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Open data
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Basic information
Entry | Database: PDB / ID: 2aun | ||||||
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Title | Active site His285Ala mutant of LD-carboxypeptidase | ||||||
![]() | hypothetical protein | ||||||
![]() | HYDROLASE / LD-carboxypeptidase / peptidoglycan hydrolase / serine peptidase / serine-histidine-glutamate triad / nucleophilic elbow | ||||||
Function / homology | ![]() muramoyltetrapeptide carboxypeptidase activity / muramoyltetrapeptide carboxypeptidase / peptidoglycan turnover / peptidoglycan biosynthetic process / serine-type peptidase activity / cell wall organization / regulation of cell shape / proteolysis / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Korza, H.J. / Bochtler, M. | ||||||
![]() | ![]() Title: Pseudomonas aeruginosa LD-carboxypeptidase, a serine peptidase with a Ser-His-Glu triad and a nucleophilic elbow. Authors: Korza, H.J. / Bochtler, M. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 127.7 KB | Display | ![]() |
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PDB format | ![]() | 99.3 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 435.6 KB | Display | ![]() |
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Full document | ![]() | 439.2 KB | Display | |
Data in XML | ![]() | 25 KB | Display | |
Data in CIF | ![]() | 36.3 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1zrsSC ![]() 2aumC 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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Unit cell |
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Components
#1: Protein | Mass: 34570.285 Da / Num. of mol.: 2 / Mutation: H285A mutation Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() References: UniProt: Q9HTZ1, muramoyltetrapeptide carboxypeptidase #2: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 1.98 Å3/Da / Density % sol: 37 % |
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Crystal grow | Temperature: 294 K / Method: vapor diffusion, sitting drop / pH: 4.5 Details: citric acid, pH 4.5, VAPOR DIFFUSION, SITTING DROP, temperature 294K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Apr 11, 2005 / Details: Osmic Max-Flux |
Radiation | Monochromator: Osmic Max-Flux / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.54 Å / Relative weight: 1 |
Reflection | Resolution: 2.4→15 Å / Num. all: 21640 / Num. obs: 21640 / % possible obs: 99.3 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 3.1 % / Biso Wilson estimate: 23 Å2 / Rmerge(I) obs: 0.137 / Rsym value: 0.137 / Net I/σ(I): 7.8 |
Reflection shell | Resolution: 2.4→2.43 Å / Rmerge(I) obs: 0.363 / Mean I/σ(I) obs: 3.2 / Num. unique all: 822 / Rsym value: 0.363 / % possible all: 99.2 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 1ZRS Resolution: 2.4→15 Å / Cross valid method: THROUGHOUT / σ(F): 0 / Stereochemistry target values: Engh & Huber
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Refinement step | Cycle: LAST / Resolution: 2.4→15 Å
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