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- PDB-2b3l: Crystal structure of type I human methionine aminopeptidase in th... -
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Open data
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Basic information
Entry | Database: PDB / ID: 2b3l | ||||||
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Title | Crystal structure of type I human methionine aminopeptidase in the apo form | ||||||
![]() | Methionine aminopeptidase 1 | ||||||
![]() | HYDROLASE / methionine aminopeptidase / human / metalloprotease / pitabread fold | ||||||
Function / homology | ![]() N-terminal protein amino acid modification / peptidyl-methionine modification / initiator methionyl aminopeptidase activity / methionyl aminopeptidase / metalloexopeptidase activity / metalloaminopeptidase activity / protein maturation / aminopeptidase activity / cytosolic ribosome / platelet aggregation ...N-terminal protein amino acid modification / peptidyl-methionine modification / initiator methionyl aminopeptidase activity / methionyl aminopeptidase / metalloexopeptidase activity / metalloaminopeptidase activity / protein maturation / aminopeptidase activity / cytosolic ribosome / platelet aggregation / Inactivation, recovery and regulation of the phototransduction cascade / regulation of translation / proteolysis / metal ion binding / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Addlagatta, A. / Hu, X. / Liu, J.O. / Matthews, B.W. | ||||||
![]() | ![]() Title: Structural Basis for the Functional Differences between Type I and Type II Human Methionine Aminopeptidases(,). Authors: Addlagatta, A. / Hu, X. / Liu, J.O. / Matthews, B.W. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 161.4 KB | Display | ![]() |
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PDB format | ![]() | 125.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 2b3hC ![]() 2b3kC ![]() 1yj3S C: citing same article ( S: Starting model for refinement |
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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: 36935.926 Da / Num. of mol.: 1 / Fragment: residues 81-384 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() | ||||
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#2: Chemical | ChemComp-K / | ||||
#3: Chemical | #4: Chemical | ChemComp-ACY / | #5: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.38 Å3/Da / Density % sol: 48.23 % |
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, hanging drop / pH: 6 Details: PEG 2000, potassium chloride, hepes, sodium chloride, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC QUANTUM 210 / Detector: CCD / Date: Jul 6, 2004 / Details: Double Crystal Si(111) |
Radiation | Monochromator: Double Crystal Si(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 1.5→50 Å / Num. all: 51841 / Num. obs: 51841 / % possible obs: 95.1 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Rmerge(I) obs: 0.031 / Χ2: 0.992 |
Reflection shell | Resolution: 1.5→1.55 Å / % possible obs: 82.3 % / Rmerge(I) obs: 0.128 / Num. measured obs: 4470 / Χ2: 0.976 / % possible all: 83.3 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB Entry 1YJ3 Resolution: 1.5→50 Å / σ(F): 0 / σ(I): 0 / Stereochemistry target values: Engh & Huber
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Displacement parameters | Biso mean: 25.8 Å2 | ||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.5→50 Å
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