+Open data
-Basic information
Entry | Database: PDB / ID: 2jyw | ||||||
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Title | Solution structure of C-terminal domain of APOBEC3G | ||||||
Components | DNA dC->dU-editing enzyme APOBEC-3G | ||||||
Keywords | HYDROLASE / Protein / Zinc / Alternative splicing / Antiviral defense / Cytoplasm / Host-virus interaction / Metal-binding / Nucleus / Polymorphism / Ubl conjugation | ||||||
Function / homology | Function and homology information apolipoprotein B mRNA editing enzyme complex / dCTP deaminase activity / cytidine deamination / base conversion or substitution editing / single-stranded DNA cytosine deaminase / DNA cytosine deamination / cytidine to uridine editing / deoxycytidine deaminase activity / cytidine deaminase activity / negative regulation of single stranded viral RNA replication via double stranded DNA intermediate ...apolipoprotein B mRNA editing enzyme complex / dCTP deaminase activity / cytidine deamination / base conversion or substitution editing / single-stranded DNA cytosine deaminase / DNA cytosine deamination / cytidine to uridine editing / deoxycytidine deaminase activity / cytidine deaminase activity / negative regulation of single stranded viral RNA replication via double stranded DNA intermediate / negative regulation of viral process / retrotransposon silencing / DNA demethylation / negative regulation of viral genome replication / APOBEC3G mediated resistance to HIV-1 infection / positive regulation of defense response to virus by host / P-body / Vif-mediated degradation of APOBEC3G / defense response to virus / ribonucleoprotein complex / innate immune response / RNA binding / zinc ion binding / identical protein binding / nucleus / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR / simulated annealing, torsion angle dynamics | ||||||
Model details | C-terminal domain of APOBEC3G | ||||||
Authors | Chen, K. / Harjes, E. / Gross, P.J. / Fahmy, A. / Lu, Y. / Shindo, K. / Harris, R.S. / Matsuo, H. | ||||||
Citation | Journal: Nature / Year: 2008 Title: Structure of the DNA deaminase domain of the HIV-1 restriction factor APOBEC3G. Authors: Chen, K.M. / Harjes, E. / Gross, P.J. / Fahmy, A. / Lu, Y. / Shindo, K. / Harris, R.S. / Matsuo, H. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2jyw.cif.gz | 592.9 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2jyw.ent.gz | 507.7 KB | Display | PDB format |
PDBx/mmJSON format | 2jyw.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/jy/2jyw ftp://data.pdbj.org/pub/pdb/validation_reports/jy/2jyw | 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: 22717.479 Da / Num. of mol.: 1 / Fragment: C-terminal domain / Mutation: L37K, C46A, F113K, C124A, C159A Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: APOBEC3G / Plasmid: pGEX6P2_A3G198-384 / Production host: Escherichia coli (E. coli) References: UniProt: Q9HC16, Hydrolases; Acting on carbon-nitrogen bonds, other than peptide bonds; In cyclic amidines |
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#2: Chemical | ChemComp-ZN / |
-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 | Ionic strength: 0 / pH: 7.4 / Pressure: ambient / Temperature: 293 K |
-NMR measurement
NMR spectrometer |
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-Processing
NMR software |
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Refinement | Method: simulated annealing, torsion angle dynamics / Software ordinal: 1 | ||||||||||||||||||||||||||||||||
NMR constraints | NOE constraints total: 2008 / NOE intraresidue total count: 242 / NOE long range total count: 656 / NOE medium range total count: 506 / NOE sequential total count: 604 / Hydrogen bond constraints total count: 142 / Protein phi angle constraints total count: 115 / Protein psi angle constraints total count: 115 | ||||||||||||||||||||||||||||||||
NMR representative | Selection criteria: closest to the average | ||||||||||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: lowest energy, ramachandran parameters Conformers calculated total number: 100 / Conformers submitted total number: 10 / Maximum torsion angle constraint violation: 4.03 ° / Maximum upper distance constraint violation: 0.21 Å |