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Open data
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Basic information
Entry | Database: PDB / ID: 1dcz | ||||||
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Title | BIOTIN CARBOXYL CARRIER DOMAIN OF TRANSCARBOXYLASE (TC 1.3S) | ||||||
![]() | TRANSCARBOXYLASE 1.3S SUBUNIT | ||||||
![]() | TRANSFERASE / ANTIPARALLEL BETA SHEET / HAMMERHEAD / BIOCYTIN | ||||||
Function / homology | ![]() methylmalonyl-CoA carboxytransferase / methylmalonyl-CoA carboxytransferase activity Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | SOLUTION NMR / DISTANCE GEOMETRY, SIMULATED ANNEALING HYBRID METHOD | ||||||
Model type details | minimized average | ||||||
![]() | Reddy, D.V. / Shenoy, B.C. / Carey, P.R. / Sonnichsen, F.D. | ||||||
![]() | ![]() Title: High resolution solution structure of the 1.3S subunit of transcarboxylase from Propionibacterium shermanii. Authors: Reddy, D.V. / Shenoy, B.C. / Carey, P.R. / Sonnichsen, F.D. #1: ![]() Title: Structural Characterization of the Entire 1.3S Subunit of Transcarboxylase from Propionibacterium shermanii Authors: Reddy, D.V. / Rothemund, S. / Shenoy, B.C. / Carey, P.R. / Sonnichsen, F.D. #2: ![]() Title: Absence of Observable Biotin-Protein Interactions in the 1.3S Subunit of Transcarboxylase: An NMR Study Authors: Reddy, D.V. / Shenoy, B.C. / Carey, P.R. / Sonnichsen, F.D. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 31.8 KB | Display | ![]() |
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PDB format | ![]() | 21.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related 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: 7822.057 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Species: Propionibacterium freudenreichii / Strain: subsp. shermanii / Production host: ![]() ![]() References: UniProt: P02904, methylmalonyl-CoA carboxytransferase |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||
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NMR experiment |
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NMR details | Text: BIOTIN ATTACHED TO LYS 89 WAS OMITTED FROM COORDINATES. RESIDUES 1-46 APPEARED UNSTRUCTURED, OMITTED FROM CALCULATIONS AND COORDINATES. |
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Sample preparation
Details |
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Sample conditions | Ionic strength: 0 / pH: 6.7 / Pressure: 1 atm / Temperature: 20 K | ||||||||
Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
NMR spectrometer |
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Processing
NMR software |
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Refinement | Method: DISTANCE GEOMETRY, SIMULATED ANNEALING HYBRID METHOD Software ordinal: 1 Details: DG_SUB_EMBED, DGSA, REFINE WITH DIRECT J-REFINEMENT | ||||||||||||||||||||
NMR representative | Selection criteria: minimized average structure | ||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with acceptable covalent geometry Conformers calculated total number: 50 / Conformers submitted total number: 1 |