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- PDB-5nti: Structural states of RORgt: X-ray elucidation of molecular mechan... -

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Basic information

Entry
Database: PDB / ID: 5nti
TitleStructural states of RORgt: X-ray elucidation of molecular mechanisms and binding interactions for natural and synthetic compounds
Components
  • ASN-SER-HIS-GLN-LYS-VAL-THR-LEU-LEU-GLN-LEU-LEU-LEU-GLY-HIS-LYS-ASN-GLU-GLU-ASN
  • Nuclear receptor ROR-gamma
KeywordsSIGNALING PROTEIN / nuclear hormone receptor / ligand-binding domain / agonist
Function / homology
Function and homology information


ovarian follicle rupture / NR1H2 & NR1H3 regulate gene expression linked to gluconeogenesis / T-helper 17 cell differentiation / ligand-activated transcription factor activity / cellular response to sterol / regulation of steroid metabolic process / NR1H2 & NR1H3 regulate gene expression linked to lipogenesis / lipid storage / nuclear glucocorticoid receptor binding / Peyer's patch development ...ovarian follicle rupture / NR1H2 & NR1H3 regulate gene expression linked to gluconeogenesis / T-helper 17 cell differentiation / ligand-activated transcription factor activity / cellular response to sterol / regulation of steroid metabolic process / NR1H2 & NR1H3 regulate gene expression linked to lipogenesis / lipid storage / nuclear glucocorticoid receptor binding / Peyer's patch development / positive regulation of circadian rhythm / oxysterol binding / T-helper cell differentiation / RUNX3 Regulates Immune Response and Cell Migration / negative regulation of thymocyte apoptotic process / regulation of fat cell differentiation / histone deacetylase complex / regulation of glucose metabolic process / lymph node development / adipose tissue development / nuclear retinoid X receptor binding / xenobiotic metabolic process / SUMOylation of transcription cofactors / cellular response to estradiol stimulus / nuclear estrogen receptor binding / nuclear receptor binding / circadian regulation of gene expression / Heme signaling / fibrillar center / DNA-binding transcription repressor activity, RNA polymerase II-specific / histone deacetylase binding / Nuclear Receptor transcription pathway / circadian rhythm / transcription corepressor activity / nuclear receptor activity / sequence-specific double-stranded DNA binding / Circadian Clock / Interleukin-4 and Interleukin-13 signaling / Estrogen-dependent gene expression / transcription coactivator activity / nuclear body / DNA-binding transcription factor activity, RNA polymerase II-specific / nuclear speck / RNA polymerase II cis-regulatory region sequence-specific DNA binding / DNA-binding transcription factor activity / signaling receptor binding / chromatin / nucleolus / regulation of transcription by RNA polymerase II / positive regulation of DNA-templated transcription / negative regulation of transcription by RNA polymerase II / positive regulation of transcription by RNA polymerase II / zinc ion binding / nucleoplasm / nucleus / cytosol
Similarity search - Function
Nuclear receptor-interacting protein 1 / Nuclear receptor-interacting protein 1, repression domain 1 / Nuclear receptor-interacting protein 1, repression domain 2 / Nuclear receptor-interacting protein 1, repression domain 3 / Nuclear receptor-interacting protein 1, repression domain 4 / Nuclear receptor-interacting protein 1 repression 1 / Nuclear receptor-interacting protein 1 repression 2 / Nuclear receptor-interacting protein 1 repression 3 / Nuclear receptor-interacting protein 1 repression 4 / Nuclear receptor ROR ...Nuclear receptor-interacting protein 1 / Nuclear receptor-interacting protein 1, repression domain 1 / Nuclear receptor-interacting protein 1, repression domain 2 / Nuclear receptor-interacting protein 1, repression domain 3 / Nuclear receptor-interacting protein 1, repression domain 4 / Nuclear receptor-interacting protein 1 repression 1 / Nuclear receptor-interacting protein 1 repression 2 / Nuclear receptor-interacting protein 1 repression 3 / Nuclear receptor-interacting protein 1 repression 4 / Nuclear receptor ROR / Retinoid-related orphan receptors, DNA-binding domain / Retinoid X Receptor / Retinoid X Receptor / Nuclear hormone receptor / Nuclear hormones receptors DNA-binding region signature. / Zinc finger, nuclear hormone receptor-type / Zinc finger, C4 type (two domains) / Nuclear hormone receptors DNA-binding domain profile. / c4 zinc finger in nuclear hormone receptors / Nuclear hormone receptor, ligand-binding domain / Nuclear hormone receptor-like domain superfamily / Ligand-binding domain of nuclear hormone receptor / Nuclear receptor (NR) ligand-binding (LBD) domain profile. / Ligand binding domain of hormone receptors / Zinc finger, NHR/GATA-type / Orthogonal Bundle / Mainly Alpha
Similarity search - Domain/homology
CHOLEST-5-EN-3-YL HYDROGEN SULFATE / Nuclear receptor-interacting protein 1 / Nuclear receptor ROR-gamma
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.4 Å
AuthorsKallen, J.
CitationJournal: ChemMedChem / Year: 2017
Title: Structural States of ROR gamma t: X-ray Elucidation of Molecular Mechanisms and Binding Interactions for Natural and Synthetic Compounds.
Authors: Kallen, J. / Izaac, A. / Be, C. / Arista, L. / Orain, D. / Kaupmann, K. / Guntermann, C. / Hoegenauer, K. / Hintermann, S.
History
DepositionApr 28, 2017Deposition site: PDBE / Processing site: PDBE
Revision 1.0Jun 21, 2017Provider: repository / Type: Initial release
Revision 1.1Jul 19, 2017Group: Database references / Category: citation
Item: _citation.country / _citation.journal_volume ..._citation.country / _citation.journal_volume / _citation.page_first / _citation.page_last / _citation.title
Revision 1.2May 1, 2024Group: Data collection / Database references / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Nuclear receptor ROR-gamma
B: Nuclear receptor ROR-gamma
C: Nuclear receptor ROR-gamma
D: Nuclear receptor ROR-gamma
P: ASN-SER-HIS-GLN-LYS-VAL-THR-LEU-LEU-GLN-LEU-LEU-LEU-GLY-HIS-LYS-ASN-GLU-GLU-ASN
Q: ASN-SER-HIS-GLN-LYS-VAL-THR-LEU-LEU-GLN-LEU-LEU-LEU-GLY-HIS-LYS-ASN-GLU-GLU-ASN
R: ASN-SER-HIS-GLN-LYS-VAL-THR-LEU-LEU-GLN-LEU-LEU-LEU-GLY-HIS-LYS-ASN-GLU-GLU-ASN
S: ASN-SER-HIS-GLN-LYS-VAL-THR-LEU-LEU-GLN-LEU-LEU-LEU-GLY-HIS-LYS-ASN-GLU-GLU-ASN
hetero molecules


