[English] 日本語
Yorodumi
- PDB-6a73: Complex structure of CSN2 with IP6 -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 6a73
TitleComplex structure of CSN2 with IP6
ComponentsCOP9 signalosome complex subunit 2,Endolysin
KeywordsSIGNALING PROTEIN / subunit2 of COP9 Signalosome (CSN).
Function / homology
Function and homology information


trophectodermal cell proliferation / protein deneddylation / regulation of protein neddylation / COP9 signalosome / protein neddylation / RHOBTB1 GTPase cycle / inner cell mass cell proliferation / skeletal muscle cell differentiation / viral release from host cell by cytolysis / peptidoglycan catabolic process ...trophectodermal cell proliferation / protein deneddylation / regulation of protein neddylation / COP9 signalosome / protein neddylation / RHOBTB1 GTPase cycle / inner cell mass cell proliferation / skeletal muscle cell differentiation / viral release from host cell by cytolysis / peptidoglycan catabolic process / DNA Damage Recognition in GG-NER / neuron differentiation / Formation of TC-NER Pre-Incision Complex / transcription corepressor activity / cell wall macromolecule catabolic process / Cargo recognition for clathrin-mediated endocytosis / lysozyme / lysozyme activity / Neddylation / host cell cytoplasm / transcription by RNA polymerase II / defense response to bacterium / protein phosphorylation / negative regulation of transcription by RNA polymerase II / signal transduction / nucleoplasm / nucleus / cytosol / cytoplasm
Similarity search - Function
: / PCI/PINT associated module / motif in proteasome subunits, Int-6, Nip-1 and TRIP-15 / PCI domain / Proteasome component (PCI) domain / PCI domain profile. / Endolysin T4 type / T4-type lysozyme / : / Glycoside hydrolase, family 24 ...: / PCI/PINT associated module / motif in proteasome subunits, Int-6, Nip-1 and TRIP-15 / PCI domain / Proteasome component (PCI) domain / PCI domain profile. / Endolysin T4 type / T4-type lysozyme / : / Glycoside hydrolase, family 24 / Phage lysozyme / Lysozyme domain superfamily / Lysozyme-like domain superfamily / Tetratricopeptide-like helical domain superfamily / Winged helix DNA-binding domain superfamily
Similarity search - Domain/homology
INOSITOL HEXAKISPHOSPHATE / Endolysin / COP9 signalosome complex subunit 2
Similarity search - Component
Biological speciesHomo sapiens (human)
Enterobacteria phage RB59 (virus)
MethodX-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 2.447 Å
AuthorsLiu, L. / Li, D. / Rao, F. / Wang, T.
Funding support China, 1items
OrganizationGrant numberCountry
Ministry of Science and Technology (China)2018YFA0507103 China
CitationJournal: Proc.Natl.Acad.Sci.USA / Year: 2020
Title: Basis for metabolite-dependent Cullin-RING ligase deneddylation by the COP9 signalosome.
Authors: Lin, H. / Zhang, X. / Liu, L. / Fu, Q. / Zang, C. / Ding, Y. / Su, Y. / Xu, Z. / He, S. / Yang, X. / Wei, X. / Mao, H. / Cui, Y. / Wei, Y. / Zhou, C. / Du, L. / Huang, N. / Zheng, N. / Wang, T. / Rao, F.
History
DepositionJul 2, 2018Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0Jul 3, 2019Provider: repository / Type: Initial release
Revision 1.1Feb 12, 2020Group: Database references / Category: citation / citation_author
Item: _citation.country / _citation.journal_abbrev ..._citation.country / _citation.journal_abbrev / _citation.journal_id_ASTM / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.pdbx_database_id_DOI / _citation.title / _citation.year
Revision 1.2Feb 26, 2020Group: Database references / Category: citation / Item: _citation.pdbx_database_id_PubMed / _citation.title
Revision 1.3Mar 11, 2020Group: Database references / Category: citation
Item: _citation.journal_volume / _citation.page_first / _citation.page_last
Revision 1.4Oct 14, 2020Group: Structure summary / Category: chem_comp / Item: _chem_comp.pdbx_synonyms
Revision 1.5Nov 22, 2023Group: Data collection / Database references / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: COP9 signalosome complex subunit 2,Endolysin
B: COP9 signalosome complex subunit 2,Endolysin
hetero molecules


Theoretical massNumber of molelcules
Total (without water)72,1436
Polymers70,6312
Non-polymers1,5124
Water3,081171
1
A: COP9 signalosome complex subunit 2,Endolysin
hetero molecules


Theoretical massNumber of molelcules
Total (without water)36,0713
Polymers35,3151
Non-polymers7562
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area760 Å2
ΔGint-19 kcal/mol
Surface area15860 Å2
MethodPISA
2
B: COP9 signalosome complex subunit 2,Endolysin
hetero molecules


