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- PDB-3t5v: Sac3:Thp1:Sem1 complex -

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Basic information

Entry
Database: PDB / ID: 3t5v
TitleSac3:Thp1:Sem1 complex
Components
  • 26S proteasome complex subunit SEM1Proteasome
  • Nuclear mRNA export protein SAC3
  • Nuclear mRNA export protein THP1
KeywordsTRANSCRIPTION / PCI / mRNA nuclear export / mRNA / nuclear
Function / homology
Function and homology information


actin filament-based process / cellular bud site selection / SAGA complex localization to transcription regulatory region / transcription export complex 2 / post-transcriptional tethering of RNA polymerase II gene DNA at nuclear periphery / nuclear pore cytoplasmic filaments / nuclear mRNA surveillance / maintenance of DNA trinucleotide repeats / filamentous growth / mRNA 3'-end processing ...actin filament-based process / cellular bud site selection / SAGA complex localization to transcription regulatory region / transcription export complex 2 / post-transcriptional tethering of RNA polymerase II gene DNA at nuclear periphery / nuclear pore cytoplasmic filaments / nuclear mRNA surveillance / maintenance of DNA trinucleotide repeats / filamentous growth / mRNA 3'-end processing / proteasome regulatory particle, lid subcomplex / poly(A)+ mRNA export from nucleus / proteasome storage granule / transcription-coupled nucleotide-excision repair / proteasome assembly / mRNA export from nucleus / protein folding chaperone / protein export from nucleus / proteasome complex / transcription elongation by RNA polymerase II / double-strand break repair via homologous recombination / ribosomal small subunit biogenesis / mitotic cell cycle / nuclear envelope / ubiquitin-dependent protein catabolic process / double-stranded DNA binding / proteasome-mediated ubiquitin-dependent protein catabolic process / molecular adaptor activity / regulation of cell cycle / protein-containing complex binding / positive regulation of transcription by RNA polymerase II / RNA binding / nucleus / cytosol / cytoplasm
Similarity search - Function
Single alpha-helices involved in coiled-coils or other helix-helix interfaces - #1210 / Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat - #990 / Csn12 family / Nuclear mRNA export protein Sac3 / SAC3 helical domain / Leucine permease transcriptional regulator helical domain / SAC3/GANP/THP3 / SAC3/GANP/THP3, conserved domain / SAC3/GANP family / DSS1/SEM1 ...Single alpha-helices involved in coiled-coils or other helix-helix interfaces - #1210 / Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat - #990 / Csn12 family / Nuclear mRNA export protein Sac3 / SAC3 helical domain / Leucine permease transcriptional regulator helical domain / SAC3/GANP/THP3 / SAC3/GANP/THP3, conserved domain / SAC3/GANP family / DSS1/SEM1 / DSS1/SEM1 family / DSS1_SEM1 / PCI/PINT associated module / PCI domain / Proteasome component (PCI) domain / PCI domain profile. / Single alpha-helices involved in coiled-coils or other helix-helix interfaces / Helix non-globular / Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat / Special / Alpha Horseshoe / Mainly Alpha
Similarity search - Domain/homology
26S proteasome complex subunit SEM1 / Nuclear mRNA export protein SAC3 / Nuclear mRNA export protein THP1
Similarity search - Component
Biological speciesSaccharomyces cerevisiae (brewer's yeast)
MethodX-RAY DIFFRACTION / SYNCHROTRON / SAD / Resolution: 2.9 Å
AuthorsStewart, M. / Ellisdon, A.M.
CitationJournal: Nat.Struct.Mol.Biol. / Year: 2012
Title: Structural basis for the assembly and nucleic acid binding of the TREX-2 transcription-export complex.
Authors: Ellisdon, A.M. / Dimitrova, L. / Hurt, E. / Stewart, M.
History
DepositionJul 28, 2011Deposition site: RCSB / Processing site: RCSB
Revision 1.0Feb 22, 2012Provider: repository / Type: Initial release
Revision 1.1Mar 21, 2012Group: Database references
Revision 1.2Feb 28, 2024Group: Data collection / Database references
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / struct_ref_seq_dif
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_ref_seq_dif.details