Theoretical massNumber of molelcules
Total (without water)130,10312
Polymers128,2368
Non-polymers1,8674
Water9,656536
1
A: Nuclear receptor ROR-gamma
P: ASN-SER-HIS-GLN-LYS-VAL-THR-LEU-LEU-GLN-LEU-LEU-LEU-GLY-HIS-LYS-ASN-GLU-GLU-ASN
hetero molecules


Theoretical massNumber of molelcules
Total (without water)32,5263
Polymers32,0592
Non-polymers4671
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area1940 Å2
ΔGint-18 kcal/mol
Surface area12590 Å2
MethodPISA
2
B: Nuclear receptor ROR-gamma
Q: ASN-SER-HIS-GLN-LYS-VAL-THR-LEU-LEU-GLN-LEU-LEU-LEU-GLY-HIS-LYS-ASN-GLU-GLU-ASN
hetero molecules


Theoretical massNumber of molelcules
Total (without water)32,5263
Polymers32,0592
Non-polymers4671
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area1970 Å2
ΔGint-18 kcal/mol
Surface area12600 Å2
MethodPISA
3
C: Nuclear receptor ROR-gamma
R: ASN-SER-HIS-GLN-LYS-VAL-THR-LEU-LEU-GLN-LEU-LEU-LEU-GLY-HIS-LYS-ASN-GLU-GLU-ASN
hetero molecules


Theoretical massNumber of molelcules
Total (without water)32,5263
Polymers32,0592
Non-polymers4671
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area1960 Å2
ΔGint-18 kcal/mol
Surface area12590 Å2
MethodPISA
4
D: Nuclear receptor ROR-gamma
S: ASN-SER-HIS-GLN-LYS-VAL-THR-LEU-LEU-GLN-LEU-LEU-LEU-GLY-HIS-LYS-ASN-GLU-GLU-ASN
hetero molecules


Theoretical massNumber of molelcules
Total (without water)32,5263
Polymers32,0592
Non-polymers4671
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2020 Å2
ΔGint-19 kcal/mol
Surface area12590 Å2
MethodPISA
Unit cell
Length a, b, c (Å)86.289, 70.000, 96.863
Angle α, β, γ (deg.)90.000, 108.070, 90.000
Int Tables number4
Space group name H-MP1211

