[English] 日本語
Yorodumi
- PDB-3zgq: Crystal structure of human interferon-induced protein IFIT5 -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 3zgq
TitleCrystal structure of human interferon-induced protein IFIT5
ComponentsINTERFERON-INDUCED PROTEIN WITH TETRATRICOPEPTIDE REPEATS 5
KeywordsIMMUNE SYSTEM / RNA BINDING / INTERFERON RESPONSE
Function / homology
Function and homology information


RNA cap binding / poly(U) RNA binding / negative regulation of viral genome replication / ruffle membrane / Interferon alpha/beta signaling / actin cytoskeleton / apical part of cell / double-stranded DNA binding / positive regulation of canonical NF-kappaB signal transduction / defense response to virus ...RNA cap binding / poly(U) RNA binding / negative regulation of viral genome replication / ruffle membrane / Interferon alpha/beta signaling / actin cytoskeleton / apical part of cell / double-stranded DNA binding / positive regulation of canonical NF-kappaB signal transduction / defense response to virus / tRNA binding / single-stranded RNA binding / innate immune response / RNA binding / plasma membrane / cytosol
Similarity search - Function
Tetratricopeptide repeat 2 / Tetratricopeptide repeat / Tetratricopeptide repeat / Tetratricopeptide repeat / Tetratricopeptide repeat domain / Tetratricopeptide repeat / TPR repeat region circular profile. / TPR repeat profile. / Tetratricopeptide repeats / Tetratricopeptide repeat ...Tetratricopeptide repeat 2 / Tetratricopeptide repeat / Tetratricopeptide repeat / Tetratricopeptide repeat / Tetratricopeptide repeat domain / Tetratricopeptide repeat / TPR repeat region circular profile. / TPR repeat profile. / Tetratricopeptide repeats / Tetratricopeptide repeat / Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat / Alpha Horseshoe / Tetratricopeptide-like helical domain superfamily / Mainly Alpha
Similarity search - Domain/homology
DI(HYDROXYETHYL)ETHER / Interferon-induced protein with tetratricopeptide repeats 5
Similarity search - Component
Biological speciesHOMO SAPIENS (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MAD / Resolution: 2.203 Å
AuthorsKatibah, G.E. / Lee, H.J. / Huizar, J.P. / Vogan, J.M. / Alber, T. / Collins, K.
CitationJournal: Mol.Cell / Year: 2013
Title: TRNA Binding, Structure, and Localization of the Human Interferon-Induced Protein Ifit5.
Authors: Katibah, G.E. / Lee, H.J. / Huizar, J.P. / Vogan, J.M. / Alber, T. / Collins, K.
History
DepositionDec 19, 2012Deposition site: PDBE / Processing site: PDBE
Revision 1.0Jan 23, 2013Provider: repository / Type: Initial release
Revision 1.1Mar 6, 2013Group: Database references

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: INTERFERON-INDUCED PROTEIN WITH TETRATRICOPEPTIDE REPEATS 5
hetero molecules


Theoretical massNumber of molelcules
Total (without water)56,0402
Polymers55,9341
Non-polymers1061
Water4,179232
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
Unit cell
Length a, b, c (Å)63.833, 71.793, 116.920
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number19
Space group name H-MP212121

-
Components

#1: Protein INTERFERON-INDUCED PROTEIN WITH TETRATRICOPEPTIDE REPEATS 5 / IFIT-5 / INTERFERON-INDUCED 58 KDA PROTEIN / RETINOIC ACID-AND INTERFERON-INDUCIBLE 58 KDA PROTEIN / P58


Mass: 55933.715 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Details: RESIDUES 190-195 ARE DISORDERED / Source: (gene. exp.) HOMO SAPIENS (human) / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / Variant (production host): ROSETTA / References: UniProt: Q13325
#2: Chemical ChemComp-PEG / DI(HYDROXYETHYL)ETHER / Diethylene glycol


Mass: 106.120 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C4H10O3
#3: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 232 / Source method: isolated from a natural source / Formula: H2O

-
Experimental details

-
Experiment

ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 1

-
Sample preparation

CrystalDensity Matthews: 2.39 Å3/Da / Density % sol: 48.61 % / Description: NONE
Crystal growpH: 6.5 / Details: pH 6.5