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Nuclear mRNA export protein SAC3
B: Nuclear mRNA export protein THP1
C: 26S proteasome complex subunit SEM1
D: Nuclear mRNA export protein SAC3
E: Nuclear mRNA export protein THP1
F: 26S proteasome complex subunit SEM1


Theoretical massNumber of molelcules
Total (without water)200,1536
Polymers200,1536
Non-polymers00
Water0
1
A: Nuclear mRNA export protein SAC3
B: Nuclear mRNA export protein THP1
C: 26S proteasome complex subunit SEM1


Theoretical massNumber of molelcules
Total (without water)100,0763
Polymers100,0763
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area10380 Å2
ΔGint-44 kcal/mol
Surface area35590 Å2
MethodPISA
2
D: Nuclear mRNA export protein SAC3
E: Nuclear mRNA export protein THP1
F: 26S proteasome complex subunit SEM1


Theoretical massNumber of molelcules
Total (without water)100,0763
Polymers100,0763
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area9270 Å2
ΔGint-42 kcal/mol
Surface area35240 Å2
MethodPISA
Unit cell
Length a, b, c (Å)164.770, 164.770, 276.790
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number91
Space group name H-MP4122

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Components

#1: Protein Nuclear mRNA export protein SAC3 / Leucine permease transcriptional regulator


Mass: 36944.461 Da / Num. of mol.: 2 / Fragment: M region, UNP 250-563
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Saccharomyces cerevisiae (brewer's yeast)
Gene: LEP1, SAC3, YD8358.13, YDR159W / Production host: Escherichia coli (E. coli) / References: UniProt: P46674
#2: Protein Nuclear mRNA export protein THP1 / Bud site selection protein 29


Mass: 52734.820 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Saccharomyces cerevisiae (brewer's yeast)
Gene: BUD29, O1140, THP1, YOL072W / Production host: Escherichia coli (E. coli) / References: UniProt: Q08231
#3: Protein 26S proteasome complex subunit SEM1 / Proteasome


Mass: 10397.102 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Saccharomyces cerevisiae (brewer's yeast)
Gene: DSH1, SEM1, YDR363W-A / Production host: Escherichia coli (E. coli) / References: UniProt: O94742

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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: 4.69 Å3/Da / Density % sol: 73.79 %
Crystal growTemperature: 292 K / Method: vapor diffusion, hanging drop / pH: 5.2
Details: see publication, pH 5.2, VAPOR DIFFUSION, HANGING DROP, temperature 292K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: Diamond / Beamline: I02 / Wavelength: 0.9795 Å
DetectorType: ADSC QUANTUM 315r / Detector: CCD / Date: Feb 13, 2011
RadiationMonochromator: Si 111 / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9795 Å / Relative weight: 1
ReflectionResolution: 2.9→20 Å / Num. all: 84626 / Num. obs: 84626 / % possible obs: 99.7 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 7 % / Rmerge(I) obs: 0.164 / Net I/σ(I): 7.4
Reflection shellResolution: 2.9→3.06 Å / Redundancy: 7 % / Mean I/σ(I) obs: 1.9 / % possible all: 100

