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- PDB-4l7c: Structure of keap1 kelch domain with 2-{[(1S)-2-{[(1R,2S)-2-(1H-t... -

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Basic information

Entry
Database: PDB / ID: 4l7c
TitleStructure of keap1 kelch domain with 2-{[(1S)-2-{[(1R,2S)-2-(1H-tetrazol-5-yl)cyclohexyl]carbonyl}-1,2,3,4-tetrahydroisoquinolin-1-yl]methyl}-1H-isoindole-1,3(2H)-dione
ComponentsKelch-like ECH-associated protein 1
KeywordsTRANSCRIPTION/INHIBITOR / STRESS SENSOR / KELCH DOMAIN / KELCH REPEAT MOTIF / BETA-PROPELLER / NRF2 / PROTEIN-SMALL MOLECULE COMPLEX / TRANSCRIPTION-INHIBITOR complex
Function / homology
Function and homology information


regulation of epidermal cell differentiation / Nuclear events mediated by NFE2L2 / negative regulation of response to oxidative stress / Cul3-RING ubiquitin ligase complex / ubiquitin-like ligase-substrate adaptor activity / transcription regulator inhibitor activity / inclusion body / cellular response to interleukin-4 / actin filament / centriolar satellite ...regulation of epidermal cell differentiation / Nuclear events mediated by NFE2L2 / negative regulation of response to oxidative stress / Cul3-RING ubiquitin ligase complex / ubiquitin-like ligase-substrate adaptor activity / transcription regulator inhibitor activity / inclusion body / cellular response to interleukin-4 / actin filament / centriolar satellite / disordered domain specific binding / KEAP1-NFE2L2 pathway / Antigen processing: Ubiquitination & Proteasome degradation / positive regulation of proteasomal ubiquitin-dependent protein catabolic process / Neddylation / cellular response to oxidative stress / midbody / ubiquitin-dependent protein catabolic process / in utero embryonic development / Potential therapeutics for SARS / proteasome-mediated ubiquitin-dependent protein catabolic process / RNA polymerase II-specific DNA-binding transcription factor binding / Ub-specific processing proteases / regulation of autophagy / protein ubiquitination / endoplasmic reticulum / negative regulation of transcription by RNA polymerase II / nucleoplasm / identical protein binding / cytoplasm / cytosol
Similarity search - Function
Kelch-type beta propeller / Kelch-like ECH-associated protein 1 / : / KLHDC2/KLHL20/DRC7 Kelch-repeats domain / BTB-kelch protein / BTB/Kelch-associated / BTB And C-terminal Kelch / BTB And C-terminal Kelch / Kelch motif / Kelch ...Kelch-type beta propeller / Kelch-like ECH-associated protein 1 / : / KLHDC2/KLHL20/DRC7 Kelch-repeats domain / BTB-kelch protein / BTB/Kelch-associated / BTB And C-terminal Kelch / BTB And C-terminal Kelch / Kelch motif / Kelch / Kelch repeat type 1 / Kelch-type beta propeller / BTB/POZ domain / BTB domain profile. / 6 Propeller / Neuraminidase / Broad-Complex, Tramtrack and Bric a brac / BTB/POZ domain / SKP1/BTB/POZ domain superfamily / Mainly Beta
Similarity search - Domain/homology
Chem-1VW / ACETATE ION / Kelch-like ECH-associated protein 1
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.4 Å
AuthorsJnoff, E. / Brookfield, F. / Albrecht, C. / Barker, J.J. / Barker, O. / Beaumont, E. / Bromidge, S. / Brooks, M. / Ceska, T. / Courade, J.P. ...Jnoff, E. / Brookfield, F. / Albrecht, C. / Barker, J.J. / Barker, O. / Beaumont, E. / Bromidge, S. / Brooks, M. / Ceska, T. / Courade, J.P. / Crabbe, T. / Duclos, S. / Fryatt, T. / Jigorel, E. / Kwong, J. / Sands, Z. / Smith, M.A.
CitationJournal: Chemmedchem / Year: 2014
Title: Binding Mode and Structure-Activity Relationships around Direct Inhibitors of the Nrf2-Keap1 Complex.
Authors: Jnoff, E. / Albrecht, C. / Barker, J.J. / Barker, O. / Beaumont, E. / Bromidge, S. / Brookfield, F. / Brooks, M. / Bubert, C. / Ceska, T. / Corden, V. / Dawson, G. / Duclos, S. / Fryatt, T. ...Authors: Jnoff, E. / Albrecht, C. / Barker, J.J. / Barker, O. / Beaumont, E. / Bromidge, S. / Brookfield, F. / Brooks, M. / Bubert, C. / Ceska, T. / Corden, V. / Dawson, G. / Duclos, S. / Fryatt, T. / Genicot, C. / Jigorel, E. / Kwong, J. / Maghames, R. / Mushi, I. / Pike, R. / Sands, Z.A. / Smith, M.A. / Stimson, C.C. / Courade, J.P.
History
DepositionJun 13, 2013Deposition site: RCSB / Processing site: RCSB
Revision 1.0Feb 19, 2014Provider: repository / Type: Initial release
Revision 1.1Apr 23, 2014Group: Database references
Revision 1.2Sep 20, 2023Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model / struct_ref_seq_dif / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_ref_seq_dif.details / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id
Revision 1.3Oct 30, 2024Group: Structure summary / Category: pdbx_entry_details / pdbx_modification_feature

