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Yorodumi- PDB-1eh2: STRUCTURE OF THE SECOND EPS15 HOMOLOGY DOMAIN OF HUMAN EPS15, NMR... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1eh2 | ||||||
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Title | STRUCTURE OF THE SECOND EPS15 HOMOLOGY DOMAIN OF HUMAN EPS15, NMR, 20 STRUCTURES | ||||||
Components | EPS15 | ||||||
Keywords | CALCIUM BINDING / SIGNALING DOMAIN / NPF BINDING / EF-HAND / EH DOMAIN | ||||||
Function / homology | Function and homology information Golgi to endosome transport / clathrin coat of coated pit / vesicle organization / postsynaptic neurotransmitter receptor internalization / clathrin coat assembly / endocytic recycling / aggresome / endosomal transport / positive regulation of receptor recycling / polyubiquitin modification-dependent protein binding ...Golgi to endosome transport / clathrin coat of coated pit / vesicle organization / postsynaptic neurotransmitter receptor internalization / clathrin coat assembly / endocytic recycling / aggresome / endosomal transport / positive regulation of receptor recycling / polyubiquitin modification-dependent protein binding / clathrin-coated pit / basal plasma membrane / InlB-mediated entry of Listeria monocytogenes into host cell / EGFR downregulation / Negative regulation of MET activity / SH3 domain binding / endocytosis / protein transport / Cargo recognition for clathrin-mediated endocytosis / Clathrin-mediated endocytosis / regulation of cell population proliferation / early endosome membrane / postsynapse / receptor-mediated endocytosis of virus by host cell / symbiont entry into host cell / cadherin binding / apical plasma membrane / intracellular membrane-bounded organelle / glutamatergic synapse / calcium ion binding / membrane / plasma membrane / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR / simulated annealing | ||||||
Authors | De Beer, T. / Carter, R.E. / Lobel-Rice, K.E. / Sorkin, A. / Overduin, M. | ||||||
Citation | Journal: Science / Year: 1998 Title: Structure and Asn-Pro-Phe binding pocket of the Eps15 homology domain. Authors: de Beer, T. / Carter, R.E. / Lobel-Rice, K.E. / Sorkin, A. / Overduin, M. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1eh2.cif.gz | 586.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1eh2.ent.gz | 485.5 KB | Display | PDB format |
PDBx/mmJSON format | 1eh2.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/eh/1eh2 ftp://data.pdbj.org/pub/pdb/validation_reports/eh/1eh2 | HTTPS FTP |
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-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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NMR ensembles |
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-Components
#1: Protein | Mass: 11935.817 Da / Num. of mol.: 1 / Fragment: EPS15 HOMOLOGY (EH) DOMAIN 2, RESIDUES 121-218 Source method: isolated from a genetically manipulated source Details: THIS DOMAIN CONTAINS A CALCIUM BINDING SITE / Source: (gene. exp.) Homo sapiens (human) / Gene: EPS15 / Plasmid: PRSETA / Production host: Escherichia coli (E. coli) Strain (production host): B834 (DE3) PLYSS AND BL21 (DE3) PLYSS References: UniProt: P42566 |
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#2: Chemical | ChemComp-CA / |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||||||||||||||||||||||||||
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NMR experiment |
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NMR details | Text: NMR EXPERIMENTS WERE PERFORMED ON UNLABELED, 15N-LABELED AND 13C,15N-LABELED EH2 PROTEIN |
-Sample preparation
Details | Contents: H2O AND D2O |
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Sample conditions | Ionic strength: 120 MILLIMOLAR / pH: 7.0 / Pressure: ATMOSPHERIC atm / Temperature: 298 K |
Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
NMR spectrometer |
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-Processing
Software |
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NMR software |
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Refinement | Method: simulated annealing / Software ordinal: 1 Details: THE R-6 SUMMATION METHOD WAS USED WITHIN A SIMULATED ANNEALING PROTOCOL. | |||||||||
NMR ensemble | Conformer selection criteria: 20 LOWEST NOE ENERGIES / Conformers calculated total number: 50 / Conformers submitted total number: 20 |