+Open data
-Basic information
Entry | Database: PDB / ID: 1m1l | ||||||
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Title | Human Suppressor of Fused (N-terminal domain) | ||||||
Components | Suppressor of Fused | ||||||
Keywords | SIGNALING PROTEIN / Gene regulation / Hedgehog signaling / signal transduction / fused | ||||||
Function / homology | Function and homology information smoothened signaling pathway involved in ventral spinal cord interneuron specification / smoothened signaling pathway involved in spinal cord motor neuron cell fate specification / positive regulation of cellular response to drug / GLI-SUFU complex / ciliary tip / coronary vasculature development / aorta development / ventricular septum development / skin development / ciliary base ...smoothened signaling pathway involved in ventral spinal cord interneuron specification / smoothened signaling pathway involved in spinal cord motor neuron cell fate specification / positive regulation of cellular response to drug / GLI-SUFU complex / ciliary tip / coronary vasculature development / aorta development / ventricular septum development / skin development / ciliary base / negative regulation of protein import into nucleus / negative regulation of osteoblast differentiation / heart looping / spermatid development / Hedgehog 'off' state / negative regulation of ubiquitin-dependent protein catabolic process / negative regulation of smoothened signaling pathway / neural tube closure / Degradation of GLI1 by the proteasome / Hedgehog 'on' state / Degradation of GLI2 by the proteasome / GLI3 is processed to GLI3R by the proteasome / negative regulation of DNA-binding transcription factor activity / beta-catenin binding / transcription corepressor activity / regulation of DNA-templated transcription / protein kinase binding / negative regulation of transcription by RNA polymerase II / signal transduction / nucleoplasm / nucleus / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / SAD / Resolution: 2.65 Å | ||||||
Authors | Merchant, M. / Vajdos, F.F. / Ultsch, M. / Maun, H.R. / Wendt, U. / Cannon, J. / Lazarus, R.A. / de Vos, A.M. / de Sauvage, F.J. | ||||||
Citation | Journal: Mol.Cell.Biol. / Year: 2004 Title: Suppressor of fused regulates Gli activity through a dual binding mechanism Authors: Merchant, M. / Vajdos, F.F. / Ultsch, M. / Maun, H.R. / Wendt, U. / Cannon, J. / Desmarais, W. / Lazarus, R.A. / de Vos, A.M. / de Sauvage, F.J. | ||||||
History |
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Remark 300 | BIOMOLECULE: 1 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT REMARK 300 WHICH CONSISTS ... BIOMOLECULE: 1 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT REMARK 300 WHICH CONSISTS OF 4 CHAIN(S). AUTHOR STATES THAT BIOLOGICAL UNIT IS UNKNOWN. |
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1m1l.cif.gz | 197.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1m1l.ent.gz | 160.7 KB | Display | PDB format |
PDBx/mmJSON format | 1m1l.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1m1l_validation.pdf.gz | 452.9 KB | Display | wwPDB validaton report |
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Full document | 1m1l_full_validation.pdf.gz | 476.3 KB | Display | |
Data in XML | 1m1l_validation.xml.gz | 40.7 KB | Display | |
Data in CIF | 1m1l_validation.cif.gz | 56.1 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/m1/1m1l ftp://data.pdbj.org/pub/pdb/validation_reports/m1/1m1l | HTTPS FTP |
-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 26592.730 Da / Num. of mol.: 4 / Fragment: N-terminal domain (Residues 27-262) Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Plasmid: pST-239 / Production host: Escherichia coli (E. coli) / References: UniProt: Q9UMX1 #2: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 3.94 Å3/Da / Density % sol: 68.77 % | |||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 279 K / Method: vapor diffusion, hanging drop / pH: 6 Details: 1 M LiCl, 0.1 M NaCitrate pH 5.0- 6.0, 10% w/v PEG 6000, VAPOR DIFFUSION, HANGING DROP, temperature 279K | |||||||||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS pH: 7.5 / Method: vapor diffusion, hanging drop | |||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: SSRL / Beamline: BL9-2 / Wavelength: 1 Å |
Detector | Type: ADSC QUANTUM 4 / Detector: CCD / Date: May 15, 2001 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 2.65→29.81 Å / Num. all: 48643 / Num. obs: 48643 / % possible obs: 99.2 % / Observed criterion σ(I): -3 |
Reflection | *PLUS Lowest resolution: 99 Å / Redundancy: 9.1 % / Num. measured all: 441505 / Rmerge(I) obs: 0.094 |
Reflection shell | *PLUS Highest resolution: 2.65 Å / Lowest resolution: 2.7 Å / % possible obs: 100 % / Rmerge(I) obs: 0.362 |
-Processing
Software |
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Refinement | Method to determine structure: SAD / Resolution: 2.65→29.81 Å / Cross valid method: THROUGHOUT / σ(F): 0 / Stereochemistry target values: Engh & Huber
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Refinement step | Cycle: LAST / Resolution: 2.65→29.81 Å
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Refinement | *PLUS % reflection Rfree: 8 % / Rfactor Rfree: 0.256 / Rfactor Rwork: 0.224 | ||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||
Refine LS restraints | *PLUS
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