[English] 日本語
Yorodumi
- PDB-7x4w: Crystal structure of Keap1 BTB domain in complex with dimethyl fu... -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 7x4w
TitleCrystal structure of Keap1 BTB domain in complex with dimethyl fumarate (DMF)
ComponentsKelch-like ECH-associated protein 1
KeywordsSIGNALING PROTEIN / KEAP1 / BTB domain
Function / homology
Function and homology information


regulation of epidermal cell differentiation / Nuclear events mediated by NFE2L2 / Cul3-RING ubiquitin ligase complex / ubiquitin-like ligase-substrate adaptor activity / centriolar satellite / inclusion body / cellular response to interleukin-4 / regulation of autophagy / actin filament / negative regulation of DNA-binding transcription factor activity ...regulation of epidermal cell differentiation / Nuclear events mediated by NFE2L2 / Cul3-RING ubiquitin ligase complex / ubiquitin-like ligase-substrate adaptor activity / centriolar satellite / inclusion body / cellular response to interleukin-4 / regulation of autophagy / actin filament / negative regulation of DNA-binding transcription factor activity / KEAP1-NFE2L2 pathway / disordered domain specific binding / positive regulation of proteasomal ubiquitin-dependent protein catabolic process / Antigen processing: Ubiquitination & Proteasome degradation / cellular response to oxidative stress / Neddylation / midbody / ubiquitin-dependent protein catabolic process / in utero embryonic development / RNA polymerase II-specific DNA-binding transcription factor binding / Potential therapeutics for SARS / protein ubiquitination / Ub-specific processing proteases / endoplasmic reticulum / nucleoplasm / identical protein binding / cytosol / cytoplasm
Similarity search - Function
Kelch-like ECH-associated protein 1 / : / BTB-kelch protein / BTB/Kelch-associated / BTB And C-terminal Kelch / BTB And C-terminal Kelch / Kelch / Kelch repeat type 1 / Kelch motif / Kelch-type beta propeller ...Kelch-like ECH-associated protein 1 / : / BTB-kelch protein / BTB/Kelch-associated / BTB And C-terminal Kelch / BTB And C-terminal Kelch / Kelch / Kelch repeat type 1 / Kelch motif / Kelch-type beta propeller / BTB/POZ domain / BTB domain profile. / Broad-Complex, Tramtrack and Bric a brac / BTB/POZ domain / SKP1/BTB/POZ domain superfamily
Similarity search - Domain/homology
Dimethyl fumarate / Kelch-like ECH-associated protein 1
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 3.209 Å
AuthorsQu, L.Z.
Funding support China, 1items
OrganizationGrant numberCountry
National Natural Science Foundation of China (NSFC) China
CitationJournal: Biochem.Biophys.Res.Commun. / Year: 2022
Title: Characterization of the modification of Kelch-like ECH-associated protein 1 by different fumarates.
Authors: Qu, L. / Guo, M. / Zhang, H. / Chen, X. / Wei, H. / Jiang, L. / Li, J. / Chen, Z. / Dai, S. / Chen, Y.
History
DepositionMar 3, 2022Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0Mar 8, 2023Provider: repository / Type: Initial release
Revision 1.1Sep 20, 2023Group: Data collection / Database references
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / citation / citation_author
Item: _citation.country / _citation.journal_abbrev ..._citation.country / _citation.journal_abbrev / _citation.journal_id_ASTM / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.journal_volume / _citation.page_first / _citation.page_last / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation.year
Revision 1.2Nov 29, 2023Group: Refinement description / Category: pdbx_initial_refinement_model

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: Kelch-like ECH-associated protein 1
C: Kelch-like ECH-associated protein 1
D: Kelch-like ECH-associated protein 1
E: Kelch-like ECH-associated protein 1
F: Kelch-like ECH-associated protein 1
B: Kelch-like ECH-associated protein 1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)93,4979
Polymers93,0596
Non-polymers4383
Water0
1
A: Kelch-like ECH-associated protein 1
D: Kelch-like ECH-associated protein 1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)31,3124
Polymers31,0202
Non-polymers2922
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area3900 Å2
ΔGint-35 kcal/mol
Surface area12210 Å2
MethodPISA
2
C: Kelch-like ECH-associated protein 1
B: Kelch-like ECH-associated protein 1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)31,1663
Polymers31,0202
Non-polymers1461
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area3640 Å2
ΔGint-35 kcal/mol
Surface area12610 Å2
MethodPISA
3
E: Kelch-like ECH-associated protein 1

