[English] 日本語
Yorodumi
- PDB-8s2x: SSX structure of Arabidopsis thaliana Pdx1.3 grown in microfluidi... -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 8s2x
TitleSSX structure of Arabidopsis thaliana Pdx1.3 grown in microfluidic droplets
ComponentsPyridoxal 5'-phosphate synthase subunit PDX1.3
KeywordsLYASE / Vitamin B6
Function / homology
Function and homology information


response to non-ionic osmotic stress / response to lipid hydroperoxide / chlorophyll metabolic process / pyridoxal 5'-phosphate synthase (glutamine hydrolysing) / pyridoxal 5'-phosphate synthase (glutamine hydrolysing) activity / pyridoxal phosphate biosynthetic process / hyperosmotic salinity response / pyridoxine biosynthetic process / response to UV-B / amino acid metabolic process ...response to non-ionic osmotic stress / response to lipid hydroperoxide / chlorophyll metabolic process / pyridoxal 5'-phosphate synthase (glutamine hydrolysing) / pyridoxal 5'-phosphate synthase (glutamine hydrolysing) activity / pyridoxal phosphate biosynthetic process / hyperosmotic salinity response / pyridoxine biosynthetic process / response to UV-B / amino acid metabolic process / endomembrane system / response to salt stress / response to oxidative stress / protein heterodimerization activity / protein homodimerization activity / plasma membrane / cytosol
Similarity search - Function
Pyridoxal 5'-phosphate synthase subunit PdxS/SNZ / PdxS/SNZ N-terminal domain / SOR/SNZ family / PdxS/SNZ family signature. / PdxS/SNZ family profile. / Ribulose-phosphate binding barrel / Aldolase-type TIM barrel
Similarity search - Domain/homology
CITRIC ACID / PHOSPHATE ION / Pyridoxal 5'-phosphate synthase subunit PDX1.3
Similarity search - Component
Biological speciesArabidopsis thaliana (thale cress)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.5 Å
AuthorsStubbs, J. / Tews, I. / Maly, M.
Funding support United Kingdom, 2items
OrganizationGrant numberCountry
Biotechnology and Biological Sciences Research Council (BBSRC)BB/S008470/1 United Kingdom
Biotechnology and Biological Sciences Research Council (BBSRC)BB/T008768/1 United Kingdom
Citation
#1: Journal: BioRxiv / Year: 2024
Title: Droplet microfluidics for time-resolved serial crystallography
Authors: Stubbs, J. / Tews, I. / Maly, M.
History
DepositionFeb 19, 2024Deposition site: PDBE / Processing site: PDBE
Revision 1.0Feb 28, 2024Provider: repository / Type: Initial release
Revision 1.1Mar 20, 2024Group: Database references / Category: citation / citation_author

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: Pyridoxal 5'-phosphate synthase subunit PDX1.3
B: Pyridoxal 5'-phosphate synthase subunit PDX1.3
C: Pyridoxal 5'-phosphate synthase subunit PDX1.3
D: Pyridoxal 5'-phosphate synthase subunit PDX1.3
hetero molecules


Theoretical massNumber of molelcules
Total (without water)125,87712
Polymers124,7284
Non-polymers1,1488
Water3,351186
1
A: Pyridoxal 5'-phosphate synthase subunit PDX1.3
B: Pyridoxal 5'-phosphate synthase subunit PDX1.3
C: Pyridoxal 5'-phosphate synthase subunit PDX1.3
D: Pyridoxal 5'-phosphate synthase subunit PDX1.3
hetero molecules

A: Pyridoxal 5'-phosphate synthase subunit PDX1.3
B: Pyridoxal 5'-phosphate synthase subunit PDX1.3
C: Pyridoxal 5'-phosphate synthase subunit PDX1.3
D: Pyridoxal 5'-phosphate synthase subunit PDX1.3
hetero molecules

A: Pyridoxal 5'-phosphate synthase subunit PDX1.3
B: Pyridoxal 5'-phosphate synthase subunit PDX1.3
C: Pyridoxal 5'-phosphate synthase subunit PDX1.3
D: Pyridoxal 5'-phosphate synthase subunit PDX1.3
hetero molecules


Theoretical massNumber of molelcules
Total (without water)377,63036
Polymers374,18512
Non-polymers3,44524
Water21612
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation2_555-y,x-y,z1
crystal symmetry operation3_555-x+y,-x,z1
Buried area45560 Å2
ΔGint-227 kcal/mol
Surface area110500 Å2
MethodPISA
Unit cell
Length a, b, c (Å)180.3, 180.3, 119.2
Angle α, β, γ (deg.)90, 90, 120
Int Tables number146
Space group name H-MH3
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11A
21A
32A
42A
53A
63A
74A
84A
95A
105A
116A
126A

NCS domain segments:

Beg auth comp-ID: SER / Beg label comp-ID: SER / Auth asym-ID: A / Label asym-ID: A

