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- PDB-5uyx: Structure of Human T-complex protein 1 subunit epsilon (CCT5) -

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Basic information

Entry
Database: PDB / ID: 5uyx
TitleStructure of Human T-complex protein 1 subunit epsilon (CCT5)
ComponentsT-complex protein 1 subunit epsilon
KeywordsCHAPERONE / chaperonin Hexadecameric complex ATP-dependent CCT5 gene
Function / homology
Function and homology information


positive regulation of protein localization to Cajal body / positive regulation of establishment of protein localization to telomere / BBSome-mediated cargo-targeting to cilium / chaperonin-containing T-complex / Folding of actin by CCT/TriC / positive regulation of telomerase RNA localization to Cajal body / Formation of tubulin folding intermediates by CCT/TriC / binding of sperm to zona pellucida / Prefoldin mediated transfer of substrate to CCT/TriC / beta-tubulin binding ...positive regulation of protein localization to Cajal body / positive regulation of establishment of protein localization to telomere / BBSome-mediated cargo-targeting to cilium / chaperonin-containing T-complex / Folding of actin by CCT/TriC / positive regulation of telomerase RNA localization to Cajal body / Formation of tubulin folding intermediates by CCT/TriC / binding of sperm to zona pellucida / Prefoldin mediated transfer of substrate to CCT/TriC / beta-tubulin binding / Association of TriC/CCT with target proteins during biosynthesis / chaperone-mediated protein folding / protein folding chaperone / positive regulation of telomere maintenance via telomerase / mRNA 3'-UTR binding / ATP-dependent protein folding chaperone / response to virus / mRNA 5'-UTR binding / Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding / G-protein beta-subunit binding / unfolded protein binding / protein folding / cell body / microtubule / protein stabilization / centrosome / ATP hydrolysis activity / extracellular exosome / ATP binding / cytosol
Similarity search - Function
GROEL; domain 2 / TCP-1-like chaperonin intermediate domain / GROEL; domain 1 / GroEL-like equatorial domain / T-complex protein 1, epsilon subunit / Chaperonins TCP-1 signature 1. / Chaperonins TCP-1 signature 2. / Chaperonin TCP-1, conserved site / Chaperonins TCP-1 signature 3. / Chaperone tailless complex polypeptide 1 (TCP-1) ...GROEL; domain 2 / TCP-1-like chaperonin intermediate domain / GROEL; domain 1 / GroEL-like equatorial domain / T-complex protein 1, epsilon subunit / Chaperonins TCP-1 signature 1. / Chaperonins TCP-1 signature 2. / Chaperonin TCP-1, conserved site / Chaperonins TCP-1 signature 3. / Chaperone tailless complex polypeptide 1 (TCP-1) / GroEL-like equatorial domain superfamily / TCP-1-like chaperonin intermediate domain superfamily / GroEL-like apical domain superfamily / TCP-1/cpn60 chaperonin family / Chaperonin Cpn60/GroEL/TCP-1 family / 2-Layer Sandwich / Orthogonal Bundle / Mainly Alpha / Alpha Beta
Similarity search - Domain/homology
ADENOSINE-5'-DIPHOSPHATE / T-complex protein 1 subunit epsilon
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.5 Å
AuthorsPereira, J.H. / McAndrew, R.P. / Sergeeva, O.A. / Ralston, C.Y. / King, J.A. / Adams, P.D.
CitationJournal: Sci Rep / Year: 2017
Title: Structure of the human TRiC/CCT Subunit 5 associated with hereditary sensory neuropathy.
Authors: Pereira, J.H. / McAndrew, R.P. / Sergeeva, O.A. / Ralston, C.Y. / King, J.A. / Adams, P.D.
History
DepositionFeb 24, 2017Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jul 5, 2017Provider: repository / Type: Initial release
Revision 1.1Oct 4, 2023Group: 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: T-complex protein 1 subunit epsilon
B: T-complex protein 1 subunit epsilon
C: T-complex protein 1 subunit epsilon
D: T-complex protein 1 subunit epsilon
hetero molecules


Theoretical massNumber of molelcules
Total (without water)240,7098
Polymers239,0004
Non-polymers1,7094
Water0
1
A: T-complex protein 1 subunit epsilon
B: T-complex protein 1 subunit epsilon
C: T-complex protein 1 subunit epsilon
D: T-complex protein 1 subunit epsilon
hetero molecules

A: T-complex protein 1 subunit epsilon
B: T-complex protein 1 subunit epsilon
C: T-complex protein 1 subunit epsilon
D: T-complex protein 1 subunit epsilon
hetero molecules

A: T-complex protein 1 subunit epsilon
B: T-complex protein 1 subunit epsilon
C: T-complex protein 1 subunit epsilon
D: T-complex protein 1 subunit epsilon
hetero molecules

A: T-complex protein 1 subunit epsilon
B: T-complex protein 1 subunit epsilon
C: T-complex protein 1 subunit epsilon
D: T-complex protein 1 subunit epsilon
hetero molecules


