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- PDB-1rr2: Propionibacterium shermanii transcarboxylase 5S subunit bound to ... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1rr2 | |||||||||
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Title | Propionibacterium shermanii transcarboxylase 5S subunit bound to 2-ketobutyric acid | |||||||||
![]() | transcarboxylase 5S subunit | |||||||||
![]() | TRANSFERASE / TIM-barrel / carbamylated lysine / transcarboxylase / cobalt / 2-ketobutyric acid | |||||||||
Function / homology | ![]() methylmalonyl-CoA carboxytransferase / methylmalonyl-CoA carboxytransferase activity / metal ion binding Similarity search - Function | |||||||||
Biological species | ![]() | |||||||||
Method | ![]() | |||||||||
![]() | Hall, P.R. / Zheng, R. / Antony, L. / Pusztai-Carey, M. / Carey, P.R. / Yee, V.C. | |||||||||
![]() | ![]() Title: Transcarboxylase 5S structures: assembly and catalytic mechanism of a multienzyme complex subunit. Authors: Hall, P.R. / Zheng, R. / Antony, L. / Pusztai-Carey, M. / Carey, P.R. / Yee, V.C. #1: Journal: Acta Crystallogr.,Sect.D / Year: 2004 Title: Expression and crystallization of several forms of the Propionibacterium shermanii transcarboxylase 5S subunit. Authors: Hall, P.R. / Zheng, R. / Pusztai-Carey, M. / van den Akker, F. / Carey, P.R. / Yee, V.C. | |||||||||
History |
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Remark 999 | SEQUENCE RESIDUE 184 EXISTS IN TWO ALTERNATE CONFORMATIONS: KCX, CARBAMYLATED LYSINE, AND LYS. |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 115.3 KB | Display | ![]() |
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PDB format | ![]() | 85.5 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 460 KB | Display | ![]() |
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Full document | ![]() | 467.1 KB | Display | |
Data in XML | ![]() | 22.4 KB | Display | |
Data in CIF | ![]() | 32.1 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1rqbSC ![]() 1rqeC ![]() 1rqhC ![]() 1s3hC ![]() 1u5jC ![]() 1s27 S: Starting model for refinement C: citing same article ( |
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Similar 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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Components on special symmetry positions |
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Components
#1: Protein | Mass: 59652.465 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Details: RESIDUE 184 EXISTS IN TWO ALTERNATE CONFORMATIONS: KCX AND LYS Source: (gene. exp.) ![]() Gene: 5S / Plasmid: pETBlue-2 / Production host: ![]() ![]() References: GenBank: 38304072, UniProt: Q70AC7*PLUS, methylmalonyl-CoA carboxytransferase |
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#2: Chemical | ChemComp-CO / |
#3: Chemical | ChemComp-2KT / |
#4: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.32 Å3/Da / Density % sol: 46.93 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, sitting drop / pH: 7 Details: PEG 4000, Tris , pH 7.0, VAPOR DIFFUSION, SITTING DROP, temperature 293K |
-Data collection
Diffraction | Mean temperature: 95 K |
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Diffraction source | Source: ![]() |
Detector | Type: RIGAKU RAXIS IV / Detector: IMAGE PLATE / Date: Jun 9, 2003 |
Radiation | Monochromator: Yale mirrors / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2→30 Å / Num. all: 37787 / Num. obs: 32291 / % possible obs: 85.5 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 7.6 % / Biso Wilson estimate: 18.6 Å2 / Rmerge(I) obs: 0.084 / Net I/σ(I): 22 |
Reflection shell | Resolution: 2→2.07 Å / Rmerge(I) obs: 0.233 / Mean I/σ(I) obs: 4.5 / % possible all: 71.8 |
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Processing
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Refinement | Method to determine structure: Isomorphous replacement Starting model: 1RQB Resolution: 2→27.29 Å / Rfactor Rfree error: 0.005 / Data cutoff high absF: 309498.23 / Data cutoff low absF: 0 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 0 / Stereochemistry target values: Engh & Huber Details: RESIDUE 184 EXISTS IN TWO ALTERNATE CONFORMATIONS: KCX AND LYS.
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Solvent computation | Solvent model: FLAT MODEL / Bsol: 40.2082 Å2 / ksol: 0.312023 e/Å3 | ||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 35.1 Å2
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 2→27.29 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2→2.13 Å / Rfactor Rfree error: 0.017 / Total num. of bins used: 6
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Xplor file |
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