-
Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: ALS / Beamline: 8.3.1 / Wavelength: 1.1111
DetectorType: ADSC QUANTUM 315r / Detector: CCD / Details: DOUBLE CRYSTAL SI(111)
RadiationMonochromator: DOUBLE FLAT CRYSTAL, SI(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.1111 Å / Relative weight: 1
ReflectionResolution: 2.2→47.7 Å / Num. obs: 27780 / % possible obs: 99.9 % / Observed criterion σ(I): 2 / Redundancy: 4 % / Biso Wilson estimate: 27.28 Å2 / Rmerge(I) obs: 0.11 / Net I/σ(I): 14.6
Reflection shellResolution: 2.2→2.24 Å / Redundancy: 4 % / Rmerge(I) obs: 0.7 / Mean I/σ(I) obs: 2 / % possible all: 100

-
Processing

Software
NameVersionClassification
PHENIX(PHENIX.REFINE)refinement
HKL-2000data reduction
HKL-2000data scaling
RefinementMethod to determine structure: MAD / Resolution: 2.203→47.704 Å / SU ML: 0.26 / σ(F): 1.34 / Phase error: 23.16 / Stereochemistry target values: ML / Details: RESIDUES 190-195 ARE DISORDERED
RfactorNum. reflection% reflection
Rfree0.2398 2000 7.2 %
Rwork0.1778 --
obs0.1821 27780 99.77 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Refinement stepCycle: LAST / Resolution: 2.203→47.704 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms3885 0 7 232 4124
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0084006
X-RAY DIFFRACTIONf_angle_d1.1215395
X-RAY DIFFRACTIONf_dihedral_angle_d15.721527
X-RAY DIFFRACTIONf_chiral_restr0.08582
X-RAY DIFFRACTIONf_plane_restr0.005687
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.2034-2.25850.25091370.22211764X-RAY DIFFRACTION98
2.2585-2.31950.2831410.21851816X-RAY DIFFRACTION100
2.3195-2.38780.29541410.20461810X-RAY DIFFRACTION100
2.3878-2.46490.28221410.19821833X-RAY DIFFRACTION100
2.4649-2.5530.27491420.191823X-RAY DIFFRACTION100
2.553-2.65520.27521420.191824X-RAY DIFFRACTION100
2.6552-2.7760.30011400.19371819X-RAY DIFFRACTION100
2.776-2.92230.25431420.18581831X-RAY DIFFRACTION100
2.9223-3.10540.27551430.18871829X-RAY DIFFRACTION100
3.1054-3.34510.2661430.18271845X-RAY DIFFRACTION100
3.3451-3.68160.23211430.15931852X-RAY DIFFRACTION100
3.6816-4.21410.19661440.14661863X-RAY DIFFRACTION100
4.2141-5.30820.17391470.15561888X-RAY DIFFRACTION100
5.3082-47.71490.23321540.18341983X-RAY DIFFRACTION100
Refinement TLS params.

Method: refined / Refine-ID: X-RAY DIFFRACTION

IDL112)L122)L132)L222)L232)L332)S11 (Å °)S12 (Å °)S13 (Å °)S21 (Å °)S22 (Å °)S23 (Å °)S31 (Å °)S32 (Å °)S33 (Å °)T112)T122)T132)T222)T232)T332)Origin x (Å)Origin y (Å)Origin z (Å)
13.1213-0.79580.92031.7361-0.00922.0469-0.0733-0.0850.45720.09110.05970.0704-0.1795-0.0632-0.01490.0957-0.0270.01030.08210.01050.2345.939799.5934137.488
21.983-0.9297-0.17921.49021.03271.6790.03770.25570.7378-0.36780.0350.385-0.5626-0.16710.06070.1120.0477-0.02480.18110.08440.47190.0264104.6484130.7761
32.0784-0.4305-0.09771.8870.04660.53290.11190.61340.1115-0.4012-0.02660.2055-0.1279-0.0658-0.04380.08250.0295-0.03650.15470.09250.029516.971698.283120.7398
41.5384-0.1646-0.02321.5506-1.16682.5722-0.02970.16830.16260.0267-0.1363-0.2483-0.11780.30280.09450.0643-0.0140.00880.08470.04530.109233.486794.5393130.1712
52.9775-0.53830.32632.3822-1.0111.59870.117-0.0116-0.1306-0.1619-0.231-0.34970.08580.37390.01410.1025-0.0114-0.06490.0892-0.00020.030537.626374.9756139.8427
62.11591.32261.60681.93570.31962.22640.12670.1589-0.2856-0.1778-0.0280.39510.1593-0.0985-0.04550.11020.0032-0.06070.0952-0.02960.198420.451566.684134.2327
76.08571.30790.00457.14761.96054.9902-0.2768-0.2049-0.3232-0.35070.48850.0370.55350.2126-0.14930.2770.0241-0.0430.2734-0.02040.290615.859959.6592118.2154
87.0885-0.2840.39392.12241.84254.68330.3586-0.4516-0.6485-0.67760.42620.59440.43710.0855-0.84080.4405-0.0669-0.16240.23610.1140.74381.43856.7668116.0054
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1CHAIN A AND (RESID 2 THROUGH 106 )
2X-RAY DIFFRACTION2CHAIN A AND (RESID 107 THROUGH 152 )
3X-RAY DIFFRACTION3CHAIN A AND (RESID 153 THROUGH 188 )
4X-RAY DIFFRACTION4CHAIN A AND (RESID 189 THROUGH 282 )
5X-RAY DIFFRACTION5CHAIN A AND (RESID 283 THROUGH 333 )
6X-RAY DIFFRACTION6CHAIN A AND (RESID 334 THROUGH 406 )
7X-RAY DIFFRACTION7CHAIN A AND (RESID 407 THROUGH 450 )
8X-RAY DIFFRACTION8CHAIN A AND (RESID 451 THROUGH 482 )