F: Kelch-like ECH-associated protein 1


Theoretical massNumber of molelcules
Total (without water)31,0202
Polymers31,0202
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation4_575x+1/2,-y+5/2,-z1
Buried area3660 Å2
ΔGint-37 kcal/mol
Surface area11780 Å2
MethodPISA
Unit cell
Length a, b, c (Å)84.538, 99.105, 143.136
Angle α, β, γ (deg.)90.000, 90.000, 90.000
Int Tables number19
Space group name H-MP212121

-
Components

#1: Protein
Kelch-like ECH-associated protein 1 / Cytosolic inhibitor of Nrf2 / INrf2 / Kelch-like protein 19


Mass: 15509.844 Da / Num. of mol.: 6
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: KEAP1, INRF2, KIAA0132, KLHL19 / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: Q14145
#2: Chemical ChemComp-9HB / Dimethyl fumarate / Dimethyl fumarate


Mass: 146.141 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: C6H10O4 / Feature type: SUBJECT OF INVESTIGATION
Has ligand of interestY

-
Experimental details

-
Experiment

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

-
Sample preparation

CrystalDensity Matthews: 3.22 Å3/Da / Density % sol: 61.82 %
Crystal growTemperature: 293 K / Method: vapor diffusion, hanging drop / pH: 8 / Details: 0.2 M lithium acetate, 20% PEG 3350

-
Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: ROTATING ANODE / Type: RIGAKU / Wavelength: 1.58 Å
DetectorType: RIGAKU RAXIS IV++ / Detector: IMAGE PLATE / Date: Dec 25, 2020
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.58 Å / Relative weight: 1
ReflectionResolution: 3.2→46.826 Å / Num. obs: 19199 / % possible obs: 94.6 % / Redundancy: 8.4 % / CC1/2: 1 / Net I/σ(I): 6.8
Reflection shellResolution: 3.2→3.3 Å / Num. unique obs: 1811 / CC1/2: 0.5

-
Processing

Software
NameVersionClassification
PHENIX1.10.1_2155refinement
PDB_EXTRACT3.27data extraction
HKL-2000data reduction
HKL-2000data scaling
PHENIXphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 4CXI
Resolution: 3.209→46.826 Å / SU ML: 0.53 / Cross valid method: THROUGHOUT / σ(F): 1.33 / Phase error: 32.61 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2979 1921 10.01 %
Rwork0.2375 17278 -
obs0.2437 19199 94.67 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso max: 137.22 Å2 / Biso mean: 63.4388 Å2 / Biso min: 20.74 Å2
Refinement stepCycle: final / Resolution: 3.209→46.826 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms5639 0 30 0 5669
Biso mean--91.25 --
Num. residues----750
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0025766
X-RAY DIFFRACTIONf_angle_d0.4177796
X-RAY DIFFRACTIONf_chiral_restr0.04928
X-RAY DIFFRACTIONf_plane_restr0.003987
X-RAY DIFFRACTIONf_dihedral_angle_d13.8513441
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Rfactor Rfree error: 0

