[English] 日本語
Yorodumi
- PDB-7qs0: Crystal structure of B30.2 PRYSPRY domain of TRIM10 -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 7qs0
TitleCrystal structure of B30.2 PRYSPRY domain of TRIM10
ComponentsTripartite motif-containing protein 10
KeywordsLIGASE / E3 / TRIM / TRIM10 / B30.2 domain / SPRY domain / PRYSPRY domain
Function / homology
Function and homology information


host-mediated suppression of symbiont invasion / erythrocyte differentiation / Interferon gamma signaling / ubiquitin protein ligase activity / protein ubiquitination / innate immune response / zinc ion binding / cytoplasm
Similarity search - Function
TRIM10, RING-HC finger / SPRY domain / : / SPRY-associated domain / SPRY-associated / PRY / Butyrophylin-like, SPRY domain / B-box zinc finger / B-Box-type zinc finger / B-box-type zinc finger ...TRIM10, RING-HC finger / SPRY domain / : / SPRY-associated domain / SPRY-associated / PRY / Butyrophylin-like, SPRY domain / B-box zinc finger / B-Box-type zinc finger / B-box-type zinc finger / Zinc finger B-box type profile. / Zinc finger, C3HC4 RING-type / Zinc finger, C3HC4 type (RING finger) / SPRY domain / B30.2/SPRY domain / B30.2/SPRY domain profile. / B30.2/SPRY domain superfamily / Domain in SPla and the RYanodine Receptor. / SPRY domain / Zinc finger, RING-type, conserved site / Zinc finger RING-type signature. / Ring finger / Zinc finger RING-type profile. / Zinc finger, RING-type / Concanavalin A-like lectin/glucanase domain superfamily / Zinc finger, RING/FYVE/PHD-type / Jelly Rolls / Sandwich / Mainly Beta
Similarity search - Domain/homology
Tripartite motif-containing protein 10
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.3 Å
AuthorsChaikuad, A. / Knapp, S. / Structural Genomics Consortium (SGC)
Funding support1items
OrganizationGrant numberCountry
Not funded
CitationJournal: To Be Published
Title: Crystal structure of B30.2 PRYSPRY domain of TRIM10
Authors: Chaikuad, A. / Knapp, S. / Structural Genomics Consortium (SGC)
History
DepositionJan 12, 2022Deposition site: PDBE / Processing site: PDBE
Revision 1.0May 4, 2022Provider: repository / Type: Initial release
Revision 1.1Jan 31, 2024Group: Data collection / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / pdbx_initial_refinement_model / struct_ncs_dom_lim
Item: _struct_ncs_dom_lim.beg_auth_comp_id / _struct_ncs_dom_lim.beg_label_asym_id ..._struct_ncs_dom_lim.beg_auth_comp_id / _struct_ncs_dom_lim.beg_label_asym_id / _struct_ncs_dom_lim.beg_label_comp_id / _struct_ncs_dom_lim.beg_label_seq_id / _struct_ncs_dom_lim.end_auth_comp_id / _struct_ncs_dom_lim.end_label_asym_id / _struct_ncs_dom_lim.end_label_comp_id / _struct_ncs_dom_lim.end_label_seq_id

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: Tripartite motif-containing protein 10
B: Tripartite motif-containing protein 10
C: Tripartite motif-containing protein 10
hetero molecules


Theoretical massNumber of molelcules
Total (without water)60,4277
Polymers60,1793
Non-polymers2484
Water1,36976
1
A: Tripartite motif-containing protein 10
hetero molecules


Theoretical massNumber of molelcules
Total (without water)20,2464
Polymers20,0601
Non-polymers1863
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
B: Tripartite motif-containing protein 10
hetero molecules


Theoretical massNumber of molelcules
Total (without water)20,1222
Polymers20,0601
Non-polymers621
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
3
C: Tripartite motif-containing protein 10


Theoretical massNumber of molelcules
Total (without water)20,0601
Polymers20,0601
Non-polymers00
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)65.991, 65.991, 103.312
Angle α, β, γ (deg.)90.000, 90.000, 120.000
Int Tables number145
Space group name H-MP32
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11A
21B
12A
22C
13B
23C

NCS domain segments:

Component-ID: _ / Beg auth comp-ID: ASP / Beg label comp-ID: ASP / End auth comp-ID: SER / End label comp-ID: SER / Refine code: _

Dom-IDEns-IDAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
11AA306 - 4803 - 177
21BB306 - 4803 - 177
12AA306 - 4803 - 177
22CC306 - 4803 - 177
13BB306 - 4813 - 178
23CC306 - 4813 - 178

NCS ensembles :
ID
1
2
3

-
Components

#1: Protein Tripartite motif-containing protein 10 / B30-RING finger protein / RING finger protein 9


Mass: 20059.520 Da / Num. of mol.: 3
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: TRIM10, RFB30, RNF9 / Production host: Escherichia coli BL21(DE3) (bacteria) / Variant (production host): -R3-pRARE2 / References: UniProt: Q9UDY6
#2: Chemical
ChemComp-EDO / 1,2-ETHANEDIOL / ETHYLENE GLYCOL


Mass: 62.068 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C2H6O2
#3: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 76 / 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: 2.16 Å3/Da / Density % sol: 43.01 %
Crystal growTemperature: 293.15 K / Method: vapor diffusion, sitting drop / pH: 7.5 / Details: 25% ethylene glycol