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Components

#1: Protein
Nuclear receptor ROR-gamma / Nuclear receptor RZR-gamma / Nuclear receptor subfamily 1 group F member 3 / RAR-related orphan ...Nuclear receptor RZR-gamma / Nuclear receptor subfamily 1 group F member 3 / RAR-related orphan receptor C / Retinoid-related orphan receptor-gamma


Mass: 29739.316 Da / Num. of mol.: 4 / Fragment: C-terminal domain, ligand binding domain / Mutation: C455S
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: RORC, NR1F3, RORG, RZRG / Plasmid: pET28-derived vector / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: P51449
#2: Protein/peptide
ASN-SER-HIS-GLN-LYS-VAL-THR-LEU-LEU-GLN-LEU-LEU-LEU-GLY-HIS-LYS-ASN-GLU-GLU-ASN / Nuclear factor RIP140 / Receptor-interacting protein 140


Mass: 2319.615 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P48552*PLUS
#3: Chemical
ChemComp-C3S / CHOLEST-5-EN-3-YL HYDROGEN SULFATE / CHOLESTEROL-SULFATE


Mass: 466.717 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C27H46O4S
#4: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 536 / Source method: isolated from a natural source / Formula: H2O

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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: 2.17 Å3/Da / Density % sol: 43.28 % / Mosaicity: 0.751 °
Crystal growTemperature: 298 K / Method: vapor diffusion, hanging drop / pH: 7 / Details: 14% PEG 3350, 0.04M NaFormate

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SLS / Beamline: X10SA / Wavelength: 0.9781 Å
DetectorType: MARMOSAIC 225 mm CCD / Detector: CCD / Date: Feb 8, 2008
RadiationMonochromator: SI 111 channel / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9781 Å / Relative weight: 1
ReflectionResolution: 2.4→20 Å / Num. obs: 38823 / % possible obs: 89.6 % / Redundancy: 5.8 % / Rmerge(I) obs: 0.091 / Χ2: 0.975 / Net I/σ(I): 9.3 / Num. measured all: 224418
Reflection shell
Resolution (Å)Redundancy (%)Rmerge(I) obsΧ2Diffraction-ID% possible all
2.4-2.493.10.1470.426145.9
2.49-2.583.20.1540.483165.6
2.58-2.73.60.1540.525186.5
2.7-2.844.50.1570.569198
2.84-3.025.70.1480.627199.9
3.02-3.256.60.1270.7471100
3.25-3.586.90.1150.9791100
3.58-4.096.90.0961.241100
4.09-5.147.20.0671.2961100
5.14-207.20.051.446199.9

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Processing

Software
NameVersionClassification
SCALEPACKdata scaling
REFMAC5refinement
PDB_EXTRACT3.22data extraction
DENZOdata reduction
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 1fbzg

Resolution: 2.4→19.94 Å / Cor.coef. Fo:Fc: 0.934 / Cor.coef. Fo:Fc free: 0.919 / SU B: 7.236 / SU ML: 0.17 / SU R Cruickshank DPI: 1.4952 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 1.495 / ESU R Free: 0.291
Details: HYDROGENS HAVE BEEN USED IF PRESENT IN THE INPUT U VALUES : REFINED INDIVIDUALLY
RfactorNum. reflection% reflectionSelection details
Rfree0.2328 1987 5.1 %RANDOM
Rwork0.1992 ---
obs0.201 36778 89.71 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å
Displacement parametersBiso max: 74.89 Å2 / Biso mean: 29.42 Å2 / Biso min: 10.4 Å2
Baniso -1Baniso -2Baniso -3
1--2.35 Å20 Å20.27 Å2
2--1.51 Å20 Å2
3---0.62 Å2
Refinement stepCycle: final / Resolution: 2.4→19.94 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms8256 0 128 536 8920
Biso mean--20.75 31.8 -
Num. residues----1011
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0060.0218593
X-RAY DIFFRACTIONr_angle_refined_deg0.8691.97511613
X-RAY DIFFRACTIONr_dihedral_angle_1_deg4.00651011
X-RAY DIFFRACTIONr_dihedral_angle_2_deg34.16723.084415
X-RAY DIFFRACTIONr_dihedral_angle_3_deg14.446151562
X-RAY DIFFRACTIONr_dihedral_angle_4_deg15.7771569
X-RAY DIFFRACTIONr_chiral_restr0.0560.21305
X-RAY DIFFRACTIONr_gen_planes_refined0.0030.026327
LS refinement shellResolution: 2.4→2.461 Å / Rfactor Rfree error: 0 / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.268 73 -
Rwork0.222 1326 -
all-1399 -
obs--44.71 %

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