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- PDB-4e6u: Structure of LpxA from Acinetobacter baumannii at 1.4A resolution... -
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Open data
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Basic information
Entry | Database: PDB / ID: 4e6u | ||||||
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Title | Structure of LpxA from Acinetobacter baumannii at 1.4A resolution (P63 form) | ||||||
![]() | Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase | ||||||
![]() | TRANSFERASE / lipopolysaccaride synthesis | ||||||
Function / homology | ![]() Udp N-acetylglucosamine O-acyltransferase; Domain 2 / Udp N-acetylglucosamine O-acyltransferase, C-terminal domain / Hexapeptide repeat proteins / UDP N-Acetylglucosamine Acyltransferase; domain 1 / 3 Solenoid / Up-down Bundle / Mainly Beta / Mainly Alpha Similarity search - Domain/homology | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Badger, J. / Chie-Leon, B. / Logan, C. / Sridhar, V. / Sankaran, B. / Zwart, P.H. / Nienaber, V. | ||||||
![]() | ![]() Title: Structure determination of LpxA from the lipopolysaccharide-synthesis pathway of Acinetobacter baumannii. Authors: Badger, J. / Chie-Leon, B. / Logan, C. / Sridhar, V. / Sankaran, B. / Zwart, P.H. / Nienaber, V. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 71.3 KB | Display | ![]() |
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PDB format | ![]() | 52.4 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 451.2 KB | Display | ![]() |
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Full document | ![]() | 451.7 KB | Display | |
Data in XML | ![]() | 14.9 KB | Display | |
Data in CIF | ![]() | 22.5 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related 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: 28472.334 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() References: UniProt: F0QHB3, UniProt: A0A7U4DSW1*PLUS, acyl-[acyl-carrier-protein]-UDP-N-acetylglucosamine O-acyltransferase | ||||
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#2: Chemical | #3: Chemical | ChemComp-EDO / #4: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.46 Å3/Da / Density % sol: 64.49 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 7.5 Details: 2ul of 25mg/ml protein, 2uL of 1.8M LiSO4, 0.1M Hepes 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: RAYONIX MX-225 / Detector: CCD / Date: Nov 6, 2010 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.979 Å / Relative weight: 1 |
Reflection | Resolution: 1.41→50 Å / Num. all: 73881 / Num. obs: 73881 / % possible obs: 99.8 % / Observed criterion σ(I): -4 / Redundancy: 11.3 % / Rmerge(I) obs: 0.064 / Net I/σ(I): 36.1 |
Reflection shell | Resolution: 1.41→1.46 Å / Redundancy: 11.2 % / Rmerge(I) obs: 0.591 / Mean I/σ(I) obs: 5 / Num. unique all: 63291 / % possible all: 99.8 |
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Processing
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Refinement | Method to determine structure: 4E6T / Resolution: 1.41→36.09 Å / Cor.coef. Fo:Fc: 0.97 / Cor.coef. Fo:Fc free: 0.968 / SU B: 0.758 / SU ML: 0.031 / Cross valid method: THROUGHOUT / ESU R: 0.049 / ESU R Free: 0.05 / Stereochemistry target values: MAXIMUM LIKELIHOOD
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: MASK | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 20.799 Å2
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Refinement step | Cycle: LAST / Resolution: 1.41→36.09 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.412→1.449 Å / Total num. of bins used: 20
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