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- PDB-9rub: CRYSTAL STRUCTURE OF ACTIVATED RIBULOSE-1,5-BISPHOSPHATE CARBOXYL... -
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Open data
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Basic information
Entry | Database: PDB / ID: 9rub | ||||||
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Title | CRYSTAL STRUCTURE OF ACTIVATED RIBULOSE-1,5-BISPHOSPHATE CARBOXYLASE COMPLEXED WITH ITS SUBSTRATE, RIBULOSE-1,5-BISPHOSPHATE | ||||||
![]() | RIBULOSE-1,5-BISPHOSPHATE CARBOXYLASE | ||||||
![]() | 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 | ![]() | ||||||
![]() | Lundqvist, T. / Schneider, G. | ||||||
![]() | ![]() Title: Crystal structure of activated ribulose-1,5-bisphosphate carboxylase complexed with its substrate, ribulose-1,5-bisphosphate. Authors: Lundqvist, T. / Schneider, G. #1: ![]() Title: Comparison of the Crystal Structures of L2 and L8S8 Rubisco Suggests a Functional Role for the Small Subunit Authors: Schneider, G. / Knight, S. / Andersson, I. / Lindqvist, Y. / Lundqvist, T. / Branden, C.-I. #2: ![]() Title: Crystallographic Refinement and Structure of Ribulose-1,5-Bisphosphate Carboxylase from Rhodospirillum Rubrum at 1.7 Angstroms Resolution Authors: Schneider, G. / Lindqvist, Y. / Lundqvist, T. #3: ![]() Title: Crystal Structure of the Complex of Ribulose-1,5-Bisphosphate Carboxylase and a Transition State Analogue, 2-Carboxy-D-Arabinitol 1,5-Bisphosphate Authors: Lundqvist, T. / Schneider, G. #4: ![]() Title: Crystal Structure of the Binary Complex of Ribulose-1,5-Bisphosphate Carboxylase and its Product, 3-Phospho-D-Glycerate Authors: Lundqvist, T. / Schneider, G. #5: ![]() Title: Three-Dimensional Structure of Ribulose-1,5-Bisphosphate Carboxylase(Slash) Oxygenase from Rhodospirillum Rubrum at 2.9 Angstroms Resolution Authors: Schneider, G. / Lindqvist, Y. / Branden, C.-I. / Lorimer, G. | ||||||
History |
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Remark 700 | SHEET SHEETS *ACT* AND *BCT* PRESENTED BELOW ARE ACTUALLY EIGHT-STRANDED BETA/ALPHA BARRELS. THESE ...SHEET SHEETS *ACT* AND *BCT* PRESENTED BELOW ARE ACTUALLY EIGHT-STRANDED BETA/ALPHA BARRELS. THESE ARE REPRESENTED AS NINE-STRANDED SHEETS 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 | ![]() | 185.7 KB | Display | ![]() |
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PDB format | ![]() | 147.6 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 480.7 KB | Display | ![]() |
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Full document | ![]() | 607 KB | Display | |
Data in XML | ![]() | 35.4 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: RESIDUES PRO A 167 AND B 167 ARE CIS PROLINES. 2: RESIDUES LYS A 191 AND LYS B 191 ARE CARBAMYLATED AT THE EPSILON-AMINO GROUP. | ||||||||
Noncrystallographic symmetry (NCS) | NCS oper: (Code: given Matrix: (0.37374, -0.056007, 0.940855), Vector: Details | THE TRANSFORMATION GIVEN ON THE *MTRIX* RECORDS BELOW WILL YIELD APPROXIMATE COORDINATES FOR CHAIN *A* WHEN APPLIED TO COORDINATES OF CHAIN *B*. RESIDUES 422 - 450 WERE OMITTED WHEN GENERATING THIS TRANSFORMATION MATRIX. | |
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Components
#1: Protein | Mass: 50538.918 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() References: UniProt: P04718, ribulose-bisphosphate carboxylase #2: Sugar | #3: Chemical | #4: Chemical | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.38 Å3/Da / Density % sol: 48.29 % | ||||||||||||||||||||||||||||||
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Crystal grow | *PLUS Temperature: 4, 20 ℃ / Method: microdialysis / PH range low: 5.8 / PH range high: 5 | ||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Reflection | *PLUS Highest resolution: 2.6 Å / Num. obs: 25502 / % possible obs: 82 % / Num. measured all: 47847 / Rmerge(I) obs: 0.083 |
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Processing
Software | Name: PROLSQ / Classification: refinement | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Refinement | Rfactor obs: 0.199 / Highest resolution: 2.6 Å Details: RESIDUES A 191 AND B 191 ARE MODIFIED LYSINES WHICH ARE CARBAMYLATED AT THE EPSILON-AMINO GROUP. THE CARBAMYL GROUPS ARE PRESENTED AS HET GROUPS *CBX* AT THE END OF CHAINS *A* AND *B*. | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Highest resolution: 2.6 Å
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Refine LS restraints |
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Software | *PLUS Name: X-PLOR/PROLSQ / Classification: refinement | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Lowest resolution: 10 Å / Rfactor obs: 0.199 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS Type: p_angle_d / Dev ideal: 2.6 |