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- PDB-1cri: THE ROLE OF A CONSERVED INTERNAL WATER MOLECULE AND ITS ASSOCIATE... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1cri | ||||||
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Title | THE ROLE OF A CONSERVED INTERNAL WATER MOLECULE AND ITS ASSOCIATED HYDROGEN BOND NETWORK IN CYTOCHROME C | ||||||
![]() | CYTOCHROME C | ||||||
![]() | ELECTRON TRANSPORT(CYTOCHROME) | ||||||
Function / homology | ![]() Release of apoptotic factors from the mitochondria / Pyroptosis / Respiratory electron transport / Detoxification of Reactive Oxygen Species / mitochondrial electron transport, cytochrome c to oxygen / mitochondrial electron transport, ubiquinol to cytochrome c / : / mitochondrial intermembrane space / electron transfer activity / heme binding ...Release of apoptotic factors from the mitochondria / Pyroptosis / Respiratory electron transport / Detoxification of Reactive Oxygen Species / mitochondrial electron transport, cytochrome c to oxygen / mitochondrial electron transport, ubiquinol to cytochrome c / : / mitochondrial intermembrane space / electron transfer activity / heme binding / mitochondrion / metal ion binding Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Berghuis, A.M. / Brayer, G.D. | ||||||
![]() | ![]() Title: The role of a conserved internal water molecule and its associated hydrogen bond network in cytochrome c. Authors: Berghuis, A.M. / Guillemette, J.G. / McLendon, G. / Sherman, F. / Smith, M. / Brayer, G.D. #1: ![]() Title: Mutation of Tyrosine-67 in Cytochrome C Significantly Alters the Local Heme Environment Authors: Berghuis, A.M. / Guillemette, G.J. / Smith, M. / Brayer, G.D. #2: ![]() Title: Effect of the Asn 52-> Ile Mutation on the Redox Potential of Yeast Cytochrome C: Theory and Experiment Authors: Langen, R. / Brayer, G.D. / Berghuis, A.M. / Mclendon, G. / Sherman, F. / Warshel, A. #3: ![]() Title: Oxidation State-Dependent Conformational Changes in Cytochrome C Authors: Berghuis, A.M. / Brayer, G.D. #4: ![]() Title: Enhanced Thermodynamic Stabilities of Yeast Iso-1-Cytochrome C with Amino Acid Replacements at Position 52 and 102 Authors: Hickey, D.R. / Berghuis, A.M. / Lafond, G. / Jaeger, J.A. / Cardillo, T.S. / Mclendon, D. / Das, G. / Sherman, F. / Brayer, G.D. / Mclendon, G. #5: ![]() Title: Effects of Reaction Free Energy in Biological Electron Transfer in Vitro and in Vivo (in: Electron Transfer in Inorganic, Organic, and Biological Systems) Authors: Mclendon, G. / Hickey, D.R. / Berghuis, A.M. / Sherman, F. / Brayer, G.D. #6: ![]() Title: High-Resolution Refinement of Yeast Iso-1-Cytochrome C and Comparisons with Other Eukaryotic Cytochrome C Authors: Louie, G.V. / Brayer, G.D. #7: ![]() Title: Crystallization of Yeast Iso-2-Cytochrome C Using a Novel Hair Seeding Technique Authors: Leung, C.J. / Nall, B.T. / Brayer, G.D. | ||||||
History |
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Remark 650 | HELIX THE END OF THE 50 HELIX (RESIDUE 55) IS DISTORTED. | ||||||
Remark 700 | SHEET RESIDUES IN SHEET S1 FORM A HIGHLY DISTORTED BETA TYPE CONFORMATION. |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 32.8 KB | Display | ![]() |
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PDB format | ![]() | 25.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 816.5 KB | Display | ![]() |
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Full document | ![]() | 820.3 KB | Display | |
Data in XML | ![]() | 8.1 KB | Display | |
Data in CIF | ![]() | 9.9 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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Links
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Assembly
Deposited unit | ![]()
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1 |
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Unit cell |
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Atom site foot note | 1: THE HEME GROUP IS COVALENTLY ATTACHED TO THE PROTEIN VIA THIOETHER BONDS TO THE SG ATOMS OF CYS 14 AND CYS 17. |
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Components
#1: Protein | Mass: 12096.931 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Gene: POTENTIAL / References: UniProt: P00044 |
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#2: Chemical | ChemComp-SO4 / |
#3: Chemical | ChemComp-HEM / |
#4: Water | ChemComp-HOH / |
Compound details | THIS PROTEIN HAS BEEN STABILIZED FOR ANALYSES BY THE MUTATION OF CYSTEINE 102 TO A THREONINE ...THIS PROTEIN HAS BEEN STABILIZED |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 1.92 Å3/Da / Density % sol: 35.85 % | ||||||||||||||||||||||||
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Crystal grow | *PLUS Method: vapor diffusion, hanging drop / Details: using a hair-seeding / PH range low: 6.4 / PH range high: 6 | ||||||||||||||||||||||||
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 Å / Num. obs: 4771 / Num. measured all: 12907 / Rmerge(I) obs: 0.063 |
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Processing
Software | Name: PROLSQ / Classification: refinement | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Refinement | Rfactor obs: 0.181 / Highest resolution: 2 Å | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Highest resolution: 2 Å
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Refine LS restraints |
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Software | *PLUS Name: PROLSQ / Classification: refinement | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Highest resolution: 2 Å / Num. reflection obs: 4538 / Rfactor obs: 0.181 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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