[English] 日本語
Yorodumi
- PDB-1vlr: Crystal structure of mRNA decapping enzyme (DcpS) from Mus muscul... -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 1vlr
TitleCrystal structure of mRNA decapping enzyme (DcpS) from Mus musculus at 1.83 A resolution
ComponentsmRNA decapping enzyme
KeywordsRNA BINDING PROTEIN / 16740816 / mRNA decapping enzyme (DcpS) / STRUCTURAL GENOMICS / JCSG / PROTEIN STRUCTURE INITIATIVE / PSI / Joint Center for Structural Genomics
Function / homology
Function and homology information


cellular response to menadione / : / mRNA decay by 3' to 5' exoribonuclease / 5'-(N7-methyl 5'-triphosphoguanosine)-[mRNA] diphosphatase / deadenylation-dependent decapping of nuclear-transcribed mRNA / RNA 7-methylguanosine cap binding / mRNA cis splicing, via spliceosome / negative regulation of programmed cell death / P-body / mitochondrion ...cellular response to menadione / : / mRNA decay by 3' to 5' exoribonuclease / 5'-(N7-methyl 5'-triphosphoguanosine)-[mRNA] diphosphatase / deadenylation-dependent decapping of nuclear-transcribed mRNA / RNA 7-methylguanosine cap binding / mRNA cis splicing, via spliceosome / negative regulation of programmed cell death / P-body / mitochondrion / nucleoplasm / identical protein binding / nucleus / cytoplasm / cytosol
Similarity search - Function
mRNA decapping enzyme DcpS N-terminal fold / mRNA decapping enzyme DcpS N-terminal domain / Scavenger mRNA decapping enzyme, N-terminal domain / Scavenger mRNA decapping enzyme DcpS/DCS2 / Scavenger mRNA decapping enzyme, N-terminal / Scavenger mRNA decapping enzyme (DcpS) N-terminal / Scavenger mRNA decapping enzyme C-term binding / Histidine triad, conserved site / HIT domain signature. / HIT-like ...mRNA decapping enzyme DcpS N-terminal fold / mRNA decapping enzyme DcpS N-terminal domain / Scavenger mRNA decapping enzyme, N-terminal domain / Scavenger mRNA decapping enzyme DcpS/DCS2 / Scavenger mRNA decapping enzyme, N-terminal / Scavenger mRNA decapping enzyme (DcpS) N-terminal / Scavenger mRNA decapping enzyme C-term binding / Histidine triad, conserved site / HIT domain signature. / HIT-like / HIT family, subunit A / HIT-like superfamily / Phosphorylase Kinase; domain 1 / 2-Layer Sandwich / Alpha Beta
Similarity search - Domain/homology
m7GpppX diphosphatase
Similarity search - Component
Biological speciesMus musculus (house mouse)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.83 Å
AuthorsJoint Center for Structural Genomics (JCSG)
CitationJournal: Proteins / Year: 2005
Title: Crystal structure of an Apo mRNA decapping enzyme (DcpS) from Mouse at 1.83 A resolution.
Authors: Han, G.W. / Schwarzenbacher, R. / McMullan, D. / Abdubek, P. / Ambing, E. / Axelrod, H. / Biorac, T. / Canaves, J.M. / Chiu, H.J. / Dai, X. / Deacon, A.M. / DiDonato, M. / Elsliger, M.A. / ...Authors: Han, G.W. / Schwarzenbacher, R. / McMullan, D. / Abdubek, P. / Ambing, E. / Axelrod, H. / Biorac, T. / Canaves, J.M. / Chiu, H.J. / Dai, X. / Deacon, A.M. / DiDonato, M. / Elsliger, M.A. / Godzik, A. / Grittini, C. / Grzechnik, S.K. / Hale, J. / Hampton, E. / Haugen, J. / Hornsby, M. / Jaroszewski, L. / Klock, H.E. / Koesema, E. / Kreusch, A. / Kuhn, P. / Lesley, S.A. / McPhillips, T.M. / Miller, M.D. / Moy, K. / Nigoghossian, E. / Paulsen, J. / Quijano, K. / Reyes, R. / Spraggon, G. / Stevens, R.C. / van den Bedem, H. / Velasquez, J. / Vincent, J. / White, A. / Wolf, G. / Xu, Q. / Hodgson, K.O. / Wooley, J. / Wilson, I.A.
History
DepositionAug 10, 2004Deposition site: RCSB / Processing site: RCSB
Revision 1.0Aug 24, 2004Provider: repository / Type: Initial release
Revision 1.1Apr 26, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Jan 25, 2023Group: Database references / Derived calculations / Category: database_2 / struct_ref_seq_dif / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_ref_seq_dif.details / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id
Revision 1.4Sep 20, 2023Group: Data collection / Refinement description
Category: chem_comp_atom / chem_comp_bond / pdbx_initial_refinement_model

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: mRNA decapping enzyme
B: mRNA decapping enzyme
hetero molecules


