[English] 日本語
Yorodumi
- PDB-9hv7: Crystal structure of Tetraspanin TSPAN10mutant Large Extracellula... -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 9hv7
TitleCrystal structure of Tetraspanin TSPAN10mutant Large Extracellular Loop (LEL)
ComponentsTetraspanin-10
KeywordsSIGNALING PROTEIN / Membrane organization / Signal Transductions
Function / homologyTetraspanin, conserved site / Transmembrane 4 family signature. / Tetraspanin, EC2 domain superfamily / Tetraspanin/Peripherin / Tetraspanin family / establishment of protein localization to organelle / enzyme binding / plasma membrane / Tetraspanin-10
Function and homology information
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.55 Å
AuthorsNagarathinam, K. / Krey, T.
Funding support1items
OrganizationGrant numberCountry
Not funded
CitationJournal: To Be Published
Title: Evolutionary relationship of Tetraspanins
Authors: Nagarathinam, K. / Karakulova, D. / Thiyagaraj, D. / Krey, T.
History
DepositionDec 24, 2024Deposition site: PDBE / Processing site: PDBE
Revision 1.0Nov 19, 2025Provider: repository / Type: Initial release

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: Tetraspanin-10
B: Tetraspanin-10


Theoretical massNumber of molelcules
Total (without water)27,9752
Polymers27,9752
Non-polymers00
Water1,910106
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area1130 Å2
ΔGint1 kcal/mol
Surface area13050 Å2
Unit cell
Length a, b, c (Å)62.300, 62.300, 117.480
Angle α, β, γ (deg.)90.000, 90.000, 90.000
Int Tables number96
Space group name H-MP43212
Space group name HallP4nw2abw
Symmetry operation#1: x,y,z
#2: -y+1/2,x+1/2,z+3/4
#3: y+1/2,-x+1/2,z+1/4
#4: x+1/2,-y+1/2,-z+1/4
#5: -x+1/2,y+1/2,-z+3/4
#6: -x,-y,z+1/2
#7: y,x,-z
#8: -y,-x,-z+1/2
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
d_1ens_1(chain "A" and (resid 176 through 186 or resid 188...
d_2ens_1(chain "B" and (resid 176 through 186 or resid 188...

NCS domain segments:

Ens-ID: ens_1

Dom-IDComponent-IDBeg auth comp-IDBeg label comp-IDEnd auth comp-IDEnd label comp-IDAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
d_11GLYGLYLEULEUAA176 - 1864 - 14
d_12VALVALASPASPAA188 - 24616 - 74
d_13GLNGLNLEULEUAA257 - 26385 - 91
d_14LEULEUARGARGAA265 - 28493 - 112
d_15TRPTRPLEULEUAA286 - 294114 - 122
d_16PHEPHEGLNGLNAA296 - 297124 - 125
d_21GLYGLYLEULEUBB176 - 1864 - 14
d_22VALVALASPASPBB188 - 24616 - 74
d_23GLNGLNLEULEUBB257 - 26385 - 91
d_24LEULEUARGARGBB265 - 28493 - 112
d_25TRPTRPLEULEUBB286 - 294114 - 122
d_26PHEPHEGLNGLNBB296 - 297124 - 125

NCS oper: (Code: givenMatrix: (-0.128220821005, 0.991458773817, 0.0238520624392), (0.991662452239, 0.127861471305, 0.0160319984484), (0.0128453057263, 0.0257088307329, -0.999586941763)Vector: 31. ...NCS oper: (Code: given
Matrix: (-0.128220821005, 0.991458773817, 0.0238520624392), (0.991662452239, 0.127861471305, 0.0160319984484), (0.0128453057263, 0.0257088307329, -0.999586941763)
Vector: 31.3299057783, -27.9509909054, 0.0752010663314)

-
Components

#1: Protein Tetraspanin-10 / Tspan-10 / Oculospanin


Mass: 13987.688 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: TSPAN10, OCSP / Production host: Drosophila melanogaster (fruit fly) / References: UniProt: Q9H1Z9
#2: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 106 / Source method: isolated from a natural source / Formula: H2O
Has protein modificationY

-
Experimental details

-
Experiment

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

-
Sample preparation

CrystalDensity Matthews: 2.09 Å3/Da / Density % sol: 41.24 % / Description: Tetragonal
Crystal growTemperature: 293 K / Method: vapor diffusion, sitting drop / pH: 6.5
Details: 0.3M Diethylene glycol; 0.3M Triethylene glycol; 0.3M Tetraethylene glycol;0.3M Pentaethylene glycol; 25% v/v MPD; 25% PEG 1000; 25% w/v PEG 3350