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

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


Theoretical massNumber of molelcules
Total (without water)100,73611
Polymers99,0293
Non-polymers1,7078
Water3,585199
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)76.290, 125.610, 132.630
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number18
Space group name H-MP21221

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Components

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


Mass: 33009.801 Da / Num. of mol.: 3 / Fragment: Kelch domain, UNP residues 321-609 / Mutation: R354D
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: KEAP1, INRF2, KIAA0132, KLHL19 / Plasmid: pET28a / Production host: Escherichia coli (E. coli) / References: UniProt: Q14145
#2: Chemical ChemComp-1VW / 2-{[(1S)-2-{[(1R,2S)-2-(1H-tetrazol-5-yl)cyclohexyl]carbonyl}-1,2,3,4-tetrahydroisoquinolin-1-yl]methyl}-1H-isoindole-1,3(2H)-dione


Mass: 470.523 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: C26H26N6O3
#3: Chemical
ChemComp-ACT / ACETATE ION


Mass: 59.044 Da / Num. of mol.: 5 / Source method: obtained synthetically / Formula: C2H3O2
#4: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 199 / Source method: isolated from a natural source / Formula: H2O
Has protein modificationY

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Experimental details

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Experiment

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

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Sample preparation

CrystalDensity Matthews: 3.21 Å3/Da / Density % sol: 61.66 %
Crystal growTemperature: 296 K / Method: vapor diffusion, hanging drop / pH: 4.6
Details: 1 ul of protein at 12 mg/ml in 20 mM Tris-HCl pH 7.5, 5 mM DTT, 5 mM compound 1 + 2 ul of 2.15 M Sodium Acetate , VAPOR DIFFUSION, HANGING DROP, temperature 296K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SLS / Beamline: X06DA / Wavelength: 1 Å
DetectorType: DECTRIS PILATUS 2M / Detector: PIXEL / Date: Nov 22, 2012 / Details: mirror
RadiationMonochromator: Bartels Monochromator / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 2.4→36.71 Å / Num. all: 50637 / Num. obs: 48009 / % possible obs: 99.92 % / Observed criterion σ(F): 2 / Observed criterion σ(I): 2
Reflection shellResolution: 2.4→2.462 Å / % possible all: 100

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Processing

Software
NameVersionClassification
GO.COMdata collection
PHASERphasing
REFMAC5.7.0032refinement
XDSdata reduction
XDSdata scaling
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 1ZGK

1zgk


Resolution: 2.4→36.66 Å / Cor.coef. Fo:Fc: 0.902 / Cor.coef. Fo:Fc free: 0.886 / SU B: 9.881 / SU ML: 0.224 / Cross valid method: THROUGHOUT / ESU R: 0.385 / ESU R Free: 0.262 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.28064 2573 5.1 %RANDOM
Rwork0.26547 ---
all0.26626 50637 --
obs0.26626 48009 99.92 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso mean: 42.493 Å2
Baniso -1Baniso -2Baniso -3
1-0.76 Å20 Å2-0 Å2
2--0.06 Å20 Å2
3----0.81 Å2
Refinement stepCycle: LAST / Resolution: 2.4→36.66 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms6609 0 125 199 6933
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0040.0197004
X-RAY DIFFRACTIONr_bond_other_d0.0010.026301
X-RAY DIFFRACTIONr_angle_refined_deg0.9561.9569559
X-RAY DIFFRACTIONr_angle_other_deg0.643314416
X-RAY DIFFRACTIONr_dihedral_angle_1_deg5.2865875
X-RAY DIFFRACTIONr_dihedral_angle_2_deg29.93522.776335
X-RAY DIFFRACTIONr_dihedral_angle_3_deg13.628151020
X-RAY DIFFRACTIONr_dihedral_angle_4_deg14.9051567
X-RAY DIFFRACTIONr_chiral_restr0.0510.2999
X-RAY DIFFRACTIONr_gen_planes_refined0.0020.0218341
X-RAY DIFFRACTIONr_gen_planes_other0.0010.021767
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_it
X-RAY DIFFRACTIONr_mcbond_other
X-RAY DIFFRACTIONr_mcangle_it
X-RAY DIFFRACTIONr_scbond_it
X-RAY DIFFRACTIONr_scangle_it
X-RAY DIFFRACTIONr_rigid_bond_restr
X-RAY DIFFRACTIONr_sphericity_free
X-RAY DIFFRACTIONr_sphericity_bonded
LS refinement shellResolution: 2.4→2.462 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.383 187 -
Rwork0.377 3519 -
obs--100 %

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