[English] 日本語
Yorodumi
- PDB-8qex: Streptavidin variant with a cobalt catalyst for CH metal-catalyze... -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 8qex
TitleStreptavidin variant with a cobalt catalyst for CH metal-catalyzed hydrogen-atom-transfer (M-HAT)
ComponentsStreptavidin
KeywordsMETAL BINDING PROTEIN / metal-catalyzed hydrogen-atom-transfer / artificial radical cyclase / protein design
Function / homology
Function and homology information


biotin binding / extracellular region
Similarity search - Function
Avidin-like, conserved site / Avidin-like domain signature. / Avidin / : / Avidin/streptavidin / Avidin-like superfamily / Avidin family / Avidin-like domain profile.
Similarity search - Domain/homology
Biological speciesStreptomyces avidinii (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.9 Å
AuthorsJakob, R.P. / Chen, D. / Ward, T.R.
Funding support1items
OrganizationGrant numberCountry
Not funded
CitationJournal: Nat.Chem. / Year: 2024
Title: An evolved artificial radical cyclase enables the construction of bicyclic terpenoid scaffolds via an H-atom transfer pathway.
Authors: Chen, D. / Zhang, X. / Vorobieva, A.A. / Tachibana, R. / Stein, A. / Jakob, R.P. / Zou, Z. / Graf, D.A. / Li, A. / Maier, T. / Correia, B.E. / Ward, T.R.
History
DepositionSep 1, 2023Deposition site: PDBE / Processing site: PDBE
Revision 1.0Jul 31, 2024Provider: repository / Type: Initial release
Revision 1.1Oct 16, 2024Group: Database references / Structure summary / Category: citation / citation_author / pdbx_entry_details
Item: _citation.journal_volume / _citation.page_first ..._citation.journal_volume / _citation.page_first / _citation.page_last / _citation_author.identifier_ORCID / _pdbx_entry_details.has_protein_modification

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: Streptavidin
B: Streptavidin
hetero molecules


Theoretical massNumber of molelcules
Total (without water)36,4884
Polymers34,8922
Non-polymers1,5962
Water2,936163
1
A: Streptavidin
B: Streptavidin
hetero molecules

A: Streptavidin
B: Streptavidin
hetero molecules


Theoretical massNumber of molelcules
Total (without water)72,9758
Polymers69,7844
Non-polymers3,1914
Water724
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation2_656-x+1,y,-z+11
Buried area10120 Å2
ΔGint-56 kcal/mol
Surface area19980 Å2
MethodPISA
Unit cell
Length a, b, c (Å)48.456, 80.534, 78.766
Angle α, β, γ (deg.)90.00, 103.92, 90.00
Int Tables number5
Space group name H-MI121
Components on special symmetry positions
IDModelComponents
11A-319-

HOH

21A-346-

HOH

31B-349-

HOH

41B-356-

HOH

-
Components

#1: Protein Streptavidin


Mass: 17445.941 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Streptomyces avidinii (bacteria) / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: P22629
#2: Chemical ChemComp-UFU / cobalt Streptavidin


Mass: 797.871 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C41H50CoN6O5S / Feature type: SUBJECT OF INVESTIGATION
#3: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 163 / 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: 2.14 Å3/Da / Density % sol: 42.46 %
Crystal growTemperature: 293 K / Method: vapor diffusion
Details: 0.05 M Citric acid, 19 % w/v PEG 1000, 0.1 M Lithium sulfate, 0.05 M Sodium phosphate dibasic dihydrate

-
Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: SLS / Beamline: X06SA / Wavelength: 1 Å
DetectorType: DECTRIS EIGER X 16M / Detector: PIXEL / Date: Mar 31, 2023
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 1.9→45.25 Å / Num. obs: 22733 / % possible obs: 98.2 % / Redundancy: 7.1 % / CC1/2: 0.997 / Rpim(I) all: 0.079 / Rrim(I) all: 0.155 / Net I/σ(I): 8.7
Reflection shellResolution: 1.9→1.97 Å / Mean I/σ(I) obs: 2 / Num. unique obs: 2267 / CC1/2: 0.816 / Rpim(I) all: 0.59 / Rrim(I) all: 1.15 / % possible all: 97

-
Processing

Software
NameVersionClassification
REFMAC5.8.0267refinement
XDSdata reduction
XSCALEdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 1.9→45.25 Å / Cor.coef. Fo:Fc: 0.927 / Cor.coef. Fo:Fc free: 0.917 / SU B: 3.978 / SU ML: 0.116 / Cross valid method: FREE R-VALUE / ESU R: 0.179 / ESU R Free: 0.155 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.25416 1163 5.1 %RANDOM
Rwork0.22883 ---
obs0.23014 21597 98.06 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso mean: 25.607 Å2
Baniso -1Baniso -2Baniso -3
1--0.03 Å2-0 Å2-0.14 Å2
2--0.15 Å20 Å2
3----0.04 Å2
Refinement stepCycle: 1 / Resolution: 1.9→45.25 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms1843 0 108 168 2119
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.010.0122011
X-RAY DIFFRACTIONr_bond_other_d0.0010.0141778
X-RAY DIFFRACTIONr_angle_refined_deg1.5911.5962767
X-RAY DIFFRACTIONr_angle_other_deg1.4191.554045
X-RAY DIFFRACTIONr_dihedral_angle_1_deg7.065242
X-RAY DIFFRACTIONr_dihedral_angle_2_deg21.1822.04588
X-RAY DIFFRACTIONr_dihedral_angle_3_deg11.3915255
X-RAY DIFFRACTIONr_dihedral_angle_4_deg16.145159
X-RAY DIFFRACTIONr_chiral_restr0.070.2263
X-RAY DIFFRACTIONr_gen_planes_refined0.0080.022243
X-RAY DIFFRACTIONr_gen_planes_other0.0010.02489
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_it2.5332.495980
X-RAY DIFFRACTIONr_mcbond_other2.5312.493979
X-RAY DIFFRACTIONr_mcangle_it3.7813.7121218
X-RAY DIFFRACTIONr_mcangle_other3.7793.7161219
X-RAY DIFFRACTIONr_scbond_it2.7782.8071030
X-RAY DIFFRACTIONr_scbond_other2.7772.8081031
X-RAY DIFFRACTIONr_scangle_it
X-RAY DIFFRACTIONr_scangle_other4.1634.091549
X-RAY DIFFRACTIONr_long_range_B_refined6.65529.7632230
X-RAY DIFFRACTIONr_long_range_B_other6.65729.4912206
X-RAY DIFFRACTIONr_rigid_bond_restr
X-RAY DIFFRACTIONr_sphericity_free
X-RAY DIFFRACTIONr_sphericity_bonded
Refine LS restraints NCS

Ens-ID: 1 / Number: 3674 / Refine-ID: X-RAY DIFFRACTION / Type: interatomic distance / Rms dev position: 0.09 Å / Weight position: 0.05

Dom-IDAuth asym-ID
1A
2B
LS refinement shellResolution: 1.9→1.949 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.295 83 -
Rwork0.292 1573 -
obs--96.67 %

+
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