-
Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: SOLEIL / Beamline: PROXIMA 1 / Wavelength: 0.984002 Å
DetectorType: DECTRIS EIGER X 16M / Detector: PIXEL / Date: Jun 6, 2024
RadiationMonochromator: Si(111) crystal / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.984002 Å / Relative weight: 1
ReflectionResolution: 1.55→44.05 Å / Num. obs: 34211 / % possible obs: 99.91 % / Redundancy: 10.29 % / Biso Wilson estimate: 29.61 Å2 / CC1/2: 0.999 / Net I/σ(I): 16.22
Reflection shellResolution: 1.552→1.608 Å / Mean I/σ(I) obs: 1.18 / Num. unique obs: 3322 / CC1/2: 0.671

-
Processing

Software
NameVersionClassification
PHENIX1.21.2_5419refinement
MxCuBEdata collection
XDS20240712data reduction
XSCALEdata scaling
PHASERphasing
Cootmodel building
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 1.55→44.05 Å / SU ML: 0.2058 / Cross valid method: FREE R-VALUE / σ(F): 1.35 / Phase error: 22.1094
Stereochemistry target values: GeoStd + Monomer Library + CDL v1.2
RfactorNum. reflection% reflection
Rfree0.2276 1710 5 %
Rwork0.1971 32499 -
obs0.1986 34209 99.92 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.1 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso mean: 37.56 Å2
Refinement stepCycle: LAST / Resolution: 1.55→44.05 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms1772 0 0 106 1878
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00591810
X-RAY DIFFRACTIONf_angle_d0.83482460
X-RAY DIFFRACTIONf_chiral_restr0.0495263
X-RAY DIFFRACTIONf_plane_restr0.0088331
X-RAY DIFFRACTIONf_dihedral_angle_d16.4645652
Refine LS restraints NCSType: Torsion NCS / Rms dev position: 0.769710065019 Å
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
1.55-1.60.33391400.30252662X-RAY DIFFRACTION99.29
1.6-1.650.25561380.26312622X-RAY DIFFRACTION100
1.65-1.710.29251400.26422655X-RAY DIFFRACTION100
1.71-1.780.32831400.28272673X-RAY DIFFRACTION99.96
1.78-1.860.24111410.24042680X-RAY DIFFRACTION100
1.86-1.960.23711410.20312673X-RAY DIFFRACTION100
1.96-2.080.22541420.19652693X-RAY DIFFRACTION100
2.08-2.240.23281410.19752685X-RAY DIFFRACTION100
2.24-2.460.2031430.18082717X-RAY DIFFRACTION100
2.46-2.820.21981440.20212739X-RAY DIFFRACTION100
2.82-3.550.23011450.19372756X-RAY DIFFRACTION100
3.55-44.050.21811550.18252944X-RAY DIFFRACTION99.81
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)
13.849762256730.715039383514-3.498166350281.25938795847-1.071862214554.29993965276-0.272462713640.102134642044-0.89371299395-0.146556052165-0.3361597346650.2336396212030.607099914571-0.509720940237-0.1766042888850.192018405732-0.0410410907297-0.05870804759890.3784733188020.01389893210630.335487663843.59767844117-14.7285320593-11.4750779876
20.688869582888-0.6193646749630.1636296659190.7954730906740.195005992630.4993846943470.1067187341360.1188872281450.0427952631194-0.121485191278-0.251383974042-0.256686443045-0.1331351130180.232881314092-7.05683736844E-50.3026581624870.03470166031960.007089800560110.3381841944810.05049824212320.30337594802610.7386381793-6.83690014309-19.2947354677
33.043275626231.313669647831.433354398891.27996532883-0.3541088116112.001902425070.0860481626950.178329510598-0.345470584242-0.142829409760.0931883595141-0.402413274610.002884387449210.225708764897-0.0007138056348130.2931403001990.00635593103646-0.0260767256480.3419381075780.07437568890960.39831093115319.1665964295-14.5851458142-14.4069805666
42.38486967821-4.61318377215-0.231415013152.000815490822.837781611933.489619352871.085904842521.315614901950.777182573031-1.18118342763-0.178381192124-2.66587587795-0.3782134463270.6141948090770.3141603381690.3538354726440.02867550967790.1277328230970.5533265990990.01151779057670.7061941837325.3403358658-5.53892866288-13.1552175278
