+Open data
-Basic information
Entry | Database: PDB / ID: 1y1a | ||||||
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Title | CRYSTAL STRUCTURE OF CALCIUM AND INTEGRIN BINDING PROTEIN | ||||||
Components | Calcium and integrin binding 1 (calmyrin) | ||||||
Keywords | METAL BINDING PROTEIN / CALCIUM-BINDING PROTEIN / INTEGRIN / EF-HAND / GLUTATHIONE / GLUTATHIOLATION | ||||||
Function / homology | Function and homology information calcium-dependent protein kinase inhibitor activity / thrombopoietin-mediated signaling pathway / endomitotic cell cycle / positive regulation of male germ cell proliferation / filopodium tip / positive regulation of calcineurin-NFAT signaling cascade / negative regulation of microtubule depolymerization / protein serine/threonine kinase inhibitor activity / positive regulation of cell adhesion mediated by integrin / positive regulation of cell-matrix adhesion ...calcium-dependent protein kinase inhibitor activity / thrombopoietin-mediated signaling pathway / endomitotic cell cycle / positive regulation of male germ cell proliferation / filopodium tip / positive regulation of calcineurin-NFAT signaling cascade / negative regulation of microtubule depolymerization / protein serine/threonine kinase inhibitor activity / positive regulation of cell adhesion mediated by integrin / positive regulation of cell-matrix adhesion / platelet formation / positive regulation of cell migration involved in sprouting angiogenesis / positive regulation of catalytic activity / regulation of cell division / spermatid development / positive regulation of protein targeting to membrane / negative regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction / negative regulation of megakaryocyte differentiation / cytoplasmic microtubule organization / protein-membrane adaptor activity / positive regulation of substrate adhesion-dependent cell spreading / extrinsic apoptotic signaling pathway / cellular response to nerve growth factor stimulus / negative regulation of protein phosphorylation / cell periphery / response to ischemia / positive regulation of protein localization to plasma membrane / sarcolemma / positive regulation of protein serine/threonine kinase activity / cellular response to growth factor stimulus / ruffle membrane / small GTPase binding / double-strand break repair / negative regulation of neuron projection development / lamellipodium / cellular response to tumor necrosis factor / positive regulation of NF-kappaB transcription factor activity / regulation of cell population proliferation / growth cone / perikaryon / positive regulation of cell growth / angiogenesis / vesicle / transmembrane transporter binding / positive regulation of ERK1 and ERK2 cascade / cell adhesion / neuron projection / positive regulation of cell migration / positive regulation of protein phosphorylation / apical plasma membrane / cell division / axon / negative regulation of cell population proliferation / centrosome / neuronal cell body / apoptotic process / DNA damage response / calcium ion binding / positive regulation of cell population proliferation / negative regulation of apoptotic process / perinuclear region of cytoplasm / Golgi apparatus / magnesium ion binding / endoplasmic reticulum / extracellular exosome / nucleoplasm / membrane / nucleus / plasma membrane / cytoplasm Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MAD / Resolution: 2.3 Å | ||||||
Authors | Blamey, C.J. / Ceccarelli, C. / Naik, U.P. / Bahnson, B.J. | ||||||
Citation | Journal: Protein Sci. / Year: 2005 Title: The crystal structure of calcium- and integrin-binding protein 1: Insights into redox regulated functions Authors: Blamey, C.J. / Ceccarelli, C. / Naik, U.P. / Bahnson, B.J. | ||||||
History |