Dom-IDComponent-IDEns-IDEnd auth comp-IDEnd label comp-IDAuth seq-IDLabel seq-ID
111GLYGLY22 - 28921 - 288
211GLYGLY22 - 28921 - 288
322LEULEU22 - 28821 - 287
422LEULEU22 - 28821 - 287
533GLUGLU22 - 29021 - 289
633GLUGLU22 - 29021 - 289
744LEULEU22 - 28821 - 287
844LEULEU22 - 28821 - 287
955GLYGLY22 - 28921 - 288
1055GLYGLY22 - 28921 - 288
1166LEULEU22 - 28821 - 287
1266LEULEU22 - 28821 - 287

NCS ensembles :
IDDetails
1Local NCS retraints between domains: 1 2
2Local NCS retraints between domains: 3 4
3Local NCS retraints between domains: 5 6
4Local NCS retraints between domains: 7 8
5Local NCS retraints between domains: 9 10
6Local NCS retraints between domains: 11 12

-
Components

#1: Protein
Pyridoxal 5'-phosphate synthase subunit PDX1.3 / AtPDX1.3 / AtPDX1 / 1 / PLP synthase subunit PDX1.3


Mass: 31182.057 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Arabidopsis thaliana (thale cress) / Gene: PDX13, GIP2, PDX1L3, RSR4, At5g01410, T10O8.120 / Production host: Escherichia coli (E. coli)
References: UniProt: Q8L940, pyridoxal 5'-phosphate synthase (glutamine hydrolysing)
#2: Chemical
ChemComp-CIT / CITRIC ACID / Citric acid


Mass: 192.124 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C6H8O7
#3: Chemical
ChemComp-PO4 / PHOSPHATE ION / Phosphate


Mass: 94.971 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: PO4
#4: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 186 / Source method: isolated from a natural source / Formula: H2O
Has ligand of interestN

-
Experimental details

-
Experiment

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

-
Sample preparation

CrystalDensity Matthews: 2.99 Å3/Da / Density % sol: 58.86 %
Crystal growTemperature: 294 K / Method: microfluidic / pH: 7 / Details: 600 mM Sodium citrate and 100 mM HEPES pH 7

-
Data collection

DiffractionMean temperature: 293 K / Serial crystal experiment: Y
Diffraction sourceSource: SYNCHROTRON / Site: ESRF / Beamline: ID29 / Wavelength: 1.07 Å
DetectorType: PSI JUNGFRAU 4M / Detector: PIXEL / Date: Jan 26, 2023
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.07 Å / Relative weight: 1
ReflectionResolution: 2.5→94.75 Å / Num. obs: 50011 / % possible obs: 100 % / Redundancy: 44.2 % / Biso Wilson estimate: 45.27 Å2 / CC1/2: 0.96 / CC star: 0.99 / Net I/σ(I): 5
Reflection shellResolution: 2.5→2.54 Å / Redundancy: 44.2 % / Mean I/σ(I) obs: 0.8 / Num. unique obs: 4635 / CC1/2: 0.27 / CC star: 0.65 / % possible all: 100
Serial crystallography sample deliveryDescription: SOS Chip / Method: fixed target
Serial crystallography data reductionCrystal hits: 20827 / Frames indexed: 20635 / Frames total: 245400

