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- PDB-1rba: SUBSTITUTION OF ASP193 TO ASN AT THE ACTIVE SITE OF RIBULOSE-1,5-... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1rba | ||||||
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Title | SUBSTITUTION OF ASP193 TO ASN AT THE ACTIVE SITE OF RIBULOSE-1,5-BISPHOSPHATE CARBOXYLASE RESULTS IN CONFORMATIONAL CHANGES | ||||||
![]() | RUBISCO | ||||||
![]() | LYASE(CARBON-CARBON) | ||||||
Function / homology | ![]() ribulose-bisphosphate carboxylase / ribulose-bisphosphate carboxylase activity / reductive pentose-phosphate cycle / monooxygenase activity / magnesium ion binding Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() | ||||||
![]() | Schneider, G. / Soderlind, E. | ||||||
![]() | ![]() Title: Substitution of ASP193 to ASN at the active site of ribulose-1,5-bisphosphate carboxylase results in conformational changes. Authors: Soderlind, E. / Schneider, G. / Gutteridge, S. | ||||||
History |
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Remark 700 | SHEET THE SHEETS PRESENTED AS *ACT* AND *BCT* ON SHEET RECORDS BELOW ARE ACTUALLY EIGHT-STRANDED ...SHEET THE SHEETS PRESENTED AS *ACT* AND *BCT* ON SHEET RECORDS BELOW ARE ACTUALLY EIGHT-STRANDED BETA-BARRELS. THIS IS REPRESENTED BY A NINE-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL. |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 167 KB | Display | ![]() |
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PDB format | ![]() | 116.4 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 390.2 KB | Display | ![]() |
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Full document | ![]() | 578.2 KB | Display | |
Data in XML | ![]() | 42.1 KB | Display | |
Data in CIF | ![]() | 58.2 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-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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Atom site foot note | 1: CIS PROLINE - PRO A 167 / 2: CIS PROLINE - PRO B 167 | ||||||||
Noncrystallographic symmetry (NCS) | NCS oper: (Code: given Matrix: (0.37374, -0.056207, 0.940855), Vector: |
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Components
#1: Protein | Mass: 50537.934 Da / Num. of mol.: 2 / Mutation: D193N Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() References: UniProt: P04718, ribulose-bisphosphate carboxylase #2: Water | ChemComp-HOH / | Sequence details | SEQUENCE ADVISORY NOTICE: DIFFERENCE BETWEEN SWISS-PROT AND PDB SEQUENCE. SWISS-PROT ENTRY NAME: ...SEQUENCE ADVISORY NOTICE: DIFFERENCE | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.31 Å3/Da / Density % sol: 46.81 % | ||||||||||||||||||||||||||||||
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Crystal grow | *PLUS Temperature: 4,20 K / Method: microdialysis / PH range low: 5.8 / PH range high: 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: 2.6 Å / Num. obs: 23071 / Num. measured all: 57727 / Rmerge(I) obs: 0.093 |
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Processing
Software | Name: PROLSQ / Classification: refinement | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Refinement | Rfactor obs: 0.207 / Highest resolution: 2.6 Å | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Highest resolution: 2.6 Å
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Refine LS restraints |
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Software | *PLUS Name: PROLSQ / Classification: refinement | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Highest resolution: 2.6 Å / Lowest resolution: 6.5 Å / Rfactor obs: 0.207 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS |