[English] 日本語
Yorodumi
- PDB-4nux: Structure of receptor A -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 4nux
TitleStructure of receptor A
ComponentsInterleukin-17 receptor A
KeywordsIMMUNE SYSTEM / SEFIR domain / cytokine / receptor / autoimmune inflammatory
Function / homology
Function and homology information


interleukin-17 receptor activity / granulocyte chemotaxis / Interleukin-17 signaling / T-helper 17 type immune response / interleukin-17A-mediated signaling pathway / positive regulation of interleukin-23 production / positive regulation of chemokine (C-X-C motif) ligand 1 production / interleukin-17-mediated signaling pathway / positive regulation of interleukin-13 production / positive regulation of interleukin-5 production ...interleukin-17 receptor activity / granulocyte chemotaxis / Interleukin-17 signaling / T-helper 17 type immune response / interleukin-17A-mediated signaling pathway / positive regulation of interleukin-23 production / positive regulation of chemokine (C-X-C motif) ligand 1 production / interleukin-17-mediated signaling pathway / positive regulation of interleukin-13 production / positive regulation of interleukin-5 production / fibroblast activation / positive regulation of cytokine production involved in inflammatory response / defense response to fungus / response to virus / protein catabolic process / positive regulation of inflammatory response / positive regulation of interleukin-6 production / cell surface receptor signaling pathway / inflammatory response / innate immune response / signaling receptor binding / SARS-CoV-2 activates/modulates innate and adaptive immune responses / extracellular region / plasma membrane
Similarity search - Function
Interleukin 17 receptor D / Interleukin-17 receptor, fibronectin-III-like domain 1 / Interleukin-17 receptor A/B, FnIII-like domain 1 superfamily / Interleukin-17 receptor A/B, FnIII-like domain 2 superfamily / Interleukin-17 receptor, fibronectin-III-like domain 1 / Interleukin-17 receptor-like / SEFIR domain / SEFIR domain / SEFIR domain profile.
Similarity search - Domain/homology
Interleukin-17 receptor A
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / SAD / Resolution: 2.295 Å
AuthorsZhang, B. / Han, Y. / Deng, J.
CitationJournal: Acta Crystallogr.,Sect.D / Year: 2014
Title: Structure of the unique SEFIR domain from human interleukin 17 receptor A reveals a composite ligand-binding site containing a conserved alpha-helix for Act1 binding and IL-17 signaling.
Authors: Zhang, B. / Liu, C. / Qian, W. / Han, Y. / Li, X. / Deng, J.
History
DepositionDec 4, 2013Deposition site: RCSB / Processing site: RCSB
Revision 1.0May 14, 2014Provider: repository / Type: Initial release
Revision 1.1Sep 24, 2014Group: Database references
Revision 1.2Feb 28, 2024Group: Data collection / Database references / Category: chem_comp_atom / chem_comp_bond / database_2
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: Interleukin-17 receptor A


Theoretical massNumber of molelcules
Total (without water)24,7721
Polymers24,7721
Non-polymers00
Water97354
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
Unit cell
Length a, b, c (Å)76.256, 136.130, 55.433
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number20
Space group name H-MC2221

-
Components

#1: Protein Interleukin-17 receptor A / IL-17 receptor A / IL-17RA / CDw217


Mass: 24771.557 Da / Num. of mol.: 1 / Fragment: SEFIR domain (UNP residues 376-591)
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: IL17RA, IL17R / Production host: Escherichia coli (E. coli) / References: UniProt: Q96F46
#2: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 54 / Source method: isolated from a natural source / Formula: H2O

-
Experimental details

-
Experiment

ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 2

-
Sample preparation

CrystalDensity Matthews: 2.9 Å3/Da / Density % sol: 57.64 %
Crystal growTemperature: 293 K / Method: evaporation / pH: 6
Details: 0.1M MES, 5%PEG6000, pH 6.0, EVAPORATION, temperature 293K

-
Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 19-ID / Wavelength: 0.97918 Å
DetectorType: ADSC QUANTUM 315 / Detector: CCD / Date: Aug 14, 2012
RadiationMonochromator: GRAPHITE / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97918 Å / Relative weight: 1
ReflectionResolution: 2.3→50 Å / Num. all: 13265 / Num. obs: 13104 / % possible obs: 98.7 % / Observed criterion σ(I): 2.3
Reflection shell
Resolution (Å)Redundancy (%)Mean I/σ(I) obsNum. unique allDiffraction-ID% possible all
2.3-2.344.81.6559187.3
6.24-506.652.9740199.7
4.95-6.246.835.86871100
4.33-4.956.937.66731100
3.93-4.337.131.16691100
3.65-3.937.126.66761100
3.44-3.657.221.96611100
3.26-3.447.220.46571100
3.12-3.267.214.76651100
3-3.127.210.86581100
2.9-37.38.86521100
2.81-2.97.37.66551100
2.73-2.817.35.46611100
2.66-2.737.256631100
2.59-2.667.33.86341100
2.53-2.597.13.66541100
2.48-2.536.636631100
2.43-2.485.92.4649199.8
2.38-2.435.32626197.4
2.34-2.384.31.6602191.5

-
Processing

Software
NameVersionClassification
HKL-3000data collection
PHENIX(phenix.refine: 1.6_289)refinement
HKL-3000data reduction
HKL-3000data scaling
RefinementMethod to determine structure: SAD / Resolution: 2.295→33.264 Å / SU ML: 0.3 / σ(F): 0.26 / Phase error: 25.78 / Stereochemistry target values: ML
RfactorNum. reflection% reflectionSelection details
Rfree0.2418 1220 10.06 %10%
Rwork0.1893 ---
obs0.1948 12124 91.21 %-
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 39.582 Å2 / ksol: 0.349 e/Å3
Displacement parameters
Baniso -1Baniso -2Baniso -3
1-9.407 Å2-0 Å2-0 Å2
2---3.3092 Å20 Å2
3----6.0979 Å2
Refinement stepCycle: LAST / Resolution: 2.295→33.264 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms1579 0 0 54 1633
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0081612
X-RAY DIFFRACTIONf_angle_d1.0662183
X-RAY DIFFRACTIONf_dihedral_angle_d16.285586
X-RAY DIFFRACTIONf_chiral_restr0.073233
X-RAY DIFFRACTIONf_plane_restr0.004283
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.2946-2.38640.31131020.2404928X-RAY DIFFRACTION71
2.3864-2.4950.30481300.22231083X-RAY DIFFRACTION84
2.495-2.62650.28331340.21011168X-RAY DIFFRACTION89
2.6265-2.7910.29431260.21611189X-RAY DIFFRACTION90
2.791-3.00640.28951410.22011236X-RAY DIFFRACTION94
3.0064-3.30860.26631340.19241285X-RAY DIFFRACTION96
3.3086-3.78680.22261460.17451293X-RAY DIFFRACTION98
3.7868-4.76880.18241490.14761320X-RAY DIFFRACTION98
4.7688-33.2680.21521580.17811402X-RAY DIFFRACTION99
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)
12.2169-0.26510.67564.0827-1.29240.5637-0.54990.2440.1826-0.26480.4409-0.1042-0.1389-0.41460.0810.40580.1371-0.17190.23520.01370.265938.265654.333927.6504
22.01540.58610.04161.17140.13850.00210.1936-0.31390.09090.0253-0.3115-0.15350.28640.16230.02380.20250.02860.01530.2380.01560.109749.829544.710139.1276
31.44060.50790.35131.59491.68092.02640.2001-0.19840.28940.4806-0.25030.39580.2135-0.2771-0.00910.1390.06880.00780.1005-0.04040.108741.957954.182936.539
42.4788-1.1506-2.23692.1001-0.59454.2862-0.3766-0.86840.11990.3742-0.07320.22630.0523-1.33680.39290.3052-0.0561-0.04290.57980.0330.40834.801637.700734.7849
55.43770.0284-1.47836.2409-3.15592.073-0.35741.0535-0.8172-0.09380.66990.24910.4438-0.7925-0.57110.19980.0387-0.13760.4711-0.03380.298237.320240.509825.1182
61.17520.96720.23522.10851.20241.1895-0.59450.05030.1377-0.57280.44210.1992-0.7821-0.30890.19770.48220.0839-0.03420.23840.05650.218740.363750.733622.6003
