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- PDB-1def: PEPTIDE DEFORMYLASE CATALYTIC CORE (RESIDUES 1-147), NMR, 9 STRUCTURES -
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Open data
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Basic information
Entry | Database: PDB / ID: 1def | ||||||
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Title | PEPTIDE DEFORMYLASE CATALYTIC CORE (RESIDUES 1-147), NMR, 9 STRUCTURES | ||||||
![]() | PEPTIDE DEFORMYLASE | ||||||
![]() | HYDROLASE / ZINC METALLOPROTEASE | ||||||
Function / homology | ![]() co-translational protein modification / peptide deformylase / peptide deformylase activity / ferrous iron binding / ribosome binding / hydrolase activity / translation / zinc ion binding / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | SOLUTION NMR | ||||||
![]() | Meinnel, T. / Dardel, F. | ||||||
![]() | ![]() Title: A new subclass of the zinc metalloproteases superfamily revealed by the solution structure of peptide deformylase. Authors: Meinnel, T. / Blanquet, S. / Dardel, F. #1: ![]() Title: The C-Terminal Domain of Peptide Deformylase is Disordered and Dispensable for Activity Authors: Meinnel, T. / Lazennec, C. / Dardel, F. / Schmitter, J.M. / Blanquet, S. #2: ![]() Title: Mapping of the Active Site Zinc Ligands of Peptide Deformylase Authors: Meinnel, T. / Lazennec, C. / Blanquet, S. #3: ![]() Title: Evidence that Peptide Deformylase and Methionyl-tRNA(Fmet) Formyltransferase are Encoded within the Same Operon in Escherichia Coli Authors: Meinnel, T. / Blanquet, S. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 429.4 KB | Display | ![]() |
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PDB format | ![]() | 349.5 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 356 KB | Display | ![]() |
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Full document | ![]() | 516 KB | Display | |
Data in XML | ![]() | 49.1 KB | Display | |
Data in CIF | ![]() | 64.5 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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1 |
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NMR ensembles |
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Components
#1: Protein | Mass: 16661.125 Da / Num. of mol.: 1 / Fragment: ACTIVE CATALYTIC CORE, RESIDUES 1 - 147 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
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#2: Chemical | ChemComp-ZN / |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR |
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NMR details | Text: IN 20 MM POTASSIUM PHOSPHATE |
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Sample preparation
Sample conditions | pH: 7.2 / Temperature: 318 K |
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Crystal grow | *PLUS Method: other / Details: NMR |
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Processing
Software |
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NMR software | Name: ![]() | ||||||||||||
NMR ensemble | Conformers submitted total number: 9 |