+Open data
-Basic information
Entry | Database: PDB / ID: 2npl | ||||||
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Title | NMR Structure of CARD d2 Domain | ||||||
Components | Coxsackievirus and Adenovirus Receptor | ||||||
Keywords | CELL ADHESION / Coxsakievirus and Adenovirus Receptor | ||||||
Function / homology | Function and homology information AV node cell-bundle of His cell adhesion involved in cell communication / cell adhesive protein binding involved in AV node cell-bundle of His cell communication / homotypic cell-cell adhesion / AV node cell to bundle of His cell communication / epithelial structure maintenance / gamma-delta T cell activation / regulation of AV node cell action potential / germ cell migration / apicolateral plasma membrane / cell-cell junction organization ...AV node cell-bundle of His cell adhesion involved in cell communication / cell adhesive protein binding involved in AV node cell-bundle of His cell communication / homotypic cell-cell adhesion / AV node cell to bundle of His cell communication / epithelial structure maintenance / gamma-delta T cell activation / regulation of AV node cell action potential / germ cell migration / apicolateral plasma membrane / cell-cell junction organization / transepithelial transport / connexin binding / cardiac muscle cell development / heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules / bicellular tight junction / intercalated disc / mitochondrion organization / cell adhesion molecule binding / neutrophil chemotaxis / acrosomal vesicle / filopodium / PDZ domain binding / Cell surface interactions at the vascular wall / adherens junction / neuromuscular junction / beta-catenin binding / Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell / cell-cell junction / integrin binding / virus receptor activity / cell junction / cell body / heart development / growth cone / actin cytoskeleton organization / basolateral plasma membrane / defense response to virus / neuron projection / membrane raft / signaling receptor binding / protein-containing complex / extracellular space / extracellular region / nucleoplasm / identical protein binding / plasma membrane / cytoplasm Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR / SA | ||||||
Model type details | minimized average | ||||||
Authors | Jiang, S. / Caffrey, M. | ||||||
Citation | Journal: Protein Sci. / Year: 2007 Title: Solution structure of the coxsackievirus and adenovirus receptor domain 2 Authors: Jiang, S. / Caffrey, M. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2npl.cif.gz | 42.2 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2npl.ent.gz | 30.5 KB | Display | PDB format |
PDBx/mmJSON format | 2npl.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/np/2npl ftp://data.pdbj.org/pub/pdb/validation_reports/np/2npl | HTTPS FTP |
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-Related structure data
Related structure data | |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 10539.775 Da / Num. of mol.: 1 / Fragment: Domain CAR 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: CXADR, CAR / Production host: Escherichia coli (E. coli) / References: UniProt: P78310 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||
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NMR experiment |
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-NMR measurement
NMR spectrometer |
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-Processing
NMR software |
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Refinement | Method: SA / Software ordinal: 1 Details: Structure is based on the average structure of the 30 lowest energy structures with 488 distance restraints, 234 dihedral restraints and 47 hodrogen bond restraints. | ||||||||||||
NMR representative | Selection criteria: minimized average structure | ||||||||||||
NMR ensemble | Conformer selection criteria: lowest energy / Conformers calculated total number: 30 / Conformers submitted total number: 1 |