[English] 日本語
Yorodumi
- PDB-8jmq: Crystal structure of hinokiresinol synthase -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 8jmq
TitleCrystal structure of hinokiresinol synthase
Components
  • Hinokiresinol synthase alpha subunit
  • Hinokiresinol synthase beta subunit
KeywordsBIOSYNTHETIC PROTEIN / hinokiresinol / hinokiresinol synthase
Function / homology: / Phloem protein 2-like / Phloem protein 2 / carbohydrate binding / Hinokiresinol synthase alpha subunit / Hinokiresinol synthase beta subunit
Function and homology information
Biological speciesAsparagus officinalis (garden asparagus)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2 Å
AuthorsDing, Y. / Ushimaru, R. / Mori, T. / Abe, I.
Funding support1items
OrganizationGrant numberCountry
Not funded
CitationJournal: J.Am.Chem.Soc. / Year: 2023
Title: Structural and Mechanistic Insights into the C-C Bond-Forming Rearrangement Reaction Catalyzed by Heterodimeric Hinokiresinol Synthase.
Authors: Ushimaru, R. / Ding, Y. / Mori, T. / Miyamoto, K. / Uchiyama, M. / Abe, I.
History
DepositionJun 5, 2023Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0Dec 20, 2023Provider: repository / Type: Initial release
Revision 1.1Oct 16, 2024Group: Structure summary / Category: pdbx_entry_details / pdbx_modification_feature

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
B: Hinokiresinol synthase beta subunit
A: Hinokiresinol synthase alpha subunit


Theoretical massNumber of molelcules
Total (without water)42,3892
Polymers42,3892
Non-polymers00
Water4,360242
1


  • Idetical with deposited unit
  • defined by author&software
  • Evidence: gel filtration
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area4670 Å2
ΔGint-23 kcal/mol
Surface area14020 Å2
MethodPISA
Unit cell
Length a, b, c (Å)105.974, 105.974, 105.974
Angle α, β, γ (deg.)90.000, 90.000, 90.000
Int Tables number198
Space group name H-MP213
Space group name HallP2ac2ab3
Symmetry operation#1: x,y,z
#2: z,x,y
#3: y,z,x
#4: -y+1/2,-z,x+1/2
#5: z+1/2,-x+1/2,-y
#6: -y,z+1/2,-x+1/2
#7: -z+1/2,-x,y+1/2
#8: -z,x+1/2,-y+1/2
#9: y+1/2,-z+1/2,-x
#10: x+1/2,-y+1/2,-z
#11: -x,y+1/2,-z+1/2
#12: -x+1/2,-y,z+1/2

-
Components

#1: Protein Hinokiresinol synthase beta subunit


Mass: 22212.457 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Asparagus officinalis (garden asparagus)
Gene: AoHRSb / Production host: Escherichia coli (E. coli) / References: UniProt: A9CQD5
#2: Protein Hinokiresinol synthase alpha subunit


Mass: 20176.369 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Asparagus officinalis (garden asparagus)
Gene: AoHRSa / Production host: Escherichia coli (E. coli) / References: UniProt: A9CQD3
#3: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 242 / Source method: isolated from a natural source / Formula: H2O
Has protein modificationY

-
Experimental details

-
Experiment

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

-
Sample preparation

CrystalDensity Matthews: 2.47 Å3/Da / Density % sol: 50.29 %
Crystal growTemperature: 293 K / Method: vapor diffusion, sitting drop / Details: 100mM Tacsimate, 20% PEG 4000, 1M LiCl

-
Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: Photon Factory / Beamline: BL-1A / Wavelength: 1.1 Å
DetectorType: DECTRIS EIGER X 4M / Detector: PIXEL / Date: Oct 30, 2021
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.1 Å / Relative weight: 1
ReflectionResolution: 2→47.39 Å / Num. obs: 27084 / % possible obs: 100 % / Redundancy: 68.9 % / Biso Wilson estimate: 29.99 Å2 / CC1/2: 1 / Rmerge(I) obs: 0.07 / Net I/σ(I): 53.6
Reflection shellResolution: 2→2.05 Å / Redundancy: 22.4 % / Rmerge(I) obs: 0.637 / Mean I/σ(I) obs: 5.3 / Num. unique obs: 1998 / CC1/2: 0.937 / % possible all: 100

-
Processing

Software
NameVersionClassification
PHENIX1.19.2_4158refinement
XDSdata reduction
Aimlessdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 2→47.39 Å / SU ML: 0.2011 / Cross valid method: FREE R-VALUE / σ(F): 1.36 / Phase error: 20.3664
Stereochemistry target values: GeoStd + Monomer Library + CDL v1.2
RfactorNum. reflection% reflection
Rfree0.2039 2001 7.4 %
Rwork0.1601 25055 -
obs0.1633 27056 99.99 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso mean: 31.72 Å2
Refinement stepCycle: LAST / Resolution: 2→47.39 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms2671 0 0 243 2914
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00682755
X-RAY DIFFRACTIONf_angle_d0.90453741
X-RAY DIFFRACTIONf_chiral_restr0.0607417
X-RAY DIFFRACTIONf_plane_restr0.0059480
X-RAY DIFFRACTIONf_dihedral_angle_d6.8693368
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2-2.050.25931440.19361754X-RAY DIFFRACTION100
2.05-2.110.23141400.16741784X-RAY DIFFRACTION100
2.11-2.170.21091440.16631770X-RAY DIFFRACTION100
2.17-2.240.20551420.16231785X-RAY DIFFRACTION100
2.24-2.320.21331400.1771741X-RAY DIFFRACTION100
2.32-2.410.22191450.16751788X-RAY DIFFRACTION100
2.41-2.520.21891420.18881785X-RAY DIFFRACTION99.95
2.52-2.650.24931420.1671752X-RAY DIFFRACTION100
2.65-2.820.221420.18211802X-RAY DIFFRACTION100
2.82-3.040.23991390.18061785X-RAY DIFFRACTION100
3.04-3.340.21121450.16851795X-RAY DIFFRACTION100
3.34-3.820.18341410.14611804X-RAY DIFFRACTION100
3.83-4.820.16691410.12691827X-RAY DIFFRACTION99.95
4.82-47.390.19381540.16211883X-RAY DIFFRACTION99.95

+
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