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Processing

Software
NameVersionClassification
ADSCQuantumdata collection
SHARPphasing
REFMAC5.6.0116refinement
MOSFLMdata reduction
SCALAdata scaling
RefinementMethod to determine structure: SAD / Resolution: 2.9→20 Å / Cor.coef. Fo:Fc: 0.948 / Cor.coef. Fo:Fc free: 0.938 / SU B: 28.693 / SU ML: 0.235 / Cross valid method: THROUGHOUT / ESU R: 0.425 / ESU R Free: 0.276 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.23089 4224 5 %RANDOM
Rwork0.20836 ---
obs0.2095 80336 99.59 %-
all-84626 --
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso mean: 38.991 Å2
Baniso -1Baniso -2Baniso -3
1--0.09 Å20 Å20 Å2
2---0.09 Å20 Å2
3---0.18 Å2
Refinement stepCycle: LAST / Resolution: 2.9→20 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms13175 0 0 0 13175
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0110.01913475
X-RAY DIFFRACTIONr_bond_other_d0.0040.029186
X-RAY DIFFRACTIONr_angle_refined_deg0.9081.95618265
X-RAY DIFFRACTIONr_angle_other_deg3.191322395
X-RAY DIFFRACTIONr_dihedral_angle_1_deg3.92851589
X-RAY DIFFRACTIONr_dihedral_angle_2_deg39.15724.419688
X-RAY DIFFRACTIONr_dihedral_angle_3_deg17.632152414
X-RAY DIFFRACTIONr_dihedral_angle_4_deg17.721584
X-RAY DIFFRACTIONr_chiral_restr0.0530.22035
X-RAY DIFFRACTIONr_gen_planes_refined0.0050.02114757
X-RAY DIFFRACTIONr_gen_planes_other0.0030.022743
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: 2.9→2.974 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.366 258 -
Rwork0.332 5363 -
obs--100 %
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)
11.7-0.28210.6191.89691.19012.5510.0890.02230.10380.03930.18830.32370.208-0.1052-0.27730.2737-0.0178-0.09210.17280.03510.4185-5.8656-18.7565-33.8552
20.255-0.00680.3680.6919-0.01191.14670.0079-0.11210.1269-0.06210.02540.14440.33220.1034-0.03330.34820.0507-0.05280.2652-0.06160.361510.6906-30.4986-24.3798
32.45990.2173-0.39891.14370.05161.32080.0404-0.43020.27540.02330.07720.03460.13240.1273-0.11760.21390.05-0.01650.4493-0.17670.284520.067-17.2021-2.9021
41.29341.4283-0.55723.1299-0.74260.8015-0.0194-0.06980.2303-0.3070.1861-0.1181-0.16940.2504-0.16670.2479-0.02510.01780.3133-0.07320.43529.4603-14.1736-27.4837
50.92970.0398-0.57481.4991-0.23693.4397-0.2086-0.0085-0.12360.00080.05050.26370.1889-0.63260.15810.4903-0.14910.07170.248-0.03560.2286-13.2115-69.2596-32.6852
62.06681.2842-0.38580.92870.20771.8328-0.1243-0.1757-0.05380.104-0.0695-0.04390.66640.03720.19380.72630.14380.02350.10680.0040.205812.7837-60.0564-18.0285
71.2090.2885-0.12510.79870.07560.2199-0.0726-0.28770.0074-0.08520.0337-0.12690.2460.23310.03890.3960.2272-0.02030.4261-0.03480.256332.4917-36.4039-15.1355
84.981911.8738-6.771529.7783-16.57779.33460.5368-0.1214-0.37430.573-1.0284-0.8102-0.53150.39180.49160.86160.1648-0.06210.5477-0.00270.41098.5882-58.7051-4.5997
95.23350.79485.19343.08212.5076.17250.0516-0.0105-0.17850.2384-0.40510.91980.3481-0.16950.35350.96010.19070.15760.1944-0.05130.336610.4149-58.3395-31.3969
100.96221.34483.42112.03515.042812.63060.2684-0.44130.0633-0.0092-0.62030.08490.2909-1.51990.35191.04920.01350.01610.57780.32680.582228.225-62.9919-9.6435
