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- PDB-3t5c: Crystal structure of N-terminal domain of FACL13 from Mycobacteri... -
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Open data
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Basic information
Entry | Database: PDB / ID: 3t5c | ||||||
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Title | Crystal structure of N-terminal domain of FACL13 from Mycobacterium tuberculosis in different space group C2 | ||||||
![]() | PROBABLE CHAIN-FATTY-ACID-CoA LIGASE FADD13 | ||||||
![]() | LIGASE / Acetyl-CoA synthetase like fold / AMP-binding | ||||||
Function / homology | ![]() long-chain-fatty-acid-CoA ligase / medium-chain fatty acid-CoA ligase activity / long-chain fatty acid-CoA ligase activity / fatty acid biosynthetic process / ATP binding / plasma membrane Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Goyal, A. / Sankaranarayanan, R. | ||||||
![]() | ![]() Title: Molecular basis of the functional divergence of fatty acyl-AMP ligase biosynthetic enzymes of Mycobacterium tuberculosis. Authors: Goyal, A. / Verma, P. / Anandhakrishnan, M. / Gokhale, R.S. / Sankaranarayanan, R. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 166.6 KB | Display | ![]() |
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PDB format | ![]() | 131.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 437.5 KB | Display | ![]() |
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Full document | ![]() | 453.4 KB | Display | |
Data in XML | ![]() | 34.8 KB | Display | |
Data in CIF | ![]() | 50.6 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 3t5aC ![]() 3t5bSC C: citing same article ( S: Starting model for refinement |
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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: 42841.777 Da / Num. of mol.: 2 / Fragment: N-terminal domain (UNP RESIDUES 1-396) Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() References: UniProt: O53306, UniProt: P9WQ36*PLUS, Ligases; Forming carbon-sulfur bonds; Acid-thiol ligases #2: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.22 Å3/Da / Density % sol: 44.51 % |
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Crystal grow | Temperature: 295 K / Method: vapor diffusion, hanging drop / pH: 7.5 Details: 25% PEG 3350, 0.1M Na-HEPES, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 295K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() |
Detector | Type: MAR scanner 345 mm plate / Detector: IMAGE PLATE / Date: Jan 18, 2009 / Details: Osmic mirrors |
Radiation | Monochromator: Ni FILTER / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.09→25 Å / Num. obs: 43434 / % possible obs: 97.8 % / Observed criterion σ(I): 2 / Redundancy: 2.2 % / Rmerge(I) obs: 0.043 / Net I/σ(I): 19.17 |
Reflection shell | Resolution: 2.09→2.16 Å / Redundancy: 2.1 % / Rmerge(I) obs: 0.321 / Mean I/σ(I) obs: 2 / Num. unique all: 4209 / % possible all: 96.3 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 3T5B Resolution: 2.09→25 Å / σ(F): 2
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Displacement parameters |
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Refinement step | Cycle: LAST / Resolution: 2.09→25 Å
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