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Open data
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Basic information
| Entry | Database: PDB / ID: 1mbf | ||||||
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| Title | MOUSE C-MYB DNA-BINDING DOMAIN REPEAT 1 | ||||||
Components | MYB PROTO-ONCOGENE PROTEIN | ||||||
Keywords | DNA BINDING PROTEIN / PROTOONCOGENE PRODUCT | ||||||
| Function / homology | Function and homology informationpositive regulation of testosterone secretion / skeletal muscle cell proliferation / myeloid cell development / positive regulation of hepatic stellate cell proliferation / negative regulation of hematopoietic progenitor cell differentiation / positive regulation of hepatic stellate cell activation / positive regulation of transforming growth factor beta production / T-helper 2 cell differentiation / homeostasis of number of cells / cellular response to leukemia inhibitory factor ...positive regulation of testosterone secretion / skeletal muscle cell proliferation / myeloid cell development / positive regulation of hepatic stellate cell proliferation / negative regulation of hematopoietic progenitor cell differentiation / positive regulation of hepatic stellate cell activation / positive regulation of transforming growth factor beta production / T-helper 2 cell differentiation / homeostasis of number of cells / cellular response to leukemia inhibitory factor / embryonic digestive tract development / myeloid cell differentiation / spleen development / stem cell division / positive regulation of glial cell proliferation / cellular response to interleukin-6 / thymus development / WD40-repeat domain binding / positive regulation of collagen biosynthetic process / response to ischemia / cellular response to retinoic acid / B cell differentiation / negative regulation of megakaryocyte differentiation / in utero embryonic development / positive regulation of smooth muscle cell proliferation / erythrocyte differentiation / RNA polymerase II transcription regulator complex / G1/S transition of mitotic cell cycle / positive regulation of miRNA transcription / cellular response to hydrogen peroxide / calcium ion transport / positive regulation of neuron apoptotic process / regulation of gene expression / mitotic cell cycle / DNA-binding transcription activator activity, RNA polymerase II-specific / response to hypoxia / DNA-binding transcription factor activity, RNA polymerase II-specific / RNA polymerase II cis-regulatory region sequence-specific DNA binding / DNA-binding transcription factor activity / negative regulation of DNA-templated transcription / regulation of DNA-templated transcription / positive regulation of DNA-templated transcription / negative regulation of transcription by RNA polymerase II / positive regulation of transcription by RNA polymerase II / DNA binding / DNA-templated transcription / nucleoplasm / nucleus / cytosol Similarity search - Function | ||||||
| Biological species | ![]() | ||||||
| Method | SOLUTION NMR | ||||||
Authors | Ogata, K. / Morikawa, S. / Nakamura, H. / Hojo, H. / Yoshimura, S. / Zhang, R. / Aimoto, S. / Ametani, Y. / Hirata, Z. / Sarai, A. ...Ogata, K. / Morikawa, S. / Nakamura, H. / Hojo, H. / Yoshimura, S. / Zhang, R. / Aimoto, S. / Ametani, Y. / Hirata, Z. / Sarai, A. / Ishii, S. / Nishimura, Y. | ||||||
Citation | Journal: Nat.Struct.Biol. / Year: 1995Title: Comparison of the free and DNA-complexed forms of the DNA-binding domain from c-Myb. Authors: Ogata, K. / Morikawa, S. / Nakamura, H. / Hojo, H. / Yoshimura, S. / Zhang, R. / Aimoto, S. / Ametani, Y. / Hirata, Z. / Sarai, A. / Ishii, S. / Nishimura, Y. #1: Journal: Cell(Cambridge,Mass.) / Year: 1994Title: Solution Structure of a Specific DNA Complex of the Myb DNA-Binding Domain with Cooperative Recognition Helices Authors: Ogata, K. / Morikawa, S. / Nakamura, H. / Sekikawa, A. / Inoue, T. / Kanai, H. / Sarai, A. / Ishii, S. / Nishimura, Y. #2: Journal: Proc.Natl.Acad.Sci.USA / Year: 1992Title: Solution Structure of a DNA-Binding Unit of Myb: A Helix-Turn-Helix-Related Motif with Conserved Tryptophans Forming a Hydrophobic Core Authors: Ogata, K. / Hojo, H. / Aimoto, S. / Nakai, T. / Nakamura, H. / Sarai, A. / Ishii, S. / Nishimura, Y. | ||||||
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Structure visualization
| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 1mbf.cif.gz | 850.6 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb1mbf.ent.gz | 714.4 KB | Display | PDB format |
| PDBx/mmJSON format | 1mbf.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/mb/1mbf ftp://data.pdbj.org/pub/pdb/validation_reports/mb/1mbf | HTTPS FTP |
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-Related structure data
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Links
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Assembly
| Deposited unit | ![]()
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| NMR ensembles |
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Components
| #1: Protein | Mass: 6317.113 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Details: GENE C-MYB, NMR, 50 STRUCTURES; ENGINEERED / Source: (natural) ![]() |
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| Has protein modification | Y |
-Experimental details
-Experiment
| Experiment | Method: SOLUTION NMR |
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Sample preparation
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| Crystal grow | *PLUS Method: other / Details: NMR |
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Processing
| Software | Name: AMBER / Classification: refinement | |||||||||
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| Refinement | Software ordinal: 1 Details: A TOTAL OF 50 STRUCTURES WERE CALCULATED. THE COORDINATES OF THE RESTRAINED MINIMIZED AVERAGED STRUCTURE WERE OBTAINED BY AVERAGING THE COORDINATES OF THE INDIVIDUAL STRUCTURES, AND THEN BY ...Details: A TOTAL OF 50 STRUCTURES WERE CALCULATED. THE COORDINATES OF THE RESTRAINED MINIMIZED AVERAGED STRUCTURE WERE OBTAINED BY AVERAGING THE COORDINATES OF THE INDIVIDUAL STRUCTURES, AND THEN BY SUBJECTING THE RESULTING COORDINATES TO THE RESTRAINED ENERGY MINIMIZATION BY PRESTO. | |||||||||
| NMR ensemble | Conformers submitted total number: 50 |
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