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- PDB-2v3x: His243Ala Escherichia coli aminopeptidase P in complex with substrate -
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Open data
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Basic information
Entry | Database: PDB / ID: 2v3x | ||||||
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Title | His243Ala Escherichia coli aminopeptidase P in complex with substrate | ||||||
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![]() | HYDROLASE / 'PITA-BREAD' ENZYME / PROLINE- SPECIFIC ENZYME / AMINOPEPTIDASE P / MANGANESE ENZYME / PROTEASE / MANGANESE / METAL-BINDING / METALLOENZYME / AMINOPEPTIDASE / METALLOPROTEASE | ||||||
Function / homology | ![]() Xaa-Pro aminopeptidase / metalloexopeptidase activity / metalloaminopeptidase activity / aminopeptidase activity / manganese ion binding / protein homotetramerization / protein-containing complex / proteolysis / identical protein binding / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Graham, S.C. / Guss, J.M. | ||||||
![]() | ![]() Title: Complexes of Mutants of Escherichia Coli Aminopeptidase P and the Tripeptide Substrate Valproleu. Authors: Graham, S.C. / Guss, J.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 | ![]() | 119.9 KB | Display | ![]() |
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PDB format | ![]() | 91.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 432.4 KB | Display | ![]() |
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Full document | ![]() | 434 KB | Display | |
Data in XML | ![]() | 24.3 KB | Display | |
Data in CIF | ![]() | 38.3 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 2v3yC ![]() 2v3zC ![]() 1wl9S 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: 49692.992 Da / Num. of mol.: 1 / Mutation: YES Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() | ||||||||
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#2: Protein/peptide | Mass: 327.419 Da / Num. of mol.: 1 / Source method: obtained synthetically / Details: TRIPEPTIDE SUBSTRATE OF AMINOPEPTIDASE P / Source: (synth.) ![]() ![]() | ||||||||
#3: Chemical | #4: Chemical | ChemComp-CL / | #5: Water | ChemComp-HOH / | Compound details | ENGINEERED | Sequence details | H243A MUTANT | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 4.4 Å3/Da / Density % sol: 72 % Description: STARTING MODEL WAS STRIPPED OF LIGANDS, SOLVENT MOLECULES AND ALTERNATE CONFORMERS BEFORE REFINEMENT. |
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Crystal grow | Temperature: 277 K / Method: vapor diffusion, hanging drop / pH: 8.5 Details: CRYSTALLISED IN 30% PEG 4K, 0.1 M TRIS PH 8.5 AT 277K. SOAKED IN 30% PEG 4K, 0.1 M TRIS PH 8.5, 1 MM MNCL2, 5 MM VAL-PRO-LEU, 10% MPD FOR 30 MIN AT 277K IMMEDIATELY PRIOR TO DATA COLLECTION. |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC CCD / Detector: CCD / Date: Apr 23, 2006 / Details: MIRRORS |
Radiation | Monochromator: SILICON 111 / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.97934 Å / Relative weight: 1 |
Reflection | Resolution: 1.7→50 Å / Num. obs: 95461 / % possible obs: 97.7 % / Observed criterion σ(I): -3 / Redundancy: 4.6 % / Biso Wilson estimate: 21.96 Å2 / Rmerge(I) obs: 0.06 / Net I/σ(I): 20.9 |
Reflection shell | Resolution: 1.7→1.76 Å / Redundancy: 4.4 % / Rmerge(I) obs: 0.34 / Mean I/σ(I) obs: 4.4 / % possible all: 98.3 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 1WL9 Resolution: 1.7→30.06 Å / Cor.coef. Fo:Fc: 0.974 / Cor.coef. Fo:Fc free: 0.968 / SU B: 1.901 / SU ML: 0.034 / TLS residual ADP flag: LIKELY RESIDUAL / Cross valid method: THROUGHOUT / ESU R: 0.058 / ESU R Free: 0.058 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS.
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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: 13.51 Å2
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Refinement step | Cycle: LAST / Resolution: 1.7→30.06 Å
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Refine LS restraints |
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