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- PDB-1bt6: P11 (S100A10), LIGAND OF ANNEXIN II IN COMPLEX WITH ANNEXIN II N-... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1bt6 | ||||||
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Title | P11 (S100A10), LIGAND OF ANNEXIN II IN COMPLEX WITH ANNEXIN II N-TERMINUS | ||||||
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![]() | COMPLEX (LIGAND/ANNEXIN) / S100 FAMILY / EF-HAND PROTEIN / COMPLEX (LIGAND-ANNEXIN) / LIGAND OF ANNEXIN II / CALCIUM/PHOSPHOLIPID BINDING PROTEIN / COMPLEX (LIGAND-ANNEXIN) complex | ||||||
Function / homology | ![]() transforming growth factor beta3 production / : / voltage-gated calcium channel activity involved in regulation of cytosolic calcium levels / positive regulation of low-density lipoprotein particle receptor binding / positive regulation of receptor-mediated endocytosis involved in cholesterol transport / AnxA2-p11 complex / membrane raft assembly / positive regulation of low-density lipoprotein particle clearance / phospholipase A2 inhibitor activity / endocardial cell differentiation ...transforming growth factor beta3 production / : / voltage-gated calcium channel activity involved in regulation of cytosolic calcium levels / positive regulation of low-density lipoprotein particle receptor binding / positive regulation of receptor-mediated endocytosis involved in cholesterol transport / AnxA2-p11 complex / membrane raft assembly / positive regulation of low-density lipoprotein particle clearance / phospholipase A2 inhibitor activity / endocardial cell differentiation / negative regulation of low-density lipoprotein particle receptor catabolic process / growth plate cartilage development / positive regulation of plasma membrane repair / positive regulation of plasminogen activation / positive regulation of chondrocyte differentiation / myelin sheath adaxonal region / Schmidt-Lanterman incisure / vesicle budding from membrane / regulation of plasminogen activation / plasma membrane protein complex / positive regulation of calcium ion transport / calcium-dependent phospholipid binding / virion binding / collagen fibril organization / Dissolution of Fibrin Clot / positive regulation of low-density lipoprotein receptor activity / extrinsic component of plasma membrane / positive regulation of receptor recycling / bone mineralization / phosphatidylserine binding / positive regulation of exocytosis / positive regulation of focal adhesion assembly / regulation of neurogenesis / basement membrane / calcium ion homeostasis / positive regulation of substrate adhesion-dependent cell spreading / positive regulation of stress fiber assembly / calcium channel complex / fibrinolysis / phosphatidylinositol-4,5-bisphosphate binding / cytoskeletal protein binding / positive regulation of GTPase activity / Neutrophil degranulation / protein localization to plasma membrane / mRNA transcription by RNA polymerase II / calcium channel activity / sarcolemma / nuclear matrix / RNA polymerase II transcription regulator complex / calcium-dependent protein binding / protease binding / basolateral plasma membrane / angiogenesis / collagen-containing extracellular matrix / vesicle / transmembrane transporter binding / early endosome / calcium ion binding / cell surface / protein homodimerization activity / positive regulation of transcription by RNA polymerase II / protein-containing complex / extracellular space / extracellular exosome / extracellular region / nucleus / plasma membrane / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Rety, S. / Sopkova, J. / Renouard, M. / Osterloh, D. / Gerke, V. / Russo-Marie, F. / Lewit-Bentley, A. | ||||||
![]() | ![]() Title: The crystal structure of a complex of p11 with the annexin II N-terminal peptide. Authors: Rety, S. / Sopkova, J. / Renouard, M. / Osterloh, D. / Gerke, V. / Tabaries, S. / Russo-Marie, F. / Lewit-Bentley, A. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 48.9 KB | Display | ![]() |
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PDB format | ![]() | 39.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 1a4pSC S: Starting model for refinement C: citing same article ( |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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2 | ![]()
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS oper:
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Components
#1: Protein | Mass: 11088.940 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() #2: Protein/peptide | Mass: 1483.706 Da / Num. of mol.: 2 / Fragment: N-TERMINAL Source method: isolated from a genetically manipulated source References: UniProt: P17785 #3: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.77 Å3/Da / Density % sol: 56 % | |||||||||||||||||||||||||||||||||||
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Crystal grow | pH: 7.5 / Details: pH 7.5 | |||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Method: unknown | |||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 280 K |
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Diffraction source | Source: ![]() ![]() |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Apr 25, 1998 / Details: FOCUSSING MONOCHROMATOR AND MONOLAYER |
Radiation | Monochromator: GE(111) / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.97 Å / Relative weight: 1 |
Reflection | Resolution: 2.4→62 Å / Num. obs: 9774 / % possible obs: 96.8 % / Observed criterion σ(I): 0 / Redundancy: 6.25 % / Rmerge(I) obs: 0.06 / Rsym value: 0.06 / Net I/σ(I): 20.6 |
Reflection shell | Resolution: 2.4→2.5 Å / Redundancy: 2.5 % / Mean I/σ(I) obs: 1.96 / Rsym value: 0.61 |
Reflection | *PLUS Num. measured all: 29481 |
Reflection shell | *PLUS Rmerge(I) obs: 0.61 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 1A4P Resolution: 2.4→20 Å / Cross valid method: THROUGHOUT / σ(F): 0
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Displacement parameters | Biso mean: 200.1 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.4→20 Å
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Refine LS restraints |
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Software | *PLUS Name: REFMAC / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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