-
Processing

Software
NameVersionClassification
REFMAC5.8.0425refinement
CrystFEL0.10.2data reduction
CrystFEL0.10.2data scaling
MOLREPphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.5→65.396 Å / Cor.coef. Fo:Fc: 0.972 / Cor.coef. Fo:Fc free: 0.959 / WRfactor Rfree: 0.173 / WRfactor Rwork: 0.141 / SU B: 10.207 / SU ML: 0.197 / Average fsc free: 0.9601 / Average fsc work: 0.9676 / Cross valid method: FREE R-VALUE / ESU R: 0.312 / ESU R Free: 0.201
Details: Hydrogens have been added in their riding positions
RfactorNum. reflection% reflection
Rfree0.1883 2510 5.02 %
Rwork0.1584 47493 -
all0.16 --
obs-50003 99.984 %
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK BULK SOLVENT
Displacement parametersBiso mean: 59.187 Å2
Baniso -1Baniso -2Baniso -3
1-0.006 Å20.003 Å20 Å2
2--0.006 Å2-0 Å2
3----0.02 Å2
Refinement stepCycle: LAST / Resolution: 2.5→65.396 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms8088 0 72 186 8346
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0060.0128294
X-RAY DIFFRACTIONr_bond_other_d0.0010.0168155
X-RAY DIFFRACTIONr_angle_refined_deg1.5111.81511198
X-RAY DIFFRACTIONr_angle_other_deg0.5041.7618676
X-RAY DIFFRACTIONr_dihedral_angle_1_deg6.551080
X-RAY DIFFRACTIONr_dihedral_angle_2_deg9.081582
X-RAY DIFFRACTIONr_dihedral_angle_3_deg14.633101442
X-RAY DIFFRACTIONr_dihedral_angle_6_deg14.10410362
X-RAY DIFFRACTIONr_chiral_restr0.0720.21280
X-RAY DIFFRACTIONr_gen_planes_refined0.0050.0210004
X-RAY DIFFRACTIONr_gen_planes_other0.0010.021868
X-RAY DIFFRACTIONr_nbd_refined0.2060.21548
X-RAY DIFFRACTIONr_symmetry_nbd_other0.1950.27110
X-RAY DIFFRACTIONr_nbtor_refined0.1680.24080
X-RAY DIFFRACTIONr_symmetry_nbtor_other0.0790.24502
X-RAY DIFFRACTIONr_xyhbond_nbd_refined0.1350.2160
X-RAY DIFFRACTIONr_symmetry_nbd_refined0.140.28
X-RAY DIFFRACTIONr_nbd_other0.1620.264
X-RAY DIFFRACTIONr_symmetry_xyhbond_nbd_refined0.1070.27
X-RAY DIFFRACTIONr_mcbond_it4.9565.5854314
X-RAY DIFFRACTIONr_mcbond_other4.9565.5874315
X-RAY DIFFRACTIONr_mcangle_it7.52310.045390
X-RAY DIFFRACTIONr_mcangle_other7.52310.0425391
X-RAY DIFFRACTIONr_scbond_it6.1936.2213980
X-RAY DIFFRACTIONr_scbond_other6.1096.2073961
X-RAY DIFFRACTIONr_scangle_it9.72811.1715806
X-RAY DIFFRACTIONr_scangle_other9.70211.1495783
X-RAY DIFFRACTIONr_lrange_it11.96251.068662
X-RAY DIFFRACTIONr_lrange_other11.95151.0858637
X-RAY DIFFRACTIONr_ncsr_local_group_10.060.058047
X-RAY DIFFRACTIONr_ncsr_local_group_20.0630.058026
X-RAY DIFFRACTIONr_ncsr_local_group_30.0780.058021
X-RAY DIFFRACTIONr_ncsr_local_group_40.0590.058110
X-RAY DIFFRACTIONr_ncsr_local_group_50.070.058076
X-RAY DIFFRACTIONr_ncsr_local_group_60.0750.057982
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDRefine-IDTypeRms dev position (Å)Weight position
11AX-RAY DIFFRACTIONLocal ncs0.060140.0501
12AX-RAY DIFFRACTIONLocal ncs0.060140.0501
23AX-RAY DIFFRACTIONLocal ncs0.063360.0501
24AX-RAY DIFFRACTIONLocal ncs0.063360.0501
35AX-RAY DIFFRACTIONLocal ncs0.078350.0501
36AX-RAY DIFFRACTIONLocal ncs0.078350.0501
47AX-RAY DIFFRACTIONLocal ncs0.058790.0501
48AX-RAY DIFFRACTIONLocal ncs0.058790.0501
59AX-RAY DIFFRACTIONLocal ncs0.070240.0501
510AX-RAY DIFFRACTIONLocal ncs0.070240.0501
611AX-RAY DIFFRACTIONLocal ncs0.075290.0501
612AX-RAY DIFFRACTIONLocal ncs0.075290.0501
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Total num. of bins used: 20

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRfactor allNum. reflection allFsc freeFsc work% reflection obs (%)WRfactor Rwork
2.5-2.5650.3522090.34835190.34837300.9050.90599.94640.341
2.565-2.6350.3111570.31734380.31735960.9320.92999.97220.306
2.635-2.7110.3471360.29533590.29734970.9110.93899.94280.279
2.711-2.7950.2491620.25732530.25634150.9590.9571000.234
2.795-2.8860.2711390.25231160.25332550.9490.9581000.229
2.886-2.9870.2741460.23630700.23732160.9460.9641000.211
2.987-3.10.2491840.22328840.22530680.9590.9691000.198
3.1-3.2260.2581880.1927830.19429720.9570.97799.96640.167
3.226-3.3690.2341400.17227010.17528410.9630.9811000.151
3.369-3.5330.1751430.14525650.14627080.9810.9871000.129
3.533-3.7240.1581150.12724880.12826030.9850.991000.114
3.724-3.9490.1721360.11422790.11624150.9820.9921000.103
3.949-4.220.117990.09922090.123080.9910.9941000.093
4.22-4.5570.123900.08620270.08821170.9910.9951000.083
4.557-4.9890.12780.08918970.0919750.9920.9951000.086
4.989-5.5740.1381100.11416800.11617900.9880.9931000.11
5.574-6.4290.154780.1314850.13215630.9850.991000.126
6.429-7.8540.1561040.12412170.12713210.9850.9911000.127
7.854-11.0280.142620.129790.12210410.9890.9921000.133
11.028-65.3960.204340.1995440.25780.9650.981000.229

+
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