Theoretical massNumber of molelcules
Total (without water)36,0713
Polymers35,3151
Non-polymers7562
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area570 Å2
ΔGint-6 kcal/mol
Surface area15860 Å2
MethodPISA
Unit cell
Length a, b, c (Å)39.804, 70.164, 81.350
Angle α, β, γ (deg.)107.03, 103.94, 90.25
Int Tables number1
Space group name H-MP1

-
Components

#1: Protein COP9 signalosome complex subunit 2,Endolysin / Signalosome subunit 2 / Alien homolog / JAB1-containing signalosome subunit 2 / Thyroid receptor- ...Signalosome subunit 2 / Alien homolog / JAB1-containing signalosome subunit 2 / Thyroid receptor-interacting protein 15 / TRIP-15 / Lysis protein / Lysozyme / Muramidase


Mass: 35315.383 Da / Num. of mol.: 2 / Mutation: C54T, C97A
Source method: isolated from a genetically manipulated source
Details: human CSN2 hybrid with lysozyme,human CSN2 hybrid with lysozyme,human CSN2 hybrid with lysozyme,human CSN2 hybrid with lysozyme
Source: (gene. exp.) Homo sapiens (human), (gene. exp.) Enterobacteria phage RB59 (virus)
Gene: COPS2, CSN2, TRIP15, e, RB59_126 / Production host: Escherichia coli (E. coli) / References: UniProt: P61201, UniProt: A0A097J809, lysozyme
#2: Chemical ChemComp-IHP / INOSITOL HEXAKISPHOSPHATE / MYO-INOSITOL HEXAKISPHOSPHATE / INOSITOL 1,2,3,4,5,6-HEXAKISPHOSPHATE


Mass: 660.035 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C6H18O24P6
#3: Chemical ChemComp-SO4 / SULFATE ION


Mass: 96.063 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: SO4
#4: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 171 / 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: 3.13 Å3/Da / Density % sol: 60.73 %
Crystal growTemperature: 293 K / Method: vapor diffusion, hanging drop
Details: 0.2 M ammonium sulfate ,100mM Bis-Tris pH 5.5, 25%PEG 3350.

-
Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: ROTATING ANODE / Type: RIGAKU MICROMAX-007 / Wavelength: 1.5418 Å
DetectorType: DECTRIS PILATUS 200K / Detector: PIXEL / Date: Feb 10, 2018
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.5418 Å / Relative weight: 1
ReflectionResolution: 2.447→20.003 Å / Num. obs: 27516 / % possible obs: 91.8 % / Redundancy: 1.8 % / Rmerge(I) obs: 0.025 / Net I/σ(I): 26.1
Reflection shellResolution: 2.45→2.49 Å / Rmerge(I) obs: 0.189 / Num. unique obs: 1305 / % possible all: 87.6

-
Processing

Software
NameVersionClassification
PHENIX(1.13_2998: ???)refinement
HKL-3000data reduction
HKL-3000data scaling
PHENIXphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 1L17 and 4ZWJ
Resolution: 2.447→20.003 Å / SU ML: 0.42 / Cross valid method: FREE R-VALUE / σ(F): 1.82 / Phase error: 34.29
RfactorNum. reflection% reflectionSelection details
Rfree0.2879 1379 5.01 %Random Selection
Rwork0.2473 ---
obs0.2503 27504 91.72 %-
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å
Refinement stepCycle: LAST / Resolution: 2.447→20.003 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms4720 0 82 171 4973
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0054881
X-RAY DIFFRACTIONf_angle_d0.9256588
X-RAY DIFFRACTIONf_dihedral_angle_d18.1252946
X-RAY DIFFRACTIONf_chiral_restr0.046720
X-RAY DIFFRACTIONf_plane_restr0.005820
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.4471-2.53440.42541120.30542059X-RAY DIFFRACTION72
2.5344-2.63570.31861340.27592435X-RAY DIFFRACTION86
2.6357-2.75540.3431380.28592566X-RAY DIFFRACTION90
2.7554-2.90020.35951410.30212626X-RAY DIFFRACTION92
2.9002-3.08130.38621350.30362677X-RAY DIFFRACTION94
3.0813-3.31820.30111430.26542734X-RAY DIFFRACTION96
3.3182-3.65030.30461390.24042749X-RAY DIFFRACTION96
3.6503-4.17440.3041430.21932715X-RAY DIFFRACTION97
4.1744-5.24350.27261490.21372772X-RAY DIFFRACTION97
5.2435-20.00380.25771450.22862792X-RAY DIFFRACTION97
Refinement TLS params.Method: refined / Origin x: -9.3689 Å / Origin y: 7.5026 Å / Origin z: -57.8356 Å
111213212223313233
T0.2327 Å20.0054 Å20 Å2-0.2848 Å20.0012 Å2--0.4472 Å2
L0.5641 °20.0318 °2-0.0254 °2--0.3198 °2-1.1332 °2--4.6581 °2
S-0.1767 Å °0.0081 Å °-0.0041 Å °-0.0046 Å °-0.2214 Å °-0.2043 Å °0.0212 Å °0.5886 Å °0.2621 Å °
Refinement TLS groupSelection details: all

+
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