+Open data
-Basic information
Entry | Database: PDB / ID: 1lxa | ||||||
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Title | UDP N-ACETYLGLUCOSAMINE ACYLTRANSFERASE | ||||||
Components | UDP N-ACETYLGLUCOSAMINE O-ACYLTRANSFERASE | ||||||
Keywords | ACYLTRANSFERASE / TRANSFERASE / LIPID A BIOSYNTHESIS / LIPID SYNTHESIS | ||||||
Function / homology | Function and homology information acyl-[acyl-carrier-protein]-UDP-N-acetylglucosamine O-acyltransferase / acyl-[acyl-carrier-protein]-UDP-N-acetylglucosamine O-acyltransferase activity / lipid A biosynthetic process / identical protein binding / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | Escherichia coli (E. coli) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 2.6 Å | ||||||
Authors | Roderick, S.L. | ||||||
Citation | Journal: Science / Year: 1995 Title: A left-handed parallel beta helix in the structure of UDP-N-acetylglucosamine acyltransferase. Authors: Raetz, C.R. / Roderick, S.L. #1: Journal: Proteins / Year: 1995 Title: Crystallization of Udp N-Acetylglucosamine O-Acyltransferase from Escherichia Coli Authors: Pfitzner, U. / Raetz, C.R.H. / Roderick, S.L. | ||||||
History |
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Remark 650 | HELIX DETERMINATION METHOD: AUTHOR DETERMINED | ||||||
Remark 700 | SHEET DETERMINATION METHOD: AUTHOR DETERMINED |
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1lxa.cif.gz | 59.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1lxa.ent.gz | 44.4 KB | Display | PDB format |
PDBx/mmJSON format | 1lxa.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1lxa_validation.pdf.gz | 365.6 KB | Display | wwPDB validaton report |
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Full document | 1lxa_full_validation.pdf.gz | 376.9 KB | Display | |
Data in XML | 1lxa_validation.xml.gz | 7.9 KB | Display | |
Data in CIF | 1lxa_validation.cif.gz | 11.2 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/lx/1lxa ftp://data.pdbj.org/pub/pdb/validation_reports/lx/1lxa | HTTPS FTP |
-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 28117.018 Da / Num. of mol.: 1 / Mutation: S64Q, V65F, D125H Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / Strain: K12 / Gene: LPXA / Plasmid: PSR1 / Gene (production host): LPXA / Production host: Escherichia coli (E. coli) References: UniProt: P0A722, acyl-[acyl-carrier-protein]-UDP-N-acetylglucosamine O-acyltransferase |
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Compound details | MET 1 THROUGH ILE 186 COMPRISES THE LEFT-HANDED BETA-HELICAL DOMAIN WITH TWO LOOP EXCURSIONS |
-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: 57.21 % | ||||||||||||||||||
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Crystal | *PLUS Density % sol: 57 % | ||||||||||||||||||
Crystal grow | *PLUS Method: vapor diffusion, hanging drop / PH range low: 6.8 / PH range high: 6.2 | ||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction source | Wavelength: 1.5418 Å |
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Detector | Type: SIEMENS / Detector: AREA DETECTOR / Date: 1995 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.6→99 Å / Num. obs: 8868 / % possible obs: 87 % / Observed criterion σ(I): 0 / Redundancy: 10 % / Rmerge(I) obs: 0.08 |
Reflection | *PLUS Num. measured all: 79727 / Rmerge(I) obs: 0.08 |
-Processing
Software |
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Refinement | Resolution: 2.6→99 Å / Isotropic thermal model: KNOWLEDGE-BASED / σ(F): 0 / Stereochemistry target values: TNT SUPPLIED
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Solvent computation | Solvent model: TWO PARAMETER RECIPROCAL SPACE / Bsol: 250 Å2 / ksol: 0.874 e/Å3 | ||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.6→99 Å
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Refine LS restraints |
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Software | *PLUS Name: X-PLOR/TNT / Classification: refinement | ||||||||||||||||||||
Refinement | *PLUS Rfactor all: 0.184 | ||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||
Displacement parameters | *PLUS |