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection Rwork% reflection obs (%)
3.2094-3.28970.41491250.3349112489
3.2897-3.37860.37391340.3074120794
3.3786-3.4780.40551320.3477121295
3.478-3.59020.36351340.2959120593
3.5902-3.71850.37971320.3007118692
3.7185-3.86730.36531350.297121093
3.8673-4.04320.371320.2768117992
4.0432-4.25620.27851330.2103119492
4.2562-4.52270.28641330.2035120193
4.5227-4.87160.25091370.1828122795
4.8716-5.36120.211430.2017128998
5.3612-6.13550.31281470.23211321100
6.1355-7.72440.27021480.23781340100
7.7244-46.8260.23621560.1849138398
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)
10.26310.09670.5575-0.06060.12080.9784-0.04350.1126-0.1925-0.03830.0791-0.12720.0595-0.0078-0.00060.24390.006-0.01660.24310.03710.315179.634109.75650.104
20.98010.3730.56240.14470.16140.87110.37950.0317-0.1731-0.02810.3018-0.1483-0.54410.14360.58280.90390.37390.18070.76780.16520.074890.94117.60741.311
30.1061-0.21830.03680.2837-0.03770.07580.1310.11630.0526-0.1370.05610.1128-0.1847-0.20440.03930.30840.01170.10190.28850.03940.173582.079117.54557.214
40.05470.18550.0770.43890.03411.7833-0.03730.1664-0.0946-0.00370.31860.0646-0.86120.48710.16450.2975-0.0036-0.04820.19440.01950.325170.8122.54360.283
51.0284-0.2838-0.77040.53280.44830.79860.09170.05880.0036-0.0557-0.23280.3168-0.0877-0.1445-0.14850.36960.0609-0.04140.23240.01090.355479.082115.46218.594
60.6268-0.31190.2440.1927-0.07960.04840.36140.28420.1944-0.0288-0.2612-0.08780.10950.31460.02980.3748-0.06670.02930.2866-0.04360.282499.487120.93314.784
70.3613-0.28010.09980.2717-0.21610.2651-0.02860.08420.3504-0.2643-0.04560.061-0.10330.2095-0.0587-0.10440.909-0.8946-0.11130.8436-0.563899.749126.1123.791
81.0102-0.29840.85230.0835-0.26630.73460.09560.39940.1418-0.2036-0.133-0.5504-0.06610.5218-0.03530.4077-0.0475-0.02570.18210.0460.6511106.683123.75416.289
90.00940.005-0.01620.0966-0.22390.4532-0.3716-0.37480.0817-0.25440.6804-0.13180.0124-0.86930.02880.3208-0.02010.00010.3995-0.06070.45397.914118.23324.207
100.24190.15590.25310.11190.21050.421-0.0272-0.4770.44020.01470.1532-0.1071-0.08870.09690.25660.36070.03420.27210.6327-0.43020.402698.606118.89834.251
110.41640.1360.36740.15160.10090.30550.22770.1822-0.4918-0.11880.1294-0.17680.17310.1540.25120.63390.21810.1775-0.5696-0.0710.4448100.981128.24928.3
120.0308-0.0049-0.0246-0.0110.01340.01170.01960.3012-0.2972-0.1712-0.02320.01280.2113-0.0888-0.00030.39660.02490.01060.25210.07690.444194.93128.66636.102
130.39810.2221-0.07620.1839-0.03690.16730.07280.0794-0.26850.00510.0750.0522-0.3207-0.17190.00620.29320.1066-0.06260.29580.01470.236981.951122.90410.468
140.8118-0.44510.08380.553-0.26260.2273-0.0971-0.7117-0.2722-0.12510.23690.256-0.1960.43980.01930.3746-0.0305-0.05390.4419-0.02480.256879.034115.9034.493
150.0873-0.1034-0.12430.04880.02140.0018-0.26450.42450.43880.2365-0.1058-0.2065-0.1991-0.2956-0.00030.3969-0.1122-0.07190.6023-0.03460.436964.01113.39210.905
160.6740.31630.34850.496-0.30460.64960.0605-0.1173-0.086-0.04840.03160.0051-0.00560.119700.3193-0.00850.03960.2356-0.01490.356279.19103.63939.074
170.04230.21970.12240.0875-0.0180.06190.27370.14550.0189-0.2063-0.07110.06070.1072-0.07150.00120.4226-0.0235-0.0430.2822-0.02340.297168.74391.81334.301
180.0531-0.0013-0.04970.149-0.058-0.01810.13930.06070.45090.15050.214-0.583-0.31850.47240.00010.5779-0.02310.13270.8973-0.07130.7754124.27799.14211.091
190.041-0.0108-0.15130.00010.14340.2840.32510.52721.10170.2011-0.2194-0.53220.38170.9707-0.00760.4326-0.2373-0.09120.7390.26380.748102.592101.7451.397
20-0.01510.0090.0043-0.0022-0.01620.02920.27180.2314-0.23270.3744-0.28140.06430.179-0.6585-0.00060.4259-0.15010.05260.7836-0.03320.6107111.31492.571-2.892