Theoretical massNumber of molelcules
Total (without water)962,83532
Polymers955,99916
Non-polymers6,83516
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation2_655-x+1,-y,z1
crystal symmetry operation3_545-y+1/2,x-1/2,z1
crystal symmetry operation4_555y+1/2,-x+1/2,z1
Buried area81790 Å2
ΔGint-359 kcal/mol
Surface area318440 Å2
MethodPISA
Unit cell
Length a, b, c (Å)204.710, 204.710, 162.950
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number90
Space group name H-MP4212

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Components

#1: Protein
T-complex protein 1 subunit epsilon / TCP-1-epsilon / CCT-epsilon


Mass: 59749.957 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: CCT5, CCTE, KIAA0098 / Production host: Escherichia coli (E. coli) / References: UniProt: P48643
#2: Chemical
ChemComp-ADP / ADENOSINE-5'-DIPHOSPHATE / Adenosine diphosphate


Mass: 427.201 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C10H15N5O10P2 / Comment: ADP, energy-carrying molecule*YM

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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: 3.57 Å3/Da / Density % sol: 65.56 %
Crystal growTemperature: 298 K / Method: vapor diffusion, sitting drop / pH: 6.4
Details: 0.1 M Sodium acetate, 0.04 Mcitric acid, 0.06 MBis-tris propane pH 6.4, 25 %PEG400

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: ALS / Beamline: 5.0.2 / Wavelength: 1 Å
DetectorType: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Feb 16, 2016
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 3.5→75.7 Å / Num. obs: 44068 / % possible obs: 100 % / Redundancy: 13.3 % / Net I/σ(I): 13.7

