[English] 日本語
Yorodumi- PDB-4me6: Crystal structure of D-alanine-D-alanine ligase A from Xanthomona... -
+Open data
-Basic information
Entry | Database: PDB / ID: 4me6 | ||||||
---|---|---|---|---|---|---|---|
Title | Crystal structure of D-alanine-D-alanine ligase A from Xanthomonas oryzae pathovar oryzae with ADP | ||||||
Components | D-alanine--D-alanine ligase | ||||||
Keywords | LIGASE / ADP-depending enzyme / d-alanine-d-alanine ligase / Nucleotide binding | ||||||
Function / homology | Function and homology information D-alanine-D-alanine ligase / D-alanine-D-alanine ligase activity / peptidoglycan biosynthetic process / cell wall organization / regulation of cell shape / ATP binding / metal ion binding / cytoplasm Similarity search - Function | ||||||
Biological species | Xanthomonas oryzae pv. oryzae (bacteria) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.1 Å | ||||||
Authors | Doan, T.T.N. / Kim, J.K. / Ahn, Y.J. / Lee, B.M. / Kang, L.W. | ||||||
Citation | Journal: Arch.Biochem.Biophys. / Year: 2014 Title: Crystal structures of d-alanine-d-alanine ligase from Xanthomonas oryzae pv. oryzae alone and in complex with nucleotides Authors: Doan, T.N.N. / Kim, J.K. / Ngo, H.P.T. / Tran, H.T. / Cha, S.S. / Chung, K.M. / Huynh, K.H. / Ahn, Y.J. / Kang, L.W. | ||||||
History |
|
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
---|
-Downloads & links
-Download
PDBx/mmCIF format | 4me6.cif.gz | 85.4 KB | Display | PDBx/mmCIF format |
---|---|---|---|---|
PDB format | pdb4me6.ent.gz | 61.1 KB | Display | PDB format |
PDBx/mmJSON format | 4me6.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 4me6_validation.pdf.gz | 775.4 KB | Display | wwPDB validaton report |
---|---|---|---|---|
Full document | 4me6_full_validation.pdf.gz | 778.9 KB | Display | |
Data in XML | 4me6_validation.xml.gz | 16.1 KB | Display | |
Data in CIF | 4me6_validation.cif.gz | 23.1 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/me/4me6 ftp://data.pdbj.org/pub/pdb/validation_reports/me/4me6 | HTTPS FTP |
-Related structure data
Related structure data | 4l1kC 3e5nS S: Starting model for refinement C: citing same article (ref.) |
---|---|
Similar structure data |
-Links
-Assembly
Deposited unit |
| ||||||||
---|---|---|---|---|---|---|---|---|---|
1 |
| ||||||||
Unit cell |
|
-Components
#1: Protein | Mass: 41945.777 Da / Num. of mol.: 1 / Mutation: M327V Source method: isolated from a genetically manipulated source Source: (gene. exp.) Xanthomonas oryzae pv. oryzae (bacteria) Strain: KACC10331 / Gene: ddlA, ddl, XOO0352 / Plasmid: pET11a / Production host: Escherichia coli (E. coli) / References: UniProt: Q5H614, D-alanine-D-alanine ligase |
---|---|
#2: Chemical | ChemComp-MG / |
#3: Chemical | ChemComp-ADP / |
#4: Water | ChemComp-HOH / |
Sequence details | RESIDUES 1-21 ARE PART OF THE MATURE PROTEIN ACCORDING TO DATABASE GI:122879012 (PROTEIN REF YP_198991.6). |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
---|
-Sample preparation
Crystal | Density Matthews: 2.03 Å3/Da / Density % sol: 39.38 % |
---|---|
Crystal grow | Temperature: 287 K / Method: vapor diffusion, sitting drop / pH: 8.5 Details: 15% (w/v) PEG 4000, 0.1M Tris (pH 8.5), 0.2M MgCl2, 0.3M dimethylethyl-(3-sulfopropyl)-ammonium, VAPOR DIFFUSION, SITTING DROP, temperature 287K |
-Data collection
Diffraction | Mean temperature: 200 K |
---|---|
Diffraction source | Source: SYNCHROTRON / Site: SPring-8 / Beamline: BL32XU |
Detector | Type: ADSC QUANTUM 210 / Detector: CCD |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Relative weight: 1 |
Reflection | Resolution: 2.1→50 Å / Num. obs: 20817 / % possible obs: 99.5 % |
Reflection shell | Resolution: 2.1→2.14 Å / Redundancy: 6.3 % / Mean I/σ(I) obs: 8.9 / Rsym value: 0.61 / % possible all: 98.9 |
-Processing
Software |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 3E5N Resolution: 2.1→38.32 Å / Cor.coef. Fo:Fc: 0.942 / Cor.coef. Fo:Fc free: 0.9 / SU B: 5.619 / SU ML: 0.147 / Cross valid method: THROUGHOUT / ESU R: 0.255 / ESU R Free: 0.211 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 26.426 Å2
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.1→38.32 Å
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints |
|