+Open data
-Basic information
Entry | Database: PDB / ID: 2mpf | ||||||
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Title | Solution structure human HCN2 CNBD in the cAMP-unbound state | ||||||
Components | Potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 2 | ||||||
Keywords | TRANSPORT PROTEIN / HCN channels | ||||||
Function / homology | Function and homology information HCN channels / HCN channel complex / intracellularly cAMP-activated cation channel activity / cellular response to cGMP / membrane depolarization during cardiac muscle cell action potential / sodium ion import across plasma membrane / voltage-gated sodium channel activity / regulation of membrane depolarization / potassium ion import across plasma membrane / voltage-gated potassium channel activity ...HCN channels / HCN channel complex / intracellularly cAMP-activated cation channel activity / cellular response to cGMP / membrane depolarization during cardiac muscle cell action potential / sodium ion import across plasma membrane / voltage-gated sodium channel activity / regulation of membrane depolarization / potassium ion import across plasma membrane / voltage-gated potassium channel activity / sodium ion transmembrane transport / voltage-gated potassium channel complex / cAMP binding / cellular response to cAMP / potassium ion transmembrane transport / regulation of membrane potential / cell-cell signaling / axon / dendrite / identical protein binding / plasma membrane Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR / torsion angle dynamics, molecular dynamics | ||||||
Model details | closest to the average, model1 | ||||||
Authors | Saponaro, A. / Pauleta, S.R. / Cantini, F. / Matzapetakis, M. / Hammann, C. / Banci, L. / Thiel, G. / Santoro, B. / Moroni, A. | ||||||
Citation | Journal: Proc.Natl.Acad.Sci.USA / Year: 2014 Title: Structural basis for the mutual antagonism of cAMP and TRIP8b in regulating HCN channel function. Authors: Saponaro, A. / Pauleta, S.R. / Cantini, F. / Matzapetakis, M. / Hammann, C. / Donadoni, C. / Hu, L. / Thiel, G. / Banci, L. / Santoro, B. / Moroni, A. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2mpf.cif.gz | 984.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2mpf.ent.gz | 836.8 KB | Display | PDB format |
PDBx/mmJSON format | 2mpf.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/mp/2mpf ftp://data.pdbj.org/pub/pdb/validation_reports/mp/2mpf | HTTPS FTP |
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-Related structure data
Similar structure data | |
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Other databases |
-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 17987.891 Da / Num. of mol.: 1 Fragment: cyclic nucleotide binding domain (UNP residues 521-672) Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: HCN2, BCNG2 / Plasmid: pET24b / Production host: Escherichia coli (E. coli) / Strain (production host): Rosetta / References: UniProt: Q9UL51 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||||||||||||||||||
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NMR experiment |
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-Sample preparation
Details |
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Sample |
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Sample conditions | pH: 7.0 / Pressure: ambient / Temperature: 298 K |
-NMR measurement
NMR spectrometer |
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-Processing
NMR software |
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Refinement | Method: torsion angle dynamics, molecular dynamics / Software ordinal: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||
NMR constraints | NOE constraints total: 1841 / NOE intraresidue total count: 508 / NOE long range total count: 461 / NOE medium range total count: 295 / NOE sequential total count: 577 / Hydrogen bond constraints total count: 36 / Protein phi angle constraints total count: 103 / Protein psi angle constraints total count: 103 | ||||||||||||||||||||||||||||||||||||||||||||||||
NMR representative | Selection criteria: closest to the average | ||||||||||||||||||||||||||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: target function / Conformers calculated total number: 500 / Conformers submitted total number: 20 / Maximum torsion angle constraint violation: 14.91 ° / Maximum upper distance constraint violation: 0.38 Å |