[English] 日本語
Yorodumi
- PDB-4g8l: Active state of intact sensor domain of human RNase L with 2-5A bound -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 4g8l
TitleActive state of intact sensor domain of human RNase L with 2-5A bound
Components2-5A-dependent ribonuclease
KeywordsHYDROLASE / Ankyrin-repeat domain / single-stranded RNA
Function / homology
Function and homology information


OAS antiviral response / Hydrolases; Acting on ester bonds; Endoribonucleases producing 5'-phosphomonoesters / negative regulation of viral genome replication / fat cell differentiation / RNA nuclease activity / RNA processing / ribonucleoprotein complex binding / RNA endonuclease activity / regulation of mRNA stability / positive regulation of glucose import ...OAS antiviral response / Hydrolases; Acting on ester bonds; Endoribonucleases producing 5'-phosphomonoesters / negative regulation of viral genome replication / fat cell differentiation / RNA nuclease activity / RNA processing / ribonucleoprotein complex binding / RNA endonuclease activity / regulation of mRNA stability / positive regulation of glucose import / mRNA processing / nuclear matrix / rRNA processing / Interferon alpha/beta signaling / defense response to virus / rRNA binding / protein kinase activity / mitochondrial matrix / protein phosphorylation / positive regulation of transcription by RNA polymerase II / RNA binding / ATP binding / identical protein binding / metal ion binding / cytosol
Similarity search - Function
RNase L, RNase domain / Ankyrin repeats (many copies) / KEN domain / KEN domain superfamily / Ribonuclease 2-5A / KEN domain profile. / domain in protein kinases, N-glycanases and other nuclear proteins / Ankyrin repeat-containing domain / Ankyrin repeat / Ankyrin repeats (3 copies) ...RNase L, RNase domain / Ankyrin repeats (many copies) / KEN domain / KEN domain superfamily / Ribonuclease 2-5A / KEN domain profile. / domain in protein kinases, N-glycanases and other nuclear proteins / Ankyrin repeat-containing domain / Ankyrin repeat / Ankyrin repeats (3 copies) / Ankyrin repeat profile. / Ankyrin repeat region circular profile. / ankyrin repeats / Ankyrin repeat / Ankyrin repeat-containing domain superfamily / Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat / Alpha Horseshoe / Protein kinase domain / Serine/Threonine protein kinases, catalytic domain / Protein kinase domain profile. / Protein kinase domain / Protein kinase-like domain superfamily / Mainly Alpha
Similarity search - Domain/homology
Chem-25A / 2-5A-dependent ribonuclease
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.8 Å
AuthorsHan, Y. / Whitney, G. / Donovan, J. / Korennykh, A.
CitationJournal: Cell Rep / Year: 2012
Title: Innate Immune Messenger 2-5A Tethers Human RNase L into Active High-Order Complexes.
Authors: Han, Y. / Whitney, G. / Donovan, J. / Korennykh, A.
History
DepositionJul 23, 2012Deposition site: RCSB / Processing site: RCSB
Revision 1.0Oct 31, 2012Provider: repository / Type: Initial release
Revision 1.1Nov 14, 2012Group: Database references
Revision 1.2Sep 13, 2023Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: 2-5A-dependent ribonuclease
B: 2-5A-dependent ribonuclease
C: 2-5A-dependent ribonuclease
D: 2-5A-dependent ribonuclease
hetero molecules


Theoretical massNumber of molelcules
Total (without water)152,6008
Polymers148,5774
Non-polymers4,0234
Water00
1
A: 2-5A-dependent ribonuclease
hetero molecules


Theoretical massNumber of molelcules
Total (without water)38,1502
Polymers37,1441
Non-polymers1,0061
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
2
B: 2-5A-dependent ribonuclease
hetero molecules


Theoretical massNumber of molelcules
Total (without water)38,1502
Polymers37,1441
Non-polymers1,0061
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
3
C: 2-5A-dependent ribonuclease
hetero molecules


Theoretical massNumber of molelcules
Total (without water)38,1502
Polymers37,1441
Non-polymers1,0061
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
4
D: 2-5A-dependent ribonuclease
hetero molecules


Theoretical massNumber of molelcules
Total (without water)38,1502
Polymers37,1441
Non-polymers1,0061
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
Unit cell
Length a, b, c (Å)62.980, 164.110, 86.220
Angle α, β, γ (deg.)90.00, 100.20, 90.00
Int Tables number4
Space group name H-MP1211
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-ID
11
21
31
41
12
22

NCS domain segments:
Dom-IDComponent-IDEns-IDSelection details
111CHAIN A AND (RESID 21:155 OR RESID 168:500 OR RESID 1996)
211chain B AND (RESID 21:155 OR RESID 168:500 OR RESID 1996)
311CHAIN C AND (RESID 21:155 OR RESID 168:500 OR RESID 1996)
411CHAIN D AND (RESID 21:155 OR RESID 168:500 OR RESID 1996)
112CHAIN A AND (RESID 1:20)
212CHAIN C AND (RESID 1:20)

NCS ensembles :
ID
1
2

-
Components

#1: Protein
2-5A-dependent ribonuclease / 2-5A-dependent RNase / Ribonuclease 4 / Ribonuclease L / RNase L


Mass: 37144.305 Da / Num. of mol.: 4 / Fragment: 2-5A-sensor domain (ANK domain)
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: RNASEL, RNS4 / Production host: Escherichia coli (E. coli)
References: UniProt: Q05823, Hydrolases; Acting on ester bonds; Endoribonucleases producing 5'-phosphomonoesters
#2: Chemical
ChemComp-25A / 5'-O-MONOPHOSPHORYLADENYLYL(2'->5')ADENYLYL(2'->5')ADENOSINE