210.0316-0.04130.04070.0359-0.04130.03410.10070.11720.09610.0310.10120.25940.01920.13220.00020.7143-0.3498-0.12681.00950.23610.581298.8394.927-2.035
220.2373-0.1842-0.16160.23370.32950.5718-0.29710.09190.44450.75740.43970.0103-0.11920.52130.02290.464-0.11590.02450.44460.12570.6395105.30996.0169.6
230.6267-0.68650.05171.2033-0.14650.01880.27980.3909-0.7495-0.4951-0.15820.6879-0.0575-0.38280.2610.4051-0.13460.20790.62540.080.6999100.29988.59813.658
240.03870.07450.02610.04870.06310.03120.34020.27880.20450.1580.3124-0.44060.617-0.00950.00310.4632-0.0201-0.06880.403-0.00120.4477104.74283.28714.373
250.03730.0335-0.02410.53620.29680.1457-0.2106-0.75230.4243-0.4415-0.1024-0.2466-0.46890.22060.00830.5034-0.0444-0.07960.8447-0.04280.593375.122157.61-9.422
260.0235-0.0305-0.00470.0230.00050.05740.21720.2297-0.1270.0859-0.5561-0.0731-0.0599-0.3061-0.00040.49970.0674-0.00640.8390.10730.755883.15149.1459.059
270.0058-0.0013-0.01040.0534-0.03630.0061-0.05840.0383-0.0153-0.03880.0670.2272-0.0819-0.348-00.52780.04140.04070.884-0.11580.455791.447147.5689.447
280.05680.0655-0.05960.01740.00760.0092-0.22660.6129-0.35820.0807-0.23470.3226-0.21240.2652-0.00070.66680.1183-0.0590.8701-0.01540.622484.577140.7793.203
290.0187-0.0340.00320.0188-0.0021-0.00330.03520.1459-0.1857-0.16630.2947-0.6663-0.33670.3550.00020.5390.1850.18380.78010.06010.485891.716150.767-0.388
300.0788-0.05940.00970.0214-0.0079-0-0.3856-0.6320.13430.04420.32980.63250.08610.0759-0.00010.43020.2018-0.0190.7504-0.19010.551697.727145.549-4.716
310.52730.25010.37170.23160.38530.7658-0.14380.20420.527-0.2147-0.8842-0.4118-0.15420.2352-0.04720.6350.2261-0.02440.46090.11550.790399.726145.085-13.203
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1( CHAIN A AND RESID 51:111 )A51 - 111
2X-RAY DIFFRACTION2( CHAIN A AND RESID 112:120 )A112 - 120
3X-RAY DIFFRACTION3( CHAIN A AND RESID 121:142 )A121 - 142
4X-RAY DIFFRACTION4( CHAIN A AND RESID 143:176 )A143 - 176
5X-RAY DIFFRACTION5( CHAIN B AND RESID 51:72 )B51 - 72
6X-RAY DIFFRACTION6( CHAIN B AND RESID 73:112 )B73 - 112
7X-RAY DIFFRACTION7( CHAIN B AND RESID 113:120 )B113 - 120
8X-RAY DIFFRACTION8( CHAIN B AND RESID 121:129 )B121 - 129
9X-RAY DIFFRACTION9( CHAIN B AND RESID 130:142 )B130 - 142
10X-RAY DIFFRACTION10( CHAIN B AND RESID 143:151 )B143 - 151
11X-RAY DIFFRACTION11( CHAIN B AND RESID 152:164 )B152 - 164
12X-RAY DIFFRACTION12( CHAIN B AND RESID 165:176 )B165 - 176
13X-RAY DIFFRACTION13( CHAIN C AND RESID 50:95 )C50 - 95
14X-RAY DIFFRACTION14( CHAIN C AND RESID 96:142 )C96 - 142
15X-RAY DIFFRACTION15( CHAIN C AND RESID 143:179 )C143 - 179
16X-RAY DIFFRACTION16( CHAIN D AND RESID 50:129 )D50 - 129
17X-RAY DIFFRACTION17( CHAIN D AND RESID 130:179 )D130 - 179
18X-RAY DIFFRACTION18( CHAIN E AND RESID 52:71 )E52 - 71
19X-RAY DIFFRACTION19( CHAIN E AND RESID 72:96 )E72 - 96
20X-RAY DIFFRACTION20( CHAIN E AND RESID 97:120 )E97 - 120
21X-RAY DIFFRACTION21( CHAIN E AND RESID 121:129 )E121 - 129
22X-RAY DIFFRACTION22( CHAIN E AND RESID 130:142 )E130 - 142
23X-RAY DIFFRACTION23( CHAIN E AND RESID 143:161 )E143 - 161
24X-RAY DIFFRACTION24( CHAIN E AND RESID 162:177 )E162 - 177
25X-RAY DIFFRACTION25( CHAIN F AND RESID 51:72 )F51 - 72
26X-RAY DIFFRACTION26( CHAIN F AND RESID 73:84 )F73 - 84
27X-RAY DIFFRACTION27( CHAIN F AND RESID 85:96 )F85 - 96
28X-RAY DIFFRACTION28( CHAIN F AND RESID 97:129 )F97 - 129
29X-RAY DIFFRACTION29( CHAIN F AND RESID 130:142 )F130 - 142
30X-RAY DIFFRACTION30( CHAIN F AND RESID 143:164 )F143 - 164
31X-RAY DIFFRACTION31( CHAIN F AND RESID 165:178 )F165 - 178

+
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