73.62110.4964-0.0860.4766-0.6141.90460.0623-0.3524-0.4594-0.03620.1202-0.48570.3280.0559-0.05420.15860.00570.06610.1458-0.00450.206457.208138.214628.6682
85.4235-1.28881.72510.59080.26557.30390.2496-0.5921-1.45370.0821-0.270.23250.6211-0.12230.33380.18760.12470.01990.1502-0.06710.233656.497830.150631.9596
93.3515-1.40380.28826.8858-2.76162.88890.4790.4205-0.18430.3344-0.01410.14270.15760.0252-0.34750.24440.0151-0.04830.20820.05220.219848.364534.878237.6886
101.5226-0.0328-1.24151.40811.42912.31970.27670.46-0.31480.0054-0.1493-0.2961-0.5377-0.3142-0.03440.25140.0822-0.03410.2579-0.03470.123848.283440.934319.1642
111.44531.69691.39461.89281.34512.3718-0.21940.2120.1728-0.39340.1255-0.1765-0.43570.30740.11890.18420.0468-0.0130.125-0.0240.185452.938351.046526.4911
121.5096-0.4224-1.23833.70170.03411.40830.23040.0635-0.0412-0.3375-0.65060.1187-0.02620.54250.33790.17880.0909-0.00530.2068-0.0490.266659.294645.147826.2744
131.6142-0.87961.61751.37690.24145.9372-0.46980.35750.2568-0.0124-0.4768-0.3123-0.17330.76440.52680.33620.0220.12090.29930.14150.2156.514155.992527.718
144.03891.86912.7185.29923.88488.30990.0604-0.07570.7664-0.9305-1.0394-0.3633-2.1923-0.12120.7330.85050.04890.02470.15280.06330.295350.247662.814327.3409
153.66590.1979-3.29610.6443-0.60569.8303-0.50980.3917-0.2321-0.7089-0.1033-0.50820.463-0.52670.58630.36750.04680.10660.20710.06860.256544.881461.183423.4223
162.86030.2291-0.20544.40871.57662.18740.4271-0.60360.61230.6854-0.2363-1.1140.55890.3946-0.48510.3704-0.0360.1148-0.0247-0.06480.335952.52665.630336.9091
171.8244-0.23911.35421.8564-1.28561.8252-0.1884-0.47910.55240.89650.0181-0.4164-0.6268-0.03910.33620.2768-0.0621-0.06520.2087-0.04260.10753.716555.109845.1963
189.22446.672-6.0735.116-4.31024.0150.7888-0.47290.20641.2402-0.2650.46340.18630.0052-0.33080.2742-0.0961-0.14640.30830.06740.252862.809342.989347.9093
197.5492-4.4085-3.07864.89764.38064.14210.5745-0.5337-0.1536-0.81851.0662-0.8728-0.12170.7197-1.33220.34010.06230.07850.29-0.0370.316961.194937.077141.6224
203.2021-2.2727-1.11787.70995.70274.35920.47340.39230.64350.9636-0.5551-0.96531.6836-0.35990.33980.3985-0.0274-0.04560.20170.08160.194856.264829.618940.8538
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1(chain A and resid 376:381)
2X-RAY DIFFRACTION2(chain A and resid 382:396)
3X-RAY DIFFRACTION3(chain A and resid 397:414)
4X-RAY DIFFRACTION4(chain A and resid 415:425)
5X-RAY DIFFRACTION5(chain A and resid 426:434)
6X-RAY DIFFRACTION6(chain A and resid 435:445)
7X-RAY DIFFRACTION7(chain A and resid 446:460)
8X-RAY DIFFRACTION8(chain A and resid 461:467)
9X-RAY DIFFRACTION9(chain A and resid 468:478)
10X-RAY DIFFRACTION10(chain A and resid 479:493)
11X-RAY DIFFRACTION11(chain A and resid 494:507)
12X-RAY DIFFRACTION12(chain A and resid 508:517)
13X-RAY DIFFRACTION13(chain A and resid 518:529)
14X-RAY DIFFRACTION14(chain A and resid 530:534)
15X-RAY DIFFRACTION15(chain A and resid 535:539)
16X-RAY DIFFRACTION16(chain A and resid 540:560)
17X-RAY DIFFRACTION17(chain A and resid 561:576)
18X-RAY DIFFRACTION18(chain A and resid 577:582)
19X-RAY DIFFRACTION19(chain A and resid 583:586)
20X-RAY DIFFRACTION20(chain A and resid 587:591)

+
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://pdbjlvh1.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