[English] 日本語
Yorodumi
- PDB-8yfh: Structure of alpha-1,3-glucanase agn1 -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 8yfh
TitleStructure of alpha-1,3-glucanase agn1
ComponentsGlucan endo-1,3-alpha-glucosidase agn1
KeywordsHYDROLASE / glucanase
Function / homology
Function and homology information


glucan endo-1,3-alpha-glucosidase / cell septum edging catabolic process / glucan endo-1,3-alpha-glucosidase activity / fungal-type cell wall disassembly involved in conjugation with cellular fusion / mating projection actin fusion focus / mating projection tip / extracellular region
Similarity search - Function
Glycoside hydrolase family 71 / Glycosyl hydrolase family 71
Similarity search - Domain/homology
Glucan endo-1,3-alpha-glucosidase agn1
Similarity search - Component
Biological speciesSchizosaccharomyces pombe DM3650 (yeast)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.8 Å
AuthorsHoraguch, Y. / Yano, S. / Makabe, K.
Funding support1items
OrganizationGrant numberCountry
Not funded
CitationJournal: To Be Published
Title: Structure of alpha-1,3-glucanase agn1
Authors: Horaguchi, Y. / Yano, S. / Makabe, K.
History
DepositionFeb 24, 2024Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0Feb 26, 2025Provider: repository / Type: Initial release

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: Glucan endo-1,3-alpha-glucosidase agn1
B: Glucan endo-1,3-alpha-glucosidase agn1
C: Glucan endo-1,3-alpha-glucosidase agn1


Theoretical massNumber of molelcules
Total (without water)133,6053
Polymers133,6053
Non-polymers00
Water20,9331162
1
A: Glucan endo-1,3-alpha-glucosidase agn1


Theoretical massNumber of molelcules
Total (without water)44,5351
Polymers44,5351
Non-polymers00
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
B: Glucan endo-1,3-alpha-glucosidase agn1


Theoretical massNumber of molelcules
Total (without water)44,5351
Polymers44,5351
Non-polymers00
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
3
C: Glucan endo-1,3-alpha-glucosidase agn1


Theoretical massNumber of molelcules
Total (without water)44,5351
Polymers44,5351
Non-polymers00
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)69.534, 114.514, 109.111
Angle α, β, γ (deg.)90.000, 104.236, 90.000
Int Tables number4
Space group name H-MP1211
Space group name HallP2yb
Symmetry operation#1: x,y,z
#2: -x,y+1/2,-z

-
Components

#1: Protein Glucan endo-1,3-alpha-glucosidase agn1 / Endo-1 / 3-alpha-glucanase agn1


Mass: 44534.848 Da / Num. of mol.: 3
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Schizosaccharomyces pombe DM3650 (yeast)
Gene: agn1, SPAC14C4.09 / Production host: Escherichia coli (E. coli)
References: UniProt: O13716, glucan endo-1,3-alpha-glucosidase
#2: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 1162 / Source method: isolated from a natural source / Formula: H2O
Has protein modificationN

-
Experimental details

-
Experiment

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

-
Sample preparation

CrystalDensity Matthews: 3.15 Å3/Da / Density % sol: 60.97 %
Crystal growTemperature: 293 K / Method: vapor diffusion, hanging drop / Details: 0.9M Disodium Malonate, 0.1M HEPES pH 7.0

-
Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: Photon Factory / Beamline: BL-5A / Wavelength: 1 Å
DetectorType: DECTRIS PILATUS3 S 6M / Detector: PIXEL / Date: Jun 24, 2022
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 1.78→48.01 Å / Num. obs: 158150 / % possible obs: 100 % / Redundancy: 5.2 % / Biso Wilson estimate: 24.34 Å2 / CC1/2: 0.999 / Net I/σ(I): 21.3
Reflection shellResolution: 1.78→1.81 Å / Num. unique obs: 7813 / CC1/2: 0.791

-
Processing

Software
NameVersionClassification
XDSdata scaling
PHENIX1.17.1_3660refinement
Cootmodel building
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 1.8→19.99 Å / SU ML: 0.1602 / Cross valid method: FREE R-VALUE / σ(F): 1.35 / Phase error: 19.0924
Stereochemistry target values: GeoStd + Monomer Library + CDL v1.2
RfactorNum. reflection% reflection
Rfree0.1914 7578 4.96 %
Rwork0.1654 145243 -
obs0.1667 152821 99.95 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso mean: 28.01 Å2
Refinement stepCycle: LAST / Resolution: 1.8→19.99 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms9459 0 0 1162 10621
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00619753
X-RAY DIFFRACTIONf_angle_d0.776213353
X-RAY DIFFRACTIONf_chiral_restr0.0541419
X-RAY DIFFRACTIONf_plane_restr0.00591725
X-RAY DIFFRACTIONf_dihedral_angle_d5.97741311
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
1.8-1.820.26382360.22974852X-RAY DIFFRACTION99.96
1.82-1.840.25782510.22364852X-RAY DIFFRACTION100
1.84-1.860.26982490.21014792X-RAY DIFFRACTION99.94
1.86-1.890.22962270.20624855X-RAY DIFFRACTION99.98
1.89-1.910.25682570.20214837X-RAY DIFFRACTION99.98
1.91-1.940.24432570.19974822X-RAY DIFFRACTION99.96
1.94-1.970.21362560.18814795X-RAY DIFFRACTION99.94
1.97-20.21982610.18094816X-RAY DIFFRACTION99.9
2-2.030.21622690.17914841X-RAY DIFFRACTION99.98
2.03-2.060.20832670.17954822X-RAY DIFFRACTION99.94
2.06-2.10.20332560.17374820X-RAY DIFFRACTION99.98
2.1-2.130.212470.17484809X-RAY DIFFRACTION99.98
2.13-2.170.21072330.16924854X-RAY DIFFRACTION99.94
2.17-2.220.20922490.16624792X-RAY DIFFRACTION99.9
2.22-2.270.19632560.17244866X-RAY DIFFRACTION99.98
2.27-2.320.2052530.16834843X-RAY DIFFRACTION100
2.32-2.380.19332430.17574834X-RAY DIFFRACTION100
2.38-2.440.21672380.16834852X-RAY DIFFRACTION99.86
2.44-2.510.20832550.17614806X-RAY DIFFRACTION99.94
2.51-2.590.21342390.17434896X-RAY DIFFRACTION100
2.59-2.690.20632550.17794809X-RAY DIFFRACTION99.94
2.69-2.790.20372420.18274879X-RAY DIFFRACTION99.94
2.79-2.920.21082390.18344854X-RAY DIFFRACTION100
2.92-3.070.22582580.17974822X-RAY DIFFRACTION100
3.08-3.270.18712780.17184842X-RAY DIFFRACTION99.98
3.27-3.520.18422980.16034822X-RAY DIFFRACTION99.96
3.52-3.870.19152600.14464855X-RAY DIFFRACTION99.98
3.87-4.420.14722340.12714865X-RAY DIFFRACTION99.94
4.42-5.550.12852390.13284910X-RAY DIFFRACTION99.92
5.55-19.990.15792760.16344929X-RAY DIFFRACTION99.83

+
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