+Open data
-Basic information
Entry | Database: PDB / ID: 7sf4 | ||||||
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Title | M. tb EgtD in complex with imatinib | ||||||
Components | Histidine N-alpha-methyltransferase | ||||||
Keywords | TRANSFERASE / Ergothioneine biosynthesis pathway / Rossmann fold domain / histidine binding site / SAM dependent methyltransferase | ||||||
Function / homology | Function and homology information ergothioneine biosynthetic process / L-histidine Nalpha-methyltransferase / : / aminoacyl-tRNA ligase activity / protein methyltransferase activity / methylation Similarity search - Function | ||||||
Biological species | Mycobacterium tuberculosis (bacteria) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.39 Å | ||||||
Authors | Sudasinghe, T.D. / Ronning, D.R. | ||||||
Funding support | United States, 1items
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Citation | Journal: Sci Rep / Year: 2021 Title: Inhibitors of Mycobacterium tuberculosis EgtD target both substrate binding sites to limit hercynine production. Authors: Sudasinghe, T.D. / Banco, M.T. / Ronning, D.R. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 7sf4.cif.gz | 259.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb7sf4.ent.gz | 209.2 KB | Display | PDB format |
PDBx/mmJSON format | 7sf4.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 7sf4_validation.pdf.gz | 1.1 MB | Display | wwPDB validaton report |
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Full document | 7sf4_full_validation.pdf.gz | 1.1 MB | Display | |
Data in XML | 7sf4_validation.xml.gz | 25.9 KB | Display | |
Data in CIF | 7sf4_validation.cif.gz | 35.9 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/sf/7sf4 ftp://data.pdbj.org/pub/pdb/validation_reports/sf/7sf4 | HTTPS FTP |
-Related structure data
Related structure data | 7scfC 7sewC 7sexC 7seyC 7sf5C 4uy5S S: Starting model for refinement C: citing same article (ref.) |
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Similar structure data |
-Links
-Assembly
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS domain:
NCS domain segments: Ens-ID: 1
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