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Open data
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Basic information
Entry | Database: PDB / ID: 2mzw | ||||||
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Title | Staphylococcus aureus FusB:EF-GC3 complex | ||||||
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![]() | TRANSLATION/ANTIBIOTIC RESISTANCE / antibiotic resistance / METAL BINDING PROTEIN / TRANSLATION-ANTIBIOTIC RESISTANCE complex | ||||||
Function / homology | ![]() ribosome disassembly / translation elongation factor activity / GTPase activity / GTP binding / metal ion binding / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | SOLUTION NMR / simulated annealing | ||||||
Model details | lowest energy, model1 | ||||||
![]() | Tomlinson, J.H. / Thompson, G.S. / Kalverda, A.P. / Zhuravleva, A. / O'Neill, A. | ||||||
![]() | ![]() Title: A target-protection mechanism of antibiotic resistance at atomic resolution: insights into FusB-type fusidic acid resistance. Authors: Tomlinson, J.H. / Thompson, G.S. / Kalverda, A.P. / Zhuravleva, A. / O'Neill, A.J. | ||||||
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 176.7 KB | Display | ![]() |
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PDB format | ![]() | 137.3 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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Assembly
Deposited unit | ![]()
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NMR ensembles |
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Components
#1: Protein | Mass: 33472.766 Da / Num. of mol.: 1 / Fragment: Domains III-V, residues 401-692 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Gene: CH51_02860, CH52_03020, DA92_03395, DP18_1097, EX97_02750, fusA, SAU060112_10722, SAXN108_0601, X998_0588 Production host: ![]() ![]() |
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#2: Protein | Mass: 27353.406 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
#3: Chemical | ChemComp-ZN / |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR Details: A structural model of the complex between the fusidic acid resistance protein FusB and a truncated form of EF-G. This model was produced using NMR data to dock X-ray structures. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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NMR experiment |
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Sample preparation
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