Mass: 1005.633 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C30H38N15O19P3

-
Experimental details

-
Experiment

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

-
Sample preparation

CrystalDensity Matthews: 2.95 Å3/Da / Density % sol: 58.33 %
Crystal growTemperature: 293 K / Method: vapor diffusion / pH: 7
Details: 200 mM sodium acetate, 18% PEG 3350, 1.3M sodium citrate, pH 7.0, VAPOR DIFFUSION, temperature 293K

-
Data collection

DiffractionMean temperature: 77 K
Diffraction sourceSource: SYNCHROTRON / Site: NSLS / Beamline: X29A / Wavelength: 1.072 Å
DetectorType: ADSC QUANTUM 315 / Detector: CCD / Date: Mar 11, 2012
RadiationMonochromator: Si 111 CHANNEL / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.072 Å / Relative weight: 1
ReflectionResolution: 2.8→39 Å / Num. obs: 42322 / % possible obs: 99.8 % / Observed criterion σ(F): 1.82 / Observed criterion σ(I): 1.82
Reflection shell
Resolution (Å)Diffraction-ID% possible all
2.8-2.9199.8
2.9-4199.8
4-6199.8
6-10199.9
10-10199.8
10-201100
20-301100
30-40195

-
Processing

Software
NameVersionClassification
CBASSdata collection
PHASERphasing
PHENIX(phenix.refine: 1.5_2)refinement
XDSdata reduction
XDSdata scaling
SCALAdata scaling
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB entry 4G8K
Resolution: 2.8→38.75 Å / SU ML: 0.34 / σ(F): 1.99 / Phase error: 32.48 / Stereochemistry target values: ML
RfactorNum. reflection% reflectionSelection details
Rfree0.2609 2115 5.01 %RANDOM
Rwork0.2282 ---
obs0.2299 42245 99.74 %-
all-42322 --
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 44.122 Å2 / ksol: 0.344 e/Å3
Displacement parameters
Baniso -1Baniso -2Baniso -3
1--17.769 Å20 Å2-10.7293 Å2
2---15.2196 Å2-0 Å2
3---29.2152 Å2
Refinement stepCycle: LAST / Resolution: 2.8→38.75 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms9147 0 268 0 9415
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0069547
X-RAY DIFFRACTIONf_angle_d0.98512912
X-RAY DIFFRACTIONf_dihedral_angle_d23.0256086
X-RAY DIFFRACTIONf_chiral_restr0.0631523
X-RAY DIFFRACTIONf_plane_restr0.0041622
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDNumberRefine-IDTypeRms dev position (Å)
11A2292X-RAY DIFFRACTIONPOSITIONAL
12B2292X-RAY DIFFRACTIONPOSITIONAL0.026
13C2288X-RAY DIFFRACTIONPOSITIONAL0.027
14D2292X-RAY DIFFRACTIONPOSITIONAL0.029
21A38X-RAY DIFFRACTIONPOSITIONAL
22C38X-RAY DIFFRACTIONPOSITIONAL0.03
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.8-2.86510.40741430.37182700X-RAY DIFFRACTION100
2.8651-2.93680.30691380.32422622X-RAY DIFFRACTION100
2.9368-3.01610.40741410.30412671X-RAY DIFFRACTION100
3.0161-3.10480.31751390.30442655X-RAY DIFFRACTION100
3.1048-3.2050.37011410.27562678X-RAY DIFFRACTION100
3.205-3.31950.28471430.26512694X-RAY DIFFRACTION100
3.3195-3.45230.31261390.23352648X-RAY DIFFRACTION100
3.4523-3.60930.25071400.22822654X-RAY DIFFRACTION100
3.6093-3.79950.22871400.20932663X-RAY DIFFRACTION100
3.7995-4.03730.26481420.21142690X-RAY DIFFRACTION100
4.0373-4.34860.21521410.18912670X-RAY DIFFRACTION100
4.3486-4.78550.23041430.18542709X-RAY DIFFRACTION100
4.7855-5.47640.23091400.19722665X-RAY DIFFRACTION100
5.4764-6.89330.25911430.21082704X-RAY DIFFRACTION100
6.8933-38.75380.16561420.17782707X-RAY DIFFRACTION99
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)
10.1926-0.1427-0.01590.2660.21720.2199-0.05160.1742-0.3087-0.09470.02380.04390.03450.1528-0.04810.2035-0.0198-0.029-0.0972-0.08920.25398.0005-29.068836.4262
20.0902-0.08570.09240.2246-0.11640.0262-0.04860.13030.3079-0.0317-0.0017-0.1314-0.00590.0388-0.00230.2132-0.0152-0.00870.09720.02470.25368.5849-65.460537.7839
30.85820.3250.05460.22450.09790.0274-0.09550.03130.4299-0.05230.09980.1047-0.0175-0.02880.20690.10270.06490.02370.347-0.22460.106416.3004-81.48435.6532
40.09380.02230.07630.1579-0.00030.044-0.08150.1134-0.3717-0.01150.0379-0.10620.0295-0.04470.00580.10030.0359-0.00180.32490.20710.405215.9787-44.95634.5239
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1CHAIN A AND RESID 16:325
2X-RAY DIFFRACTION2CHAIN B AND RESID 21:325
3X-RAY DIFFRACTION3CHAIN C AND RESID 15:325
4X-RAY DIFFRACTION4CHAIN D AND RESID 21:325

+
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://pdbjlvh1.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