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Yorodumi- PDB-1uh5: Crystal Structure of Enoyl-ACP Reductase with Triclosan at 2.2ang... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1uh5 | ||||||
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Title | Crystal Structure of Enoyl-ACP Reductase with Triclosan at 2.2angstroms | ||||||
Components | enoyl-ACP reductaseEnoyl-acyl carrier protein reductase | ||||||
Keywords | OXIDOREDUCTASE / FabI / Triclosan / P.falciparum / Enoyl-ACP reductase / NAD+ | ||||||
Function / homology | Function and homology information enoyl-[acyl-carrier-protein] reductase (NADH) activity / fatty acid biosynthetic process / nucleotide binding Similarity search - Function | ||||||
Biological species | Plasmodium falciparum (malaria parasite P. falciparum) | ||||||
Method | X-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 2.2 Å | ||||||
Authors | Swarnamukhi, P.L. / Kapoor, M. / Surolia, N. / Surolia, A. / Suguna, K. | ||||||
Citation | Journal: J.Mol.Biol. / Year: 2004 Title: Structural basis for the variation in triclosan affinity to enoyl reductases. Authors: Pidugu, L.S. / Kapoor, M. / Surolia, N. / Surolia, A. / Suguna, K. #1: Journal: Biochem.J. / Year: 2004 Title: Kinetic and structural analysis of the increased affinity of enoyl-ACP (acyl-carrier protein) reductase for triclosan in the presence of NAD+ Authors: Kapoor, M. / Swarnamukhi, P.L. / Surolia, N. / Suguna, K. / Surolia, A. | ||||||
History |
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Remark 750 | TURN Determination method: author determined |
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1uh5.cif.gz | 130.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1uh5.ent.gz | 99.2 KB | Display | PDB format |
PDBx/mmJSON format | 1uh5.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/uh/1uh5 ftp://data.pdbj.org/pub/pdb/validation_reports/uh/1uh5 | HTTPS FTP |
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-Related structure data
Related structure data | 1v35C 1enoS S: Starting model for refinement C: citing same article (ref.) |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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Details | The functional tetramer is generated by the two fold axis: -y+a, -x+b, -z+c/2 |
-Components
#1: Protein | Mass: 37244.184 Da / Num. of mol.: 2 / Fragment: residues 96-424 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Plasmodium falciparum (malaria parasite P. falciparum) Gene: FabI / Plasmid: pET28a(+) / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21 DE3 References: UniProt: Q6LFB9, UniProt: Q9BJJ9*PLUS, enoyl-[acyl-carrier-protein] reductase (NADH) #2: Chemical | #3: Chemical | #4: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.87 Å3/Da / Density % sol: 56.8 % |
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, hanging drop / pH: 5.6 Details: sodium acetate, Ammonium sulfate, pH 5.6, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K |
-Data collection
Diffraction | Mean temperature: 298 K |
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Diffraction source | Source: ROTATING ANODE / Type: RIGAKU / Wavelength: 1.5418 Å |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Oct 21, 2002 / Details: osmic mirrors |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.2→20 Å / Num. obs: 37772 / % possible obs: 97.8 % / Observed criterion σ(I): 0 / Redundancy: 7.2 % / Biso Wilson estimate: 26 Å2 / Rmerge(I) obs: 0.101 / Rsym value: 0.109 / Net I/σ(I): 20.2 |
Reflection shell | Resolution: 2.2→2.28 Å / Redundancy: 7 % / Rmerge(I) obs: 0.358 / Mean I/σ(I) obs: 7.8 / Rsym value: 0.388 / % possible all: 99.3 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 1ENO Resolution: 2.2→17.21 Å / Rfactor Rfree error: 0.004 / Data cutoff high absF: 543563.28 / Data cutoff low absF: 0 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 0 / Stereochemistry target values: Engh & Huber
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Solvent computation | Solvent model: FLAT MODEL / Bsol: 84.3064 Å2 / ksol: 0.390794 e/Å3 | ||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 35.9 Å2
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 2.2→17.21 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.2→2.34 Å / Rfactor Rfree error: 0.012 / Total num. of bins used: 6
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Xplor file |
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