[English] 日本語
Yorodumi
- PDB-8yeb: Crystal structure of L-ribulose 3-epimerase from Arthrobacter glo... -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 8yeb
TitleCrystal structure of L-ribulose 3-epimerase from Arthrobacter globiformis M30
ComponentsKetose 3-epimerase
KeywordsISOMERASE / D-allulose / ketose 3-epimerase / HYDROLASE
Function / homology
Function and homology information


Isomerases; Racemases and epimerases; Acting on carbohydrates and derivatives / racemase and epimerase activity, acting on carbohydrates and derivatives / manganese ion binding / carbohydrate metabolic process
Similarity search - Function
: / Xylose isomerase-like, TIM barrel domain / Xylose isomerase-like TIM barrel / Xylose isomerase-like superfamily
Similarity search - Domain/homology
DI(HYDROXYETHYL)ETHER / Ketose 3-epimerase
Similarity search - Component
Biological speciesArthrobacter globiformis (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.2 Å
AuthorsWatanabe, M. / Nakamich, Y. / Mine, S.
Funding support1items
OrganizationGrant numberCountry
Not funded
CitationJournal: To Be Published
Title: Crystal structure of L-ribulose 3-epimerase from Arthrobacter globiformis M30
Authors: Watanabe, M. / Nakamich, Y. / Mine, S.
History
DepositionFeb 22, 2024Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0Feb 12, 2025Provider: repository / Type: Initial release

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: Ketose 3-epimerase
E: Ketose 3-epimerase
B: Ketose 3-epimerase
C: Ketose 3-epimerase
D: Ketose 3-epimerase
F: Ketose 3-epimerase
G: Ketose 3-epimerase
H: Ketose 3-epimerase
I: Ketose 3-epimerase
J: Ketose 3-epimerase
K: Ketose 3-epimerase
L: Ketose 3-epimerase
M: Ketose 3-epimerase
N: Ketose 3-epimerase
O: Ketose 3-epimerase
P: Ketose 3-epimerase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)517,98736
Polymers517,17316
Non-polymers81320
Water22,3211239
1
A: Ketose 3-epimerase
E: Ketose 3-epimerase
G: Ketose 3-epimerase
H: Ketose 3-epimerase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)129,60310
Polymers129,2934
Non-polymers3096
Water724
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area12420 Å2
ΔGint-50 kcal/mol
Surface area36430 Å2
MethodPISA
2
B: Ketose 3-epimerase
C: Ketose 3-epimerase
hetero molecules

D: Ketose 3-epimerase
F: Ketose 3-epimerase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)129,60310
Polymers129,2934
Non-polymers3096
Water724
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation2_655-x+1,y+1/2,-z1
Buried area12330 Å2
ΔGint-51 kcal/mol
Surface area36720 Å2
MethodPISA
3
I: Ketose 3-epimerase
J: Ketose 3-epimerase
K: Ketose 3-epimerase
L: Ketose 3-epimerase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)129,3918
Polymers129,2934
Non-polymers974
Water724
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area11920 Å2
ΔGint-56 kcal/mol
Surface area36680 Å2
MethodPISA
4
M: Ketose 3-epimerase
N: Ketose 3-epimerase
hetero molecules

O: Ketose 3-epimerase
P: Ketose 3-epimerase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)129,3918
Polymers129,2934
Non-polymers974
Water724
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation2_654-x+1,y+1/2,-z-11
Buried area11840 Å2
ΔGint-52 kcal/mol
Surface area36570 Å2
MethodPISA
Unit cell
Length a, b, c (Å)130.095, 148.264, 136.707
Angle α, β, γ (deg.)90.00, 94.97, 90.00
Int Tables number4
Space group name H-MP1211

-
Components

#1: Protein
Ketose 3-epimerase / D-allulose 3-epimerase / D-AE / L-ribulose 3-epimerase


Mass: 32323.332 Da / Num. of mol.: 16
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Arthrobacter globiformis (bacteria) / Gene: DAE / Production host: Escherichia coli BL21(DE3) (bacteria)
References: UniProt: A0A1L7NQ96, Isomerases; Racemases and epimerases; Acting on carbohydrates and derivatives
#2: Chemical
ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 16 / Source method: obtained synthetically / Formula: Mg / Feature type: SUBJECT OF INVESTIGATION
#3: Chemical
ChemComp-PEG / DI(HYDROXYETHYL)ETHER


Mass: 106.120 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C4H10O3 / Feature type: SUBJECT OF INVESTIGATION
#4: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 1239 / Source method: isolated from a natural source / Formula: H2O
Has ligand of interestY
Has protein modificationN

