[English] 日本語
Yorodumi
- PDB-2ful: Crystal Structure of the C-terminal Domain of S. cerevisiae eIF5 -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 2ful
TitleCrystal Structure of the C-terminal Domain of S. cerevisiae eIF5
ComponentsEukaryotic translation initiation factor 5
KeywordsTRANSLATION / atypical HEAT motif
Function / homology
Function and homology information


eukaryotic initiation factor eIF2 binding / multi-eIF complex / formation of cytoplasmic translation initiation complex / formation of translation preinitiation complex / eukaryotic 48S preinitiation complex / GDP-dissociation inhibitor activity / regulation of translational initiation / Ribosomal scanning and start codon recognition / translation initiation factor binding / negative regulation of translational initiation ...eukaryotic initiation factor eIF2 binding / multi-eIF complex / formation of cytoplasmic translation initiation complex / formation of translation preinitiation complex / eukaryotic 48S preinitiation complex / GDP-dissociation inhibitor activity / regulation of translational initiation / Ribosomal scanning and start codon recognition / translation initiation factor binding / negative regulation of translational initiation / translation initiation factor activity / GTPase activator activity / cytosolic ribosome assembly / GTP binding / cytosol
Similarity search - Function
Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat - #180 / Translation initiation factor IF2/IF5 / Translation initiation factor IF2/IF5 domain / Translation initiation factor IF2/IF5, N-terminal / Translation initiation factor IF2/IF5, zinc-binding / Domain found in IF2B/IF5 / domain present in translation initiation factor eIF2B and eIF5 / eIF4-gamma/eIF5/eIF2-epsilon / Domain at the C-termini of GCD6, eIF-2B epsilon, eIF-4 gamma and eIF-5 / W2 domain ...Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat - #180 / Translation initiation factor IF2/IF5 / Translation initiation factor IF2/IF5 domain / Translation initiation factor IF2/IF5, N-terminal / Translation initiation factor IF2/IF5, zinc-binding / Domain found in IF2B/IF5 / domain present in translation initiation factor eIF2B and eIF5 / eIF4-gamma/eIF5/eIF2-epsilon / Domain at the C-termini of GCD6, eIF-2B epsilon, eIF-4 gamma and eIF-5 / W2 domain / W2 domain profile. / Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat / Alpha Horseshoe / Armadillo-type fold / Mainly Alpha
Similarity search - Domain/homology
Eukaryotic translation initiation factor 5
Similarity search - Component
Biological speciesSaccharomyces cerevisiae (brewer's yeast)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.5 Å
AuthorsWei, Z. / Xue, Y. / Xu, H. / Gong, W.
CitationJournal: J.Mol.Biol. / Year: 2006
Title: Crystal Structure of the C-terminal Domain of S.cerevisiae eIF5
Authors: Wei, Z. / Xue, Y. / Xu, H. / Gong, W.
History
DepositionJan 27, 2006Deposition site: RCSB / Processing site: PDBJ
Revision 1.0May 23, 2006Provider: repository / Type: Initial release
Revision 1.1May 1, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Advisory / Version format compliance
Revision 1.3Oct 18, 2017Group: Refinement description / Category: software
Item: _software.classification / _software.contact_author ..._software.classification / _software.contact_author / _software.contact_author_email / _software.date / _software.language / _software.location / _software.name / _software.type / _software.version
Revision 1.4Mar 13, 2024Group: Data collection / Database references / Derived calculations
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / struct_ref_seq_dif / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_ref_seq_dif.details / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: Eukaryotic translation initiation factor 5
B: Eukaryotic translation initiation factor 5
C: Eukaryotic translation initiation factor 5
D: Eukaryotic translation initiation factor 5
E: Eukaryotic translation initiation factor 5
F: Eukaryotic translation initiation factor 5
hetero molecules


Theoretical massNumber of molelcules
Total (without water)124,39926
Polymers122,4776
Non-polymers1,92120
Water16,502916
1
A: Eukaryotic translation initiation factor 5
hetero molecules