Theoretical massNumber of molelcules
Total (without water)81,3828
Polymers81,0102
Non-polymers3726
Water14,520806
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area8820 Å2
ΔGint-24 kcal/mol
Surface area27390 Å2
MethodPISA
Unit cell
Length a, b, c (Å)65.399, 59.231, 100.140
Angle α, β, γ (deg.)90.00, 103.80, 90.00
Int Tables number4
Space group name H-MP1211

-
Components

#1: Protein mRNA decapping enzyme / histidine triad protein member 5


Mass: 40504.754 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mus musculus (house mouse) / Gene: DcpS / Production host: Escherichia coli (E. coli) / References: UniProt: Q9DAR7
#2: Chemical
ChemComp-EDO / 1,2-ETHANEDIOL / ETHYLENE GLYCOL


Mass: 62.068 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: C2H6O2
#3: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 806 / 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: 2.35 Å3/Da / Density % sol: 47.29 %
Crystal growTemperature: 277 K / Method: vapor diffusion, sitting drop, nanodrop / pH: 7.2
Details: 0.2M KF, 20.0% PEG-3350, No Buffer pH 7.2, VAPOR DIFFUSION,SITTING DROP,NANODROP, temperature 277K

-
Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: ALS / Beamline: 5.0.3 / Wavelength: 1
DetectorType: ADSC / Detector: CCD / Date: Oct 8, 2003
RadiationMonochromator: Single crystal, cylindrically bent, Si(220) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 1.83→37.58 Å / Num. obs: 64852 / % possible obs: 97.9 % / Redundancy: 3.69 % / Biso Wilson estimate: 24.23 Å2 / Rsym value: 0.063 / Net I/σ(I): 18.07
Reflection shellResolution: 1.83→1.9 Å / Redundancy: 3.07 % / Mean I/σ(I) obs: 3.04 / Num. unique all: 5575 / Rsym value: 0.389 / % possible all: 84.84

-
Processing

Software
NameVersionClassification
DENZOdata reduction
SCALEPACKdata scaling
MOLREPphasing
REFMAC5.2.0001refinement
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 1st0

1st0


Resolution: 1.83→37.58 Å / Cor.coef. Fo:Fc: 0.96 / Cor.coef. Fo:Fc free: 0.932 / SU B: 2.301 / SU ML: 0.072 / Cross valid method: THROUGHOUT / ESU R: 0.114 / ESU R Free: 0.115 / Stereochemistry target values: MAXIMUM LIKELIHOOD
Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. THERE IS A LARGE UNMODELED PEAK IN THE DIFFERENCE MAP NEAR THE CARBONYL OXYGEN OF PRO-287 IN BOTH CHAINS.
RfactorNum. reflection% reflectionSelection details
Rfree0.20101 3300 5.1 %RANDOM
Rwork0.15838 ---
obs0.16053 61546 97.69 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: BABINET MODEL WITH MASK
Displacement parametersBiso mean: 15.046 Å2
Baniso -1Baniso -2Baniso -3
1-0.07 Å20 Å20.28 Å2
2--0.31 Å20 Å2
3----0.25 Å2
Refinement stepCycle: LAST / Resolution: 1.83→37.58 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms4885 0 24 812 5721
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0180.0225021
X-RAY DIFFRACTIONr_bond_other_d0.0020.024668
X-RAY DIFFRACTIONr_angle_refined_deg1.6671.9566816
X-RAY DIFFRACTIONr_angle_other_deg1.036310820
X-RAY DIFFRACTIONr_dihedral_angle_1_deg6.4295593
X-RAY DIFFRACTIONr_dihedral_angle_2_deg34.32423.15254
X-RAY DIFFRACTIONr_dihedral_angle_3_deg13.13715885
X-RAY DIFFRACTIONr_dihedral_angle_4_deg18.6911548
X-RAY DIFFRACTIONr_chiral_restr0.1040.2768
X-RAY DIFFRACTIONr_gen_planes_refined0.0080.025497
X-RAY DIFFRACTIONr_gen_planes_other0.0010.021043
X-RAY DIFFRACTIONr_nbd_refined0.2150.21003
X-RAY DIFFRACTIONr_nbd_other0.1990.25150
X-RAY DIFFRACTIONr_nbtor_other0.0870.23254
X-RAY DIFFRACTIONr_xyhbond_nbd_refined0.1430.2612
X-RAY DIFFRACTIONr_symmetry_vdw_refined0.2250.228
X-RAY DIFFRACTIONr_symmetry_vdw_other0.2820.2117
X-RAY DIFFRACTIONr_symmetry_hbond_refined0.2060.270
X-RAY DIFFRACTIONr_mcbond_it1.2891.53154
X-RAY DIFFRACTIONr_mcbond_other0.3341.51174
X-RAY DIFFRACTIONr_mcangle_it1.79824858
X-RAY DIFFRACTIONr_scbond_it2.75132211
X-RAY DIFFRACTIONr_scangle_it3.8644.51958
X-RAY DIFFRACTIONr_xyhbond_nbd_other0.0150.21
LS refinement shellResolution: 1.825→1.873 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.255 185 4.79 %
Rwork0.195 3680 -

+
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