+Open data
-Basic information
Entry | Database: PDB / ID: 1uuh | ||||||
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Title | Hyaluronan binding domain of human CD44 | ||||||
Components | CD44 ANTIGEN | ||||||
Keywords | LECTIN / HYALURONAN / EXTRACELLULAR MATRIX / RECEPTOR / LINK-DOMAIN / C- TYPE LECTIN / SUGAR-BINDING | ||||||
Function / homology | Function and homology information positive regulation of monocyte aggregation / Hyaluronan uptake and degradation / hyaluronic acid binding / monocyte aggregation / macrophage migration inhibitory factor receptor complex / regulation of lamellipodium morphogenesis / hyaluronan catabolic process / cellular response to fibroblast growth factor stimulus / positive regulation of heterotypic cell-cell adhesion / cartilage development ...positive regulation of monocyte aggregation / Hyaluronan uptake and degradation / hyaluronic acid binding / monocyte aggregation / macrophage migration inhibitory factor receptor complex / regulation of lamellipodium morphogenesis / hyaluronan catabolic process / cellular response to fibroblast growth factor stimulus / positive regulation of heterotypic cell-cell adhesion / cartilage development / wound healing, spreading of cells / negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator / negative regulation of DNA damage response, signal transduction by p53 class mediator / microvillus / lamellipodium membrane / Integrin cell surface interactions / collagen binding / T cell activation / Degradation of the extracellular matrix / cell-matrix adhesion / negative regulation of cysteine-type endopeptidase activity involved in apoptotic process / secretory granule membrane / cell projection / Cell surface interactions at the vascular wall / cell-cell adhesion / transmembrane signaling receptor activity / cytokine-mediated signaling pathway / positive regulation of peptidyl-tyrosine phosphorylation / Interferon gamma signaling / positive regulation of peptidyl-serine phosphorylation / cell migration / basolateral plasma membrane / positive regulation of ERK1 and ERK2 cascade / cell adhesion / apical plasma membrane / inflammatory response / focal adhesion / Neutrophil degranulation / negative regulation of apoptotic process / cell surface / Golgi apparatus / extracellular exosome / plasma membrane / cytosol Similarity search - Function | ||||||
Biological species | HOMO SAPIENS (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / OTHER / Resolution: 2.2 Å | ||||||
Authors | Teriete, P. / Banerji, S. / Noble, M. / Blundell, C. / Wright, A. / Pickford, A. / Lowe, E. / Mahoney, D. / Tammi, M. / Kahmann, J. ...Teriete, P. / Banerji, S. / Noble, M. / Blundell, C. / Wright, A. / Pickford, A. / Lowe, E. / Mahoney, D. / Tammi, M. / Kahmann, J. / Campbell, I. / Day, A. / Jackson, D. | ||||||
Citation | Journal: Mol.Cell / Year: 2004 Title: Structure of the Regulatory Hyaluronan-Binding Domain in the Inflammatory Leukocyte Homing Receptor Cd44 Authors: Teriete, P. / Banerji, S. / Noble, M. / Blundell, C. / Wright, A. / Pickford, A. / Lowe, E. / Mahoney, D. / Tammi, M. / Kahmann, J. / Campbell, I. / Day, A. / Jackson, D. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1uuh.cif.gz | 72.6 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1uuh.ent.gz | 57.5 KB | Display | PDB format |
PDBx/mmJSON format | 1uuh.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1uuh_validation.pdf.gz | 439.5 KB | Display | wwPDB validaton report |
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Full document | 1uuh_full_validation.pdf.gz | 444.7 KB | Display | |
Data in XML | 1uuh_validation.xml.gz | 16.1 KB | Display | |
Data in CIF | 1uuh_validation.cif.gz | 23.1 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/uu/1uuh ftp://data.pdbj.org/pub/pdb/validation_reports/uu/1uuh | HTTPS FTP |
-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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2 |
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS oper: (Code: given Matrix: (-0.74746, -0.61772, -0.24439), Vector: |
-Components
#1: Protein | Mass: 17695.275 Da / Num. of mol.: 2 / Fragment: HYALURONAN BINDING DOMAIN, RESIDUES 20-178 Source method: isolated from a genetically manipulated source Details: FIRST RESIDUE IS IN FACT THE LAST RESIDUE OF THE SIGNAL PEPTIDE, AND WOULD NORMALLY BE CLEAVED Source: (gene. exp.) HOMO SAPIENS (human) / Plasmid: PET19B / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21 / Variant (production host): DE3 PLYSS / References: UniProt: P16070 #2: Water | ChemComp-HOH / | Sequence details | HYALURONAN | |
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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: 2.3 Å3/Da / Density % sol: 40 % | ||||||||||||||||||||||||
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Crystal grow | Method: vapor diffusion, hanging drop / pH: 5.5 Details: HANGING-DROP PROTEIN 13 MG/ML; WELL BUFFER 12% PEG 3350, 50MM NACL, 10% GLYCEROL, pH 5.50 | ||||||||||||||||||||||||
Crystal grow | *PLUS 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: ESRF / Beamline: ID14-4 / Wavelength: 0.9795 |
Detector | Type: ADSC CCD / Detector: CCD / Date: May 15, 2002 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9795 Å / Relative weight: 1 |
Reflection | Resolution: 2.2→23.31 Å / Num. obs: 17476 / % possible obs: 99.8 % / Redundancy: 3.82 % / Rmerge(I) obs: 0.076 / Net I/σ(I): 7.2989 |
Reflection shell | Resolution: 2.2→2.32 Å / Redundancy: 3.53 % / Rmerge(I) obs: 0.18 / Mean I/σ(I) obs: 3.16 / % possible all: 99.6 |
Reflection | *PLUS Highest resolution: 2.2 Å / Lowest resolution: 23.31 Å / % possible obs: 99.4 % / Redundancy: 3.8 % / Rmerge(I) obs: 0.076 |
Reflection shell | *PLUS % possible obs: 98.2 % / Redundancy: 3.5 % / Rmerge(I) obs: 0.181 / Mean I/σ(I) obs: 3.1 |
-Processing
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Refinement | Method to determine structure: OTHER / Resolution: 2.2→57.73 Å / Cor.coef. Fo:Fc: 0.933 / Cor.coef. Fo:Fc free: 0.878 / SU B: 5.483 / SU ML: 0.141 / Cross valid method: THROUGHOUT / ESU R: 0.261 / ESU R Free: 0.216 / Stereochemistry target values: MAXIMUM LIKELIHOOD
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: BABINET MODEL PLUS MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 17.45 Å2
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Refinement step | Cycle: LAST / Resolution: 2.2→57.73 Å
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