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- PDB-3t5a: Crystal structure of N-terminal domain of FAAL28 G330W mutant fro... -
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Open data
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Basic information
Entry | Database: PDB / ID: 3t5a | ||||||
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Title | Crystal structure of N-terminal domain of FAAL28 G330W mutant from Mycobacterium tuberculosis | ||||||
![]() | Long-chain-fatty-acid--AMP ligase FadD28 | ||||||
![]() | LIGASE / Acetyl-CoA synthetase like fold / AMP-binding | ||||||
Function / homology | ![]() long-chain fatty acid adenylyltransferase FadD28 / Dimycocersyl phthiocerol biosynthesis / adenylyltransferase activity / symbiont-mediated suppression of host innate immune response / fatty-acyl-CoA synthase activity / response to host immune response / biological process involved in interaction with host / DIM/DIP cell wall layer assembly / lipid biosynthetic process / ligase activity ...long-chain fatty acid adenylyltransferase FadD28 / Dimycocersyl phthiocerol biosynthesis / adenylyltransferase activity / symbiont-mediated suppression of host innate immune response / fatty-acyl-CoA synthase activity / response to host immune response / biological process involved in interaction with host / DIM/DIP cell wall layer assembly / lipid biosynthetic process / ligase activity / fatty acid biosynthetic process / ATP binding / plasma membrane / cytosol 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 | ![]() | 104.6 KB | Display | ![]() |
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PDB format | ![]() | 77.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 428.6 KB | Display | ![]() |
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Full document | ![]() | 440.6 KB | Display | |
Data in XML | ![]() | 21.6 KB | Display | |
Data in CIF | ![]() | 31.7 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 3t5bC ![]() 3t5cC ![]() 3e53S 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
#1: Protein | Mass: 52073.285 Da / Num. of mol.: 1 / Fragment: N-terminal domain (UNP RESIDUES 1-460) / Mutation: G330W Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() References: UniProt: P96290, UniProt: P9WQ59*PLUS, Ligases; Forming carbon-sulfur bonds; Acid-thiol ligases |
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#2: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.04 Å3/Da / Density % sol: 39.79 % |
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Crystal grow | Temperature: 277 K / Method: vapor diffusion, hanging drop / pH: 6.3 Details: 18% PEG 3350, 0.1M Sodium MES, 5% ethylene glycol, 0.15M Lithium sulphate, pH 6.3, VAPOR DIFFUSION, HANGING DROP, temperature 277K |
-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: Nov 28, 2008 / 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: 2.05→25 Å / Num. obs: 25902 / % possible obs: 92.9 % / Observed criterion σ(I): 2 / Redundancy: 4.7 % / Biso Wilson estimate: 31.69 Å2 / Rmerge(I) obs: 0.098 / Net I/σ(I): 14.63 |
Reflection shell | Resolution: 2.05→2.12 Å / Redundancy: 4.4 % / Rmerge(I) obs: 0.486 / Mean I/σ(I) obs: 2.03 / Num. unique all: 2564 / % possible all: 94 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 3E53 Resolution: 2.05→25 Å / σ(F): 2
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Displacement parameters |
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Refinement step | Cycle: LAST / Resolution: 2.05→25 Å
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