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- PDB-1o78: Biotin carboxyl carrier domain of transcarboxylase (1.3S) [10-48]... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1o78 | ||||||
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Title | Biotin carboxyl carrier domain of transcarboxylase (1.3S) [10-48] deletion mutant | ||||||
![]() | BIOTIN CARBOXYL CARRIER PROTEIN OF METHYLMALONYL-COA CARBOXYL-TRANSFERASE | ||||||
![]() | CARRIER PROTEIN / TRANSCARBOXYLASE / CARBOXYL CARRIER / TRANSFERASE | ||||||
Function / homology | ![]() methylmalonyl-CoA carboxytransferase / methylmalonyl-CoA carboxytransferase activity Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | SOLUTION NMR / DISTANCE GEOMETRY, SIMULATED ANNEALING | ||||||
![]() | Jank, M.M. / Sadowsky, J.D. / Peikert, C. / Berger, S. | ||||||
![]() | ![]() Title: NMR Studies on the Solution Structure of a Deletion Mutant of the Transcarboxylase Biotin Carrier Subunit Authors: Jank, M.M. / Sadowsky, J.D. / Peikert, C. / Berger, S. #1: ![]() Title: High Resolution Solution Structure of the 1.3S Subunit of Transcarboxylase from Propionibacterium Shermanii(Dagger) Authors: Reddy, D.V. / Shenoy, B.C. / Carey, P.R. / Sonnichsen, F.D. #2: Journal: Protein Expr.Purif. / Year: 1999 Title: Expression and Biotinylation of a Mutant of the Transcarboxylase Carrier Protein from Propioni Shermanii Authors: Jank, M.M. / Bokorny, S. / Roehm, K.-H. / Berger, S. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 490 KB | Display | ![]() |
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PDB format | ![]() | 410.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 346.1 KB | Display | ![]() |
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Full document | ![]() | 499.2 KB | Display | |
Data in XML | ![]() | 29.1 KB | Display | |
Data in CIF | ![]() | 46.1 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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NMR ensembles |
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Components
#1: Protein | Mass: 8667.160 Da / Num. of mol.: 1 / Mutation: YES Source method: isolated from a genetically manipulated source Details: RESIDUES 10-48 DELETION MUTANT Source: (gene. exp.) ![]() Plasmid: PTAC1.3DELTA10-48, PCY216 / Production host: ![]() ![]() |
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Compound details | BIOTINYL 1.3S SUBUNIT (CHAIN A) SERVES AS A CARBOXYL CARRIER BETWEEN THE SUBSTRATE BINDING SITES ON ...BIOTINYL 1.3S SUBUNIT (CHAIN A) SERVES AS A CARBOXYL CARRIER BETWEEN THE SUBSTRATE BINDING SITES ON THE 12S AND 5S SUBUNITS. TRANSCARBO |
Sequence details | RESIDUES 10-48 DELETION MUTANT |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||||||||||||||||||||||||||
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NMR experiment |
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NMR details | Text: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR SPECTROSCOPY ON 13C, 15N-LABELED PROTEIN. BIOTIN WAS UNLABELED AND NOT INCLUDED IN THE STRUCTURE CALCULATION. |
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Sample preparation
Details | Contents: 2.3 MM PROTEIN, N15/C13 LABELED TC 1.3S [10-48], BIOTIN (UNLABELED) COVALENTLY ATTACHED TO LYS 89 |
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Sample conditions | Ionic strength: 2 MM AMMONIUM ACETATE / pH: 4.5 / Pressure: 1 atm / Temperature: 300 K |
Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
NMR spectrometer | Type: Bruker DRX / Manufacturer: Bruker / Model: DRX / Field strength: 600 MHz |
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Processing
NMR software |
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Refinement | Method: DISTANCE GEOMETRY, SIMULATED ANNEALING / Software ordinal: 1 Details: DGSA, REFINEMENT WITH NOES AND HYDROGEN-BOND CONSTRAINTS | ||||||||||||||||||||
NMR ensemble | Conformer selection criteria: LEAST RESTRAINT VIOLATION / Conformers calculated total number: 600 / Conformers submitted total number: 20 |