+
About Yorodumi

-
News

-
Feb 9, 2022. New format data for meta-information of EMDB entries

New format data for meta-information of EMDB entries

  • Version 3 of the EMDB header file is now the official format.
  • The previous official version 1.9 will be removed from the archive.

Related info.:EMDB header

External links:wwPDB to switch to version 3 of the EMDB data model

-
Aug 12, 2020. Covid-19 info

Covid-19 info

URL: https://pdbj.org/emnavi/covid19.php

New page: Covid-19 featured information page in EM Navigator.

Related info.:Covid-19 info / Mar 5, 2020. Novel coronavirus structure data

+
Mar 5, 2020. Novel coronavirus structure data

Novel coronavirus structure data

Related info.:Yorodumi Speices / Aug 12, 2020. Covid-19 info

External links:COVID-19 featured content - PDBj / Molecule of the Month (242):Coronavirus Proteases

+
Jan 31, 2019. EMDB accession codes are about to change! (news from PDBe EMDB page)

EMDB accession codes are about to change! (news from PDBe EMDB page)

  • The allocation of 4 digits for EMDB accession codes will soon come to an end. Whilst these codes will remain in use, new EMDB accession codes will include an additional digit and will expand incrementally as the available range of codes is exhausted. The current 4-digit format prefixed with “EMD-” (i.e. EMD-XXXX) will advance to a 5-digit format (i.e. EMD-XXXXX), and so on. It is currently estimated that the 4-digit codes will be depleted around Spring 2019, at which point the 5-digit format will come into force.
  • The EM Navigator/Yorodumi systems omit the EMD- prefix.

Related info.:Q: What is EMD? / ID/Accession-code notation in Yorodumi/EM Navigator

External links:EMDB Accession Codes are Changing Soon! / Contact to PDBj

+
Jul 12, 2017. Major update of PDB

Major update of PDB

  • wwPDB released updated PDB data conforming to the new PDBx/mmCIF dictionary.
  • This is a major update changing the version number from 4 to 5, and with Remediation, in which all the entries are updated.
  • In this update, many items about electron microscopy experimental information are reorganized (e.g. em_software).
  • Now, EM Navigator and Yorodumi are based on the updated data.

External links:wwPDB Remediation / Enriched Model Files Conforming to OneDep Data Standards Now Available in the PDB FTP Archive

-
Yorodumi

Thousand views of thousand structures

  • Yorodumi is a browser for structure data from EMDB, PDB, SASBDB, etc.
  • This page is also the successor to EM Navigator detail page, and also detail information page/front-end page for Omokage search.
  • The word "yorodu" (or yorozu) is an old Japanese word meaning "ten thousand". "mi" (miru) is to see.

Related info.:EMDB / PDB / SASBDB / Comparison of 3 databanks / Yorodumi Search / Aug 31, 2016. New EM Navigator & Yorodumi / Yorodumi Papers / Jmol/JSmol / Function and homology information / Changes in new EM Navigator and Yorodumi

Read more