Title: The Structure and History of an Ancient Protein Authors: Dickerson, R.E. | ||||||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 52.6 KB | Display | ![]() |
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PDB format | ![]() | 42.5 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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1 | ![]()
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2 | ![]()
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS oper: (Code: given Matrix: (-0.3944, -0.9189, -0.0029), Vector ![]() Details | THE TRANSFORMATION WHICH WILL PLACE THE COORDINATES OF THE OXIDIZED OUTER MOLECULE INTO BEST ALIGNMENT WITH THOSE OF THE OXIDIZED INNER MOLECULE IS GIVEN IN THE MTRIX RECORDS BELOW. THE TRANSFORMATION WHICH WILL PLACE THE COORDINATES OF THE REDUCED MOLECULE (4CYT) INTO BEST ALIGNMENT WITH THOSE OF THE OXIDIZED INNER MOLECULE IN THE SPACE OF THE LATTER IS GIVEN BELOW .2868 .8127 -.5072 47.2662 .5553 -.5724 -.6033 17.5577 -.7806 -.1086 -.6155 16.3160 | |
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Components
#1: Protein | ![]() Mass: 11416.114 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() #2: Chemical | ![]() #3: Water | ChemComp-HOH / | ![]() |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.2 Å3/Da / Density % sol: 44.11 % |
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Crystal grow![]() | *PLUS Method: otherDetails: Takano, T., (1973) J. Biol. Chem., 248, 5234., Swanson, R., (1977) J. Biol. Chem., 252, 759. |
-Data collection
Reflection | *PLUS Highest resolution: 1.8 Å / Num. obs: 16831 |
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Processing
Refinement | Highest resolution: 1.8 Å | ||||||||||||
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Refinement step | Cycle: LAST / Highest resolution: 1.8 Å
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Refinement | *PLUS Rfactor obs: 0.208 | ||||||||||||
Solvent computation | *PLUS | ||||||||||||
Displacement parameters | *PLUS |