110.0099-0.0542-0.06060.37510.42920.4991-0.00090.0080.0366-0.0574-0.0075-0.0259-0.02760.03120.00850.32710.1143-0.02480.65490.10770.573941.5963-49.8573-12.8225
122.94755.6733-2.594924.31950.8264.8962-0.0068-0.376-0.04330.74710.3423-0.52160.28840.9536-0.33550.13220.20510.00970.6056-0.11270.446949.5966-32.7476-16.6401
131.0455-0.1732-1.04653.0651-1.7422.2788-0.14240.03580.05780.00160.0802-0.17450.0507-0.11140.06230.62020.00220.0130.0699-0.02410.2182-0.8264-103.8509-75.2073
143.74970.1573-0.44370.51110.83621.9427-0.27380.19510.2421-0.00410.1547-0.1186-0.08250.29950.11910.6025-0.0039-0.04260.06880.04160.3633-0.7188-103.3405-59.0316
150.66760.0670.16441.2945-0.38370.3525-0.223-0.0116-0.22550.0690.0145-0.1608-0.1702-0.01270.20850.4780.06290.08870.12610.0370.3856-1.0772-124.9607-50.9712
162.1049-0.3061.61180.9323-0.39482.347-0.13410.1063-0.1028-0.1759-0.0373-0.16620.0218-0.09180.17140.51090.00950.0960.1029-0.00580.2596-2.6943-120.3662-64.8028
171.46990.64410.24221.5432-0.10231.42010.10240.0245-0.0561-0.075-0.1315-0.1309-0.02870.26480.02910.4811-0.0852-0.03140.16670.03540.246914.2736-67.9927-47.4399
181.61760.3797-0.02232.8435-0.17220.3545-0.018-0.11870.09740.0598-0.1108-0.39270.14690.22940.12880.62940.0556-0.19430.16540.06060.307813.6135-92.3587-33.4476
190.50320.7014-0.10361.1168-0.13570.7504-0.0165-0.1607-0.10850.1751-0.1219-0.0478-0.1527-0.0550.13840.57170.14240.00670.18780.05760.2335-8.1736-117.1453-31.5247
2015.06250.6907-0.60970.0449-0.01940.1486-0.3667-0.4413-0.3763-0.07640.04850.0038-0.1953-0.04830.31831.01640.1119-0.36620.5526-0.08180.771318.7081-103.081-29.1496
216.553211.51823.698824.427815.190520.76070.0513-0.08720.5183-0.5509-0.37170.6675-0.9788-0.57320.32040.65430.02970.03110.0159-0.00550.55492.27-86.391-31.0738
223.7654-1.0975-0.29860.33260.08360.03580.1102-0.2650.74-0.0442-0.0014-0.2284-0.06410.0423-0.10881.1446-0.1027-0.14250.47170.08950.5875.8519-102.0765-15.3419
230.0264-0.17640.04641.6663-0.48840.16130.04560.01460.0020.1344-0.1917-0.1977-0.05350.03540.14610.5123-0.028-0.01750.4846-0.03370.4539-8.2492-116.3786-17.3177
245.77332.21-1.454514.83059.0727.0162-0.0895-0.2173-0.14891.0975-0.07660.23760.68980.08660.1660.5580.07570.10280.30590.04320.1452-22.008-131.0268-26.5412
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A253 - 329
2X-RAY DIFFRACTION2A330 - 458
3X-RAY DIFFRACTION3A459 - 520
4X-RAY DIFFRACTION4A521 - 551
5X-RAY DIFFRACTION5B2 - 167
6X-RAY DIFFRACTION6B168 - 303
7X-RAY DIFFRACTION7B304 - 449
8X-RAY DIFFRACTION8B450 - 455
9X-RAY DIFFRACTION9C23 - 42
10X-RAY DIFFRACTION10C53 - 63
11X-RAY DIFFRACTION11C64 - 71
12X-RAY DIFFRACTION12C72 - 89
13X-RAY DIFFRACTION13D253 - 326
14X-RAY DIFFRACTION14D327 - 385
15X-RAY DIFFRACTION15D386 - 513
16X-RAY DIFFRACTION16D514 - 550
17X-RAY DIFFRACTION17E2 - 149
18X-RAY DIFFRACTION18E150 - 262
19X-RAY DIFFRACTION19E263 - 448
20X-RAY DIFFRACTION20E449 - 455
21X-RAY DIFFRACTION21F30 - 40
22X-RAY DIFFRACTION22F53 - 60
23X-RAY DIFFRACTION23F61 - 71
24X-RAY DIFFRACTION24F72 - 89

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