-
Experimental details

-
Experiment

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

-
Sample preparation

CrystalDensity Matthews: 2.54 Å3/Da / Density % sol: 51.57 %
Crystal growTemperature: 293 K / Method: vapor diffusion, hanging drop
Details: 25% PEG 3350, 200mM Ammonium acetate, 100mM BIS-TRIS pH 5.5

-
Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: SPring-8 / Beamline: BL44XU / Wavelength: 0.9 Å
DetectorType: DECTRIS EIGER X 16M / Detector: PIXEL / Date: Jul 22, 2019
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9 Å / Relative weight: 1
ReflectionResolution: 2.2→49.12 Å / Num. obs: 258486 / % possible obs: 99.07 % / Redundancy: 3.5 % / CC1/2: 0.995 / CC star: 0.999 / Rmerge(I) obs: 0.07938 / Rpim(I) all: 0.05003 / Rrim(I) all: 0.09409 / Net I/σ(I): 10.09
Reflection shellResolution: 2.2→2.28 Å / Redundancy: 3.3 % / Rmerge(I) obs: 0.5185 / Mean I/σ(I) obs: 1.93 / Num. unique obs: 25340 / CC1/2: 0.778 / Rpim(I) all: 0.339 / Rrim(I) all: 0.6218 / % possible all: 97.5

-
Processing

Software
NameVersionClassification
REFMAC5.8.0405refinement
XDSdata reduction
XDSdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.2→49.12 Å / Cor.coef. Fo:Fc: 0.95 / Cor.coef. Fo:Fc free: 0.928 / SU B: 7.017 / SU ML: 0.172 / Cross valid method: THROUGHOUT / ESU R: 0.274 / ESU R Free: 0.208 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.23972 12925 5 %RANDOM
Rwork0.2007 ---
obs0.20266 245568 99.07 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso mean: 44.6 Å2
Baniso -1Baniso -2Baniso -3
1--2 Å20 Å2-0.44 Å2
2--1.06 Å20 Å2
3---1 Å2
Refinement stepCycle: 1 / Resolution: 2.2→49.12 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms35382 0 44 1239 36665
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0060.01236109
X-RAY DIFFRACTIONr_bond_other_d0.0010.01633582
X-RAY DIFFRACTIONr_angle_refined_deg1.2761.63748965
X-RAY DIFFRACTIONr_angle_other_deg0.4281.57177174
X-RAY DIFFRACTIONr_dihedral_angle_1_deg5.63554607
X-RAY DIFFRACTIONr_dihedral_angle_2_deg6.8825224
X-RAY DIFFRACTIONr_dihedral_angle_3_deg16.41105791
X-RAY DIFFRACTIONr_dihedral_angle_4_deg
X-RAY DIFFRACTIONr_chiral_restr0.0560.25503
X-RAY DIFFRACTIONr_gen_planes_refined0.0060.0242915
X-RAY DIFFRACTIONr_gen_planes_other0.0010.028269
X-RAY DIFFRACTIONr_nbd_refined
X-RAY DIFFRACTIONr_nbd_other
X-RAY DIFFRACTIONr_nbtor_refined
X-RAY DIFFRACTIONr_nbtor_other
X-RAY DIFFRACTIONr_xyhbond_nbd_refined
X-RAY DIFFRACTIONr_xyhbond_nbd_other
X-RAY DIFFRACTIONr_metal_ion_refined
X-RAY DIFFRACTIONr_metal_ion_other
X-RAY DIFFRACTIONr_symmetry_vdw_refined
X-RAY DIFFRACTIONr_symmetry_vdw_other
X-RAY DIFFRACTIONr_symmetry_hbond_refined
X-RAY DIFFRACTIONr_symmetry_hbond_other
X-RAY DIFFRACTIONr_symmetry_metal_ion_refined
X-RAY DIFFRACTIONr_symmetry_metal_ion_other
X-RAY DIFFRACTIONr_mcbond_it3.5534.48118476
X-RAY DIFFRACTIONr_mcbond_other3.5534.48118476
X-RAY DIFFRACTIONr_mcangle_it5.218.04723067
X-RAY DIFFRACTIONr_mcangle_other5.218.04723068
X-RAY DIFFRACTIONr_scbond_it3.8984.78417633
X-RAY DIFFRACTIONr_scbond_other3.8984.78417634
X-RAY DIFFRACTIONr_scangle_it
X-RAY DIFFRACTIONr_scangle_other6.0628.65725899
X-RAY DIFFRACTIONr_long_range_B_refined8.83854.04157961
X-RAY DIFFRACTIONr_long_range_B_other8.84254.02157283
X-RAY DIFFRACTIONr_rigid_bond_restr
X-RAY DIFFRACTIONr_sphericity_free
X-RAY DIFFRACTIONr_sphericity_bonded
LS refinement shellResolution: 2.201→2.258 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.327 928 -
Rwork0.305 17630 -
obs--96.8 %

+
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