-
Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: SLS / Beamline: X06SA / Wavelength: 1.00002 Å
DetectorType: DECTRIS EIGER2 X 16M / Detector: PIXEL / Date: Jul 4, 2021
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.00002 Å / Relative weight: 1
ReflectionResolution: 2.3→38.32 Å / Num. obs: 22199 / % possible obs: 99.2 % / Redundancy: 8.7 % / CC1/2: 0.997 / Rmerge(I) obs: 0.09 / Rpim(I) all: 0.034 / Rrim(I) all: 0.101 / Net I/σ(I): 3.4
Reflection shell

Diffraction-ID: 1

Resolution (Å)Redundancy (%)Rmerge(I) obsMean I/σ(I) obsNum. unique obsCC1/2Rpim(I) allRrim(I) all% possible all
2.3-2.3890.3511.821740.9860.1330.401100
8.91-38.329.20.0623850.9970.0220.06697.6

-
Processing

Software
NameVersionClassification
Aimless0.7.7data scaling
REFMAC5.8.0267refinement
PDB_EXTRACT3.27data extraction
XDSdata reduction
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 6umb
Resolution: 2.3→38.32 Å / Cor.coef. Fo:Fc: 0.946 / Cor.coef. Fo:Fc free: 0.915 / SU B: 20.474 / SU ML: 0.236 / SU R Cruickshank DPI: 0.5129 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.513 / ESU R Free: 0.272 / Stereochemistry target values: MAXIMUM LIKELIHOOD
Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS U VALUES : WITH TLS ADDED
RfactorNum. reflection% reflectionSelection details
Rfree0.256 1155 5.2 %RANDOM
Rwork0.2038 ---
obs0.2065 21014 99.23 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso max: 124.72 Å2 / Biso mean: 50.251 Å2 / Biso min: 25.54 Å2
Baniso -1Baniso -2Baniso -3
1-1.31 Å20.65 Å20 Å2
2--1.31 Å20 Å2
3----4.25 Å2
Refinement stepCycle: final / Resolution: 2.3→38.32 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms4214 0 16 76 4306
Biso mean--58.02 48.22 -
Num. residues----529
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0110.0134359
X-RAY DIFFRACTIONr_bond_other_d0.0010.0173998
X-RAY DIFFRACTIONr_angle_refined_deg1.2951.6475931
X-RAY DIFFRACTIONr_angle_other_deg1.1481.5759173
X-RAY DIFFRACTIONr_dihedral_angle_1_deg8.7885529
X-RAY DIFFRACTIONr_dihedral_angle_2_deg28.27820.04247
X-RAY DIFFRACTIONr_dihedral_angle_3_deg13.76915669
X-RAY DIFFRACTIONr_dihedral_angle_4_deg22.3581542
X-RAY DIFFRACTIONr_chiral_restr0.0550.2546
X-RAY DIFFRACTIONr_gen_planes_refined0.0090.024955
X-RAY DIFFRACTIONr_gen_planes_other0.0010.021117
Refine LS restraints NCS

Refine-ID: X-RAY DIFFRACTION / Type: interatomic distance / Weight position: 0.05

Ens-IDDom-IDAuth asym-IDNumberRms dev position (Å)
11A53260.09
12B53260.09
21A51600.11
22C51600.11
31B51730.12
32C51730.12
LS refinement shellResolution: 2.3→2.36 Å / Rfactor Rfree error: 0 / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.282 76 -
Rwork0.237 1581 -
all-1657 -
obs--99.88 %
Refinement TLS params.

Method: refined / Refine-ID: X-RAY DIFFRACTION

IDL112)L122)L132)L222)L232)L332)S11 (Å °)S12 (Å °)S13 (Å °)S21 (Å °)S22 (Å °)S23 (Å °)S31 (Å °)S32 (Å °)S33 (Å °)T112)T122)T132)T222)T232)T332)Origin x (Å)Origin y (Å)Origin z (Å)
12.90650.3402-0.57832.4412-1.54575.7898-0.01770.2286-0.139-0.2787-0.0524-0.22210.46470.50030.07010.07060.0347-0.00430.0741-0.00140.103748.2903-24.9849-4.401
21.73680.1735-1.47572.3079-0.75424.27840.01070.09790.04820.00680.06690.12440.0017-0.1219-0.07760.00130.0025-0.00060.0202-0.00130.011437.4226-19.77212.5741
33.2025-0.0702-1.59692.96520.42285.1069-0.2803-0.2881-0.13970.24660.15010.10950.46570.16470.13020.14740.02030.02120.05560.02810.032356.794-42.03428.4604
41.8995-0.9976-0.87562.45330.70594.857-0.11740.00870.1793-0.00820.1695-0.13020.00850.3124-0.05210.066-0.0564-0.01160.09230.01890.03661.6847-35.133520.0604
54.17020.5239-0.64213.7503-1.28640.5402-0.21840.5932-0.1083-0.44650.18940.12180.1817-0.24290.02910.4371-0.02920.03470.4297-0.02250.309552.3015-9.431825.13
62.8073-1.1227-0.80133.57250.42443.8679-0.0758-0.29770.1357-0.10330.1075-0.1152-0.0797-0.1573-0.03170.4329-0.06940.00660.1988-0.03350.114161.4503-1.986924.6819
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A305 - 344
2X-RAY DIFFRACTION2A345 - 481
3X-RAY DIFFRACTION3B306 - 409
4X-RAY DIFFRACTION4B410 - 481
5X-RAY DIFFRACTION5C306 - 331
6X-RAY DIFFRACTION6C332 - 481

+
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