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Open data
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Basic information
Entry | Database: PDB / ID: 2byy | ||||||
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Title | E.coli KAS I H298E Mutation | ||||||
![]() | 3-OXOACYL-[ACYL-CARRIER-PROTEIN] SYNTHASE I | ||||||
![]() | TRANSFERASE / ACYLTRANSFERASE / CLAISEN CONDENSATION / FATTY ACID BIOSYNTHESIS / FATTY ACID SYNTHASE / THIOLASE FOLD | ||||||
Function / homology | ![]() monounsaturated fatty acid biosynthetic process / beta-ketoacyl-[acyl-carrier-protein] synthase I / 3-oxoacyl-[acyl-carrier-protein] synthase activity / fatty acid biosynthetic process / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Olsen, J.G. / von Wettstein-Knowles, P. / Henriksen, A. | ||||||
![]() | ![]() Title: Fatty acid synthesis. Role of active site histidines and lysine in Cys-His-His-type beta-ketoacyl-acyl carrier protein synthases. Authors: von Wettstein-Knowles, P. / Olsen, J.G. / McGuire, K.A. / Henriksen, A. #1: ![]() Title: Structures of Beta-Ketoacyl-Acyl Carrier Protein Synthase I Complexed with Fatty Acids Elucidate its Catalytic Machinery Authors: Olsen, J.G. / Kadziola, A. / von Wettstein-Knowles, P. / Siggaard-Andersen, M. / Larsen, S. #2: Journal: Biochemistry / Year: 2001 Title: Beta-Ketoacyl-Acyl Carrier Protein Synthase I of Escherichia Coli: Aspects of the Condensation Mechanism Revealed by Analyses of Mutations in the Active Site Pocket Authors: Mcguire, K.A. / Siggaard-Andersen, M. / Bangera, M.G. / Olsen, J.G. / von Wettstein-Knowles, P. #3: ![]() Title: The X-Ray Crystal Structure of Beta-Ketoacyl Acyl Carrier Protein Synthase I Authors: Olsen, J.G. / Kadziola, A. / von Wettstein-Knowles, P. / Siggaard-Andersen, M. / Lindquist, Y. / Larsen, 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 | ![]() | 308.9 KB | Display | ![]() |
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PDB format | ![]() | 249.4 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 448.4 KB | Display | ![]() |
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Full document | ![]() | 479.6 KB | Display | |
Data in XML | ![]() | 63.6 KB | Display | |
Data in CIF | ![]() | 89.1 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1h4fC ![]() 2buhC ![]() 2buiC ![]() 2bywC ![]() 2byxC ![]() 2byzC ![]() 2bz3C ![]() 2bz4C ![]() 1ek4S 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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2 | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 44052.688 Da / Num. of mol.: 4 / Mutation: YES Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() References: UniProt: P14926, UniProt: P0A953*PLUS, beta-ketoacyl-[acyl-carrier-protein] synthase I #2: Chemical | ChemComp-NH4 / #3: Water | ChemComp-HOH / | Sequence details | N-TERMINAL HIS-TAG MRGSHHHHHH | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.4 Å3/Da / Density % sol: 48 % |
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Crystal grow | pH: 6 Details: 1.9 M (NH4)2SO4, 2 % PEG400, 0.1 M BISTRIS-PROPANE PH 6.0 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARRESEARCH / Detector: CCD / Date: Oct 2, 2004 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.095 Å / Relative weight: 1 |
Reflection | Resolution: 2.2→32.5 Å / Num. obs: 215468 / % possible obs: 88.2 % / Observed criterion σ(I): 0 / Redundancy: 2.9 % / Biso Wilson estimate: 8.3 Å2 / Rmerge(I) obs: 0.11 / Net I/σ(I): 5 |
Reflection shell | Resolution: 2.2→2.32 Å / Redundancy: 2.3 % / Rmerge(I) obs: 0.16 / Mean I/σ(I) obs: 4.4 / % possible all: 72.7 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 1EK4 Resolution: 2.2→32.49 Å / Rfactor Rfree error: 0.004 / Data cutoff high absF: 3321850.59 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 0 / Stereochemistry target values: MLF
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Solvent computation | Solvent model: FLAT MODEL / Bsol: 37.5874 Å2 / ksol: 0.40115 e/Å3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 18 Å2
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 2.2→32.49 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.2→2.34 Å / Rfactor Rfree error: 0.014 / Total num. of bins used: 6
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