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Processing

Software
NameVersionClassification
PHENIX(dev_2650: ???)refinement
xia2data reduction
xia2data scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 4V81
Resolution: 3.5→75.7 Å / SU ML: 0.57 / Cross valid method: FREE R-VALUE / σ(F): 1.35 / Phase error: 33.42 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.3182 2215 5.03 %
Rwork0.2686 --
obs0.2711 44057 99.67 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Refinement stepCycle: LAST / Resolution: 3.5→75.7 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms14641 0 108 0 14749
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00214924
X-RAY DIFFRACTIONf_angle_d0.66320135
X-RAY DIFFRACTIONf_dihedral_angle_d3.1519293
X-RAY DIFFRACTIONf_chiral_restr0.0432381
X-RAY DIFFRACTIONf_plane_restr0.0042583
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
3.5-3.57610.41281340.36282564X-RAY DIFFRACTION99
3.5761-3.65930.37251290.33812558X-RAY DIFFRACTION100
3.6593-3.75080.35551310.31832564X-RAY DIFFRACTION100
3.7508-3.85220.39161490.31192586X-RAY DIFFRACTION100
3.8522-3.96560.36081510.30472583X-RAY DIFFRACTION100
3.9656-4.09350.33751320.29122577X-RAY DIFFRACTION100
4.0935-4.23980.33461260.27842582X-RAY DIFFRACTION100
4.2398-4.40960.2781280.26382605X-RAY DIFFRACTION100
4.4096-4.61020.33281360.24742596X-RAY DIFFRACTION100
4.6102-4.85330.33571210.24872630X-RAY DIFFRACTION100
4.8533-5.15730.2851400.2572597X-RAY DIFFRACTION100
5.1573-5.55540.32951380.28962628X-RAY DIFFRACTION100
5.5554-6.11420.36011410.30162641X-RAY DIFFRACTION100
6.1142-6.99840.31341620.29422631X-RAY DIFFRACTION100
6.9984-8.81510.29051350.22622698X-RAY DIFFRACTION100
8.8151-75.71740.27741620.23472802X-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)
12.65270.1244-0.35145.49731.12253.91340.0408-0.408-0.43560.08520.1707-0.05520.32410.402-0.17830.44770.0557-0.04540.6295-0.0130.843963.134719.940778.6685
21.40060.688-1.13170.4059-1.90772.36890.0163-0.30960.15290.27720.3989-0.0678-0.1097-0.0041-0.37010.9240.12720.02380.9272-0.17420.742646.36517.336996.5735
31.2719-1.0841.5654-0.1856-2.02831.76970.1908-0.1074-0.0151-0.1042-0.07790.1680.01330.045-0.10911.05090.227-0.05831.090.03510.887662.52036.9258118.7104
43.61541.8115-0.85623.0455-0.06512.33670.14460.2813-0.0557-0.04660.01530.3789-0.4222-0.4322-0.15320.59920.18260.06920.4950.08220.974548.228926.978973.8668
55.53553.9769-2.37546.0856-1.85993.9276-0.1029-0.2341-0.7739-0.2773-0.1254-0.79250.3990.240.28340.58510.10550.02630.4548-0.02880.862788.325941.771378.7463
62.145-0.4056-2.3332.3199-0.11914.53320.4034-0.32980.17540.65630.10210.2516-0.1889-0.0466-0.56450.64180.2116-0.1640.51420.0070.699776.81256.129295.1372
70.0193-1.56860.81191.7009-2.32212.7918-0.045-0.3207-0.07550.00650.33380.2846-0.0455-0.3411-0.22521.2264-0.03490.00051.04760.10081.037879.645231.1345123.6819
84.1644-0.498-0.73412.42910.0292.213-0.1508-0.00740.037-0.02780.04170.0124-0.1671-0.23560.08670.52750.00770.0240.4553-0.07930.674882.640756.487877.4774
95.9541-0.0421-3.68262.83661.65923.3356-0.11720.4435-0.8939-0.3566-0.0189-0.0727-0.1935-0.29880.06880.6174-0.0102-0.0360.54320.05970.546997.178552.865640.5675
10-0.04881.13220.62852.06023.29813.44160.13060.10150.2999-0.9174-0.46330.1201-0.7713-0.44320.18811.56470.15780.21371.30.02961.3874106.49842.84561.4262
112.19770.9826-2.24775.03413.64395.3920.9132-0.09010.7599-0.9689-0.0548-1.1007-1.2392-0.248-0.75481.66180.05640.13341.0587-0.09451.178108.415244.88662.8701
125.04673.3996-1.09683.4825-0.44623.05410.03870.38950.7351-0.35290.2171-0.1334-0.7849-0.2999-0.21340.63280.08110.12020.45970.01340.813798.942260.828944.2168
135.85352.11330.24077.1009-1.97855.19340.35350.0723-0.18560.7674-0.43160.0618-0.32570.71410.28420.6057-0.0121-0.13460.7628-0.01960.959473.3230.219843.1014
142.10422.2023-3.57192.139-3.88047.2407-1.03140.752-2.2333-1.4106-0.5583-3.37421.8378-0.32631.14130.8128-0.03020.14990.78820.00761.415973.664729.091636.1957
151.64721.507-3.87014.4408-3.99656.07660.22240.3707-0.1094-0.6963-0.0697-0.45660.6875-0.51740.03340.56730.10370.01710.719-0.10940.763256.065336.421239.3486
160.8113-0.8693-1.880.71311.26782.04480.19840.04350.10110.3320.2239-0.0539-0.1779-0.5818-0.37561.5160.40170.11661.48950.24271.676867.635941.52217.6914
170.93620.39550.30012.5238-1.19991.59930.1512-0.06360.7383-0.55370.0271-0.0579-0.64710.6672-0.31931.0160.24710.18181.3164-0.1240.949787.093115.805-11.4473
182.3130.9321-0.77082.15710.2036.59710.92421.05270.7751-0.00240.12270.2755-0.9072-0.7485-0.84431.41810.52570.08061.95280.03441.2574.37129.5441-2.1066
193.95630.0591-2.17273.5788-1.81413.08181.59490.96480.013-0.4228-0.437-1.7273-3.23151.877-1.29261.35180.15060.23791.0555-0.37140.646370.53444.99767.7783
201.2998-0.90370.05977.4577-0.82143.74430.0668-0.19570.4627-0.28950.25030.3976-0.878-0.6478-0.32160.75320.17380.08470.62790.09690.873455.525842.225245.4233
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1chain 'A' and (resid 31 through 129 )
2X-RAY DIFFRACTION2chain 'A' and (resid 130 through 241 )
3X-RAY DIFFRACTION3chain 'A' and (resid 242 through 414 )
4X-RAY DIFFRACTION4chain 'A' and (resid 415 through 536 )
5X-RAY DIFFRACTION5chain 'B' and (resid 31 through 129 )
6X-RAY DIFFRACTION6chain 'B' and (resid 130 through 230 )
7X-RAY DIFFRACTION7chain 'B' and (resid 231 through 393 )
8X-RAY DIFFRACTION8chain 'B' and (resid 394 through 536 )
9X-RAY DIFFRACTION9chain 'C' and (resid 31 through 182 )
10X-RAY DIFFRACTION10chain 'C' and (resid 183 through 295 )
11X-RAY DIFFRACTION11chain 'C' and (resid 296 through 397 )
12X-RAY DIFFRACTION12chain 'C' and (resid 398 through 536 )
13X-RAY DIFFRACTION13chain 'D' and (resid 31 through 67 )
14X-RAY DIFFRACTION14chain 'D' and (resid 68 through 91 )
15X-RAY DIFFRACTION15chain 'D' and (resid 92 through 183 )
16X-RAY DIFFRACTION16chain 'D' and (resid 184 through 256 )
17X-RAY DIFFRACTION17chain 'D' and (resid 257 through 293 )
18X-RAY DIFFRACTION18chain 'D' and (resid 294 through 356 )
19X-RAY DIFFRACTION19chain 'D' and (resid 357 through 405 )
20X-RAY DIFFRACTION20chain 'D' and (resid 406 through 528 )

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