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Remark 295 | NON-CRYSTALLOGRAPHIC SYMMETRY THE TRANSFORMATIONS PRESENTED ON THE MTRIX RECORDS BELOW DESCRIBE ... NON-CRYSTALLOGRAPHIC SYMMETRY THE TRANSFORMATIONS PRESENTED ON THE MTRIX RECORDS BELOW DESCRIBE NON-CRYSTALLOGRAPHIC RELATIONSHIPS AMONG ATOMS IN THIS ENTRY. APPLYING THE APPROPRIATE MTRIX TRANSFORMATION TO THE RESIDUES LISTED FIRST WILL YIELD APPROXIMATE COORDINATES FOR THE RESIDUES LISTED SECOND. CHAIN IDENTIFIERS GIVEN AS "?" REFER TO CHAINS FOR WHICH ATOMS ARE NOT FOUND IN THIS ENTRY. APPLIED TO TRANSFORMED TO TRANSFORM CHAIN RESIDUES CHAIN RESIDUES RMSD SSS M 1 A 52 .. 191 B 52 .. 191 0.655 WHERE SSS -> COLUMNS 8-10 OF MTRIX RECORDS | ||||||
Remark 999 | SEQUENCE GB 12654075 AAH00846 1 - 8 NOT IN ATOMS LIST A DELETION MUTANT OF CIB WHOSE SEQUENCE DOES ...SEQUENCE GB 12654075 AAH00846 1 - 8 NOT IN ATOMS LIST A DELETION MUTANT OF CIB WHOSE SEQUENCE DOES NOT INCLUDE THE FIRST EIGHT N-TERMINAL RESIDUES WAS USED FOR THE X-RAY STUDIES DESCRIBED IN THIS ENTRY. |
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1y1a.cif.gz | 95.2 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1y1a.ent.gz | 72.4 KB | Display | PDB format |
PDBx/mmJSON format | 1y1a.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/y1/1y1a ftp://data.pdbj.org/pub/pdb/validation_reports/y1/1y1a | 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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2 |
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3 |
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4 |
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5 |
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS oper:
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-Components
#1: Protein | Mass: 20980.490 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: CIB1 / Species (production host): Escherichia coli / Production host: Escherichia coli BL21 (bacteria) / Strain (production host): BL21 / References: UniProt: Q99828 #2: Chemical | ChemComp-CA / #3: Chemical | ChemComp-GSH / | #4: 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: 6.2 Å3/Da / Density % sol: 80.1 % |
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Crystal grow | Temperature: 277 K / Method: vapor diffusion, hanging drop / pH: 7 Details: 20 MG/ML PROTEIN, 50MM HEPES, 3M FORMATE, 300MM NaCl, 1% DMSO, 0.25MM DTT, pH 7.00, VAPOR DIFFUSION, HANGING DROP, temperature 277K |
-Data collection
Diffraction | Mean temperature: 100 K | |||||||||||||||
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Diffraction source | Source: SYNCHROTRON / Site: APS / Beamline: 14-ID-B / Wavelength: 1.12709 / Wavelength: 1.53578, 1.53466, 1.47954 | |||||||||||||||
Detector | Type: MAR CCD 165 mm / Detector: CCD / Date: Aug 20, 2004 | |||||||||||||||
Radiation | Protocol: MAD / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | |||||||||||||||
Radiation wavelength |
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Reflection | Resolution: 2.3→50 Å / Num. all: 44410 / Num. obs: 44410 / % possible obs: 92.9 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 10.4 % / Biso Wilson estimate: 45.8 Å2 / Rmerge(I) obs: 0.067 / Net I/σ(I): 7.9 | |||||||||||||||
Reflection shell | Resolution: 2.3→2.38 Å / Redundancy: 10.1 % / Rmerge(I) obs: 0.388 / Mean I/σ(I) obs: 2 / % possible all: 65.6 |
-Processing
Software |
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Refinement | Method to determine structure: MAD / Resolution: 2.3→47.25 Å / Rfactor Rfree error: 0.005 / Data cutoff high absF: 2357501.5 / Data cutoff low absF: 0 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 0 / σ(I): 0 / Stereochemistry target values: Engh & Huber
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Solvent computation | Solvent model: FLAT MODEL / Bsol: 50.7122 Å2 / ksol: 0.353729 e/Å3 | ||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 55.6 Å2
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 2.3→47.25 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.3→2.43 Å / Rfactor Rfree error: 0.021 / Total num. of bins used: 6
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Xplor file |
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