51.902334613611.33553124467-0.3854447449921.41331528868-0.05380612217342.49332792717-0.0726641577876-0.0795034126981-0.0515650016076-0.174698324817-0.0639699889629-0.2657897080180.7865504843190.743109521603-0.3151472515010.3090600592890.0312367138094-0.01300990900070.5227527447090.1170825367050.30187712997323.0205027228-11.4957952502-4.33418019876
60.0173279909143-0.0152647110256-0.100032514246-0.001090713684180.0545235872340.491247502798-0.11695511217-0.1910672962450.3973830795740.137106819993-0.0590652102037-0.136783462198-0.2598726458720.0810569593665-3.13966856165E-50.359499062155-0.00743246527817-0.0299495872860.3903076408870.03569654123770.361402089752-2.03915726741-2.30721298594-8.22194759499
70.302285603954-0.325868776756-0.2987784716850.4480252137960.1084516349510.710178853572-0.3737542506740.20667380851-0.6034455276160.2010216943080.0154642199830.6205262680461.19738106157-0.373281371069-0.01606164216760.405518184048-0.02381706735270.01038657792560.3014805224210.02600202058960.35675954537916.0121627799-26.644648638510.5656101407
80.911022775432-0.7419825386710.5160178472670.648531288537-0.4618842829830.326615582194-0.148516535307-0.3680864687830.05908615403970.4480004345040.09721132216390.16654685667-0.493848759448-0.15998077212-0.000182429756930.3132442239820.0297328350201-0.03464995744350.3128349416490.01416974899620.2751262155822.6825599228-18.588053482619.2163200876
91.851024312560.6787701158760.7287839036161.61935693697-1.509908897692.998588256080.114952397686-0.2209880285660.4641215703640.1094247355840.04033848458960.0499601171627-0.323570775602-0.071540861295-9.81797188831E-50.30538624034-0.0122324743017-0.03782165468880.255560565044-0.008104128850910.33785017788712.992750833-11.196315700914.5708517531
100.5443487985570.0248286126466-0.280084299630.274970092439-0.4548980769650.858903310045-0.0803083618583-0.1748734902740.8388528118550.4548072487590.1854424902240.0593598935383-0.5135237614680.116234567589-8.21792081732E-50.401812512532-0.00869004573675-0.05440304989940.333496713673-0.01441812748820.46401627360222.2090069691-5.7086387860513.7552461708
111.047514449561.26086882973-0.01329644527191.51665434859-0.07311598597472.384764164360.1760446860410.4397477684350.123116511658-0.0448305228342-0.0981579052254-0.214515354019-0.112805716238-0.43846151703-0.01962508244410.2955806881460.0432093591513-0.03119263042530.2960507692440.07887069171820.28108575964216.8449687582-6.27658775984.62733443827
122.249570520621.34528611322-1.356436413071.71363071279-0.05596354303071.435548770090.056353556753-0.268727361092-0.595686266153-0.316863592812-0.148630613121-0.3407753110290.2839774366940.1559428368460.002392722565540.402746029442-0.0193544928761-0.03761524813760.3437479100410.03700328431320.40175616239429.2640178549-30.22231988748.05399513917
Refinement TLS group

Refine-ID: X-RAY DIFFRACTION

IDRefine TLS-IDSelection detailsAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
11chain 'A' and (resid 176 through 191 )AA176 - 1911 - 16
22chain 'A' and (resid 192 through 210 )AA192 - 21017 - 35
33chain 'A' and (resid 211 through 243 )AA211 - 24336 - 68
44chain 'A' and (resid 244 through 261 )AA244 - 26169 - 77
55chain 'A' and (resid 262 through 278 )AA262 - 27878 - 94
66chain 'A' and (resid 279 through 297 )AA279 - 29795 - 113
77chain 'B' and (resid 175 through 191 )BB175 - 1911 - 17
88chain 'B' and (resid 192 through 210 )BB192 - 21018 - 36
99chain 'B' and (resid 211 through 238 )BB211 - 23837 - 64
1010chain 'B' and (resid 239 through 261 )BB239 - 26165 - 79
1111chain 'B' and (resid 262 through 278 )BB262 - 27880 - 96
1212chain 'B' and (resid 279 through 297 )BB279 - 29797 - 115

+
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