+Open data
-Basic information
Entry | Database: PDB / ID: 2uur | ||||||
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Title | N-terminal NC4 domain of collagen IX | ||||||
Components | COLLAGEN ALPHA-1(IX) CHAIN | ||||||
Keywords | STRUCTURAL PROTEIN / GLYCOPROTEIN / HYDROXYLATION / NC4 / COLLAGEN / COLLAGEN IX / POLYMORPHISM / EXTRACELLULAR MATRIX / ALTERNATIVE SPLICING | ||||||
Function / homology | Function and homology information collagen type IX trimer / Collagen chain trimerization / extracellular matrix structural constituent conferring tensile strength / Collagen biosynthesis and modifying enzymes / Signaling by PDGF / NCAM1 interactions / Assembly of collagen fibrils and other multimeric structures / Collagen degradation / ECM proteoglycans / Integrin cell surface interactions ...collagen type IX trimer / Collagen chain trimerization / extracellular matrix structural constituent conferring tensile strength / Collagen biosynthesis and modifying enzymes / Signaling by PDGF / NCAM1 interactions / Assembly of collagen fibrils and other multimeric structures / Collagen degradation / ECM proteoglycans / Integrin cell surface interactions / extracellular matrix organization / animal organ morphogenesis / carbohydrate binding / collagen-containing extracellular matrix / endoplasmic reticulum lumen / protein homodimerization activity / extracellular space / extracellular region / metal ion binding Similarity search - Function | ||||||
Biological species | HOMO SAPIENS (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MAD / Resolution: 1.8 Å | ||||||
Authors | Leppanen, V.-M. / Tossavainen, H. / Permi, P. / Lehtio, L. / Ronnholm, G. / Goldman, A. / Kilpelainen, I. / Pihlajamaa, T. | ||||||
Citation | Journal: J.Biol.Chem. / Year: 2007 Title: Crystal Structure of the N-Terminal Nc4 Domain of Collagen Ix, a Zinc Binding Member of the Laminin-Neurexin-Sex Hormone Binding Globulin (Lns) Domain Family. Authors: Leppanen, V.-M. / Tossavainen, H. / Permi, P. / Lehtio, L. / Ronnholm, G. / Goldman, A. / Kilpelainen, I. / Pihlajamaa, T. | ||||||
History |
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Remark 700 | SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN ... SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW, TWO SHEETS ARE DEFINED. |
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2uur.cif.gz | 58.5 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2uur.ent.gz | 46 KB | Display | PDB format |
PDBx/mmJSON format | 2uur.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/uu/2uur ftp://data.pdbj.org/pub/pdb/validation_reports/uu/2uur | HTTPS FTP |
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-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: 27483.232 Da / Num. of mol.: 1 / Fragment: NC4 DOMAIN, RESIDUES 24-268 Source method: isolated from a genetically manipulated source Source: (gene. exp.) HOMO SAPIENS (human) / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): ROSETTA DE3 / References: UniProt: P20849 | ||||
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#2: Chemical | ChemComp-ZN / | ||||
#3: Chemical | ChemComp-SO4 / | ||||
#4: Chemical | ChemComp-EDO / #5: Water | ChemComp-HOH / | Sequence details | THE GENBANK ENTRY INCLUDES A SIGNAL PEPTIDE OF 23 RESIDUES, WHICH IS OMITTED FROM THE STUDIED MACROMOLEC | |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.2 Å3/Da / Density % sol: 42 % |
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Crystal grow | pH: 6.5 / Details: 100 MM MES, PH 6.5 10 MM ZNSO4 20% MME-PEG 550 |
-Data collection
Diffraction | Mean temperature: 100 K | ||||||||||||
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Diffraction source | Source: SYNCHROTRON / Site: ESRF / Beamline: BM14 / Wavelength: 0.9797, 0.9796, 0.8856 | ||||||||||||
Detector | Type: MARRESEARCH / Detector: CCD / Date: Sep 20, 2003 | ||||||||||||
Radiation | Protocol: MAD / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | ||||||||||||
Radiation wavelength |
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Reflection | Resolution: 1.8→20 Å / Num. obs: 21918 / % possible obs: 99.9 % / Observed criterion σ(I): 0 / Redundancy: 7.5 % / Biso Wilson estimate: 20.2 Å2 / Rmerge(I) obs: 0.05 / Net I/σ(I): 20.5 | ||||||||||||
Reflection shell | Resolution: 1.8→1.9 Å / Rmerge(I) obs: 0.34 / Mean I/σ(I) obs: 5.1 / % possible all: 100 |
-Processing
Software |
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Refinement | Method to determine structure: MAD / Resolution: 1.8→19.96 Å / Rfactor Rfree error: 0.007 / Data cutoff high absF: 2639988.95 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 0 / Stereochemistry target values: MAXIMUM LIKELIHOOD
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Solvent computation | Solvent model: FLAT MODEL / Bsol: 53.4928 Å2 / ksol: 0.35623 e/Å3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 30.4 Å2
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 1.8→19.96 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.8→1.91 Å / Rfactor Rfree error: 0.02 / Total num. of bins used: 6
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Xplor file |
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