Theoretical massNumber of molelcules
Total (without water)20,7014
Polymers20,4131
Non-polymers2883
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
B: Eukaryotic translation initiation factor 5
hetero molecules


Theoretical massNumber of molelcules
Total (without water)20,6053
Polymers20,4131
Non-polymers1922
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
3
C: Eukaryotic translation initiation factor 5
hetero molecules


Theoretical massNumber of molelcules
Total (without water)20,6053
Polymers20,4131
Non-polymers1922
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
4
D: Eukaryotic translation initiation factor 5
hetero molecules


Theoretical massNumber of molelcules
Total (without water)20,8936
Polymers20,4131
Non-polymers4805
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
5
E: Eukaryotic translation initiation factor 5
hetero molecules


Theoretical massNumber of molelcules
Total (without water)20,7975
Polymers20,4131
Non-polymers3844
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
6
F: Eukaryotic translation initiation factor 5
hetero molecules


Theoretical massNumber of molelcules
Total (without water)20,7975
Polymers20,4131
Non-polymers3844
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)44.849, 64.536, 108.916
Angle α, β, γ (deg.)88.60, 86.57, 74.93
Int Tables number1
Space group name H-MP1

-
Components

#1: Protein
Eukaryotic translation initiation factor 5 / eIF-5


Mass: 20412.895 Da / Num. of mol.: 6 / Fragment: residues 236-412
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Saccharomyces cerevisiae (brewer's yeast)
Plasmid: pGEX4T-1 / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) / References: UniProt: P38431
#2: Chemical
ChemComp-SO4 / SULFATE ION / Sulfate


Mass: 96.063 Da / Num. of mol.: 20 / Source method: obtained synthetically / Formula: SO4
#3: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 916 / Source method: isolated from a natural source / Formula: H2O

-
Experimental details

-
Experiment

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

-
Sample preparation

CrystalDensity Matthews: 2.48 Å3/Da / Density % sol: 50.4 %
Crystal growTemperature: 277 K / Method: vapor diffusion, hanging drop / pH: 6.4
Details: 2.8M (NH4)2SO4, 0.1M MES pH6.4, VAPOR DIFFUSION, HANGING DROP, temperature 277K

-
Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 22-ID / Wavelength: 0.9794 Å
DetectorType: MARRESEARCH / Detector: CCD / Date: Nov 12, 2005
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9794 Å / Relative weight: 1
ReflectionRedundancy: 4 % / Av σ(I) over netI: 23.4 / Number: 261803 / Rmerge(I) obs: 0.061 / Χ2: 2.56 / D res high: 2.1 Å / D res low: 50 Å / Num. obs: 65439 / % possible obs: 94.7
Diffraction reflection shell

ID: 1

Highest resolution (Å)Lowest resolution (Å)Num. obs% possible obs (%)Rmerge(I) obsChi squaredRedundancy
4.5250669396.80.0656.3463.9
3.594.52659595.50.0472.6473.9
3.143.59666496.40.0512.4154
2.853.14660495.90.062.2834
2.652.85660795.60.0692.3674
2.492.65653894.50.0762.4114
2.372.49650094.30.0862.1174
2.262.37645393.10.1011.874
2.182.266421930.1131.6484
2.12.186364920.1291.4584
ReflectionResolution: 1.5→50 Å / Num. obs: 173580 / % possible obs: 92.8 % / Redundancy: 3.5 % / Rmerge(I) obs: 0.044 / Χ2: 1.045 / Net I/σ(I): 25
Reflection shell
Resolution (Å)% possible obs (%)Redundancy (%)Rmerge(I) obsNum. unique obsΧ2Diffraction-ID
1.5-1.5568.92.50.245128951.0641
1.55-1.6289.12.90.205166521.0021
1.62-1.6992.93.10.175173390.991
1.69-1.7894.13.30.141176540.9851
1.78-1.8995.13.50.112177981.0351
1.89-2.0496.13.60.08179671.1321
2.04-2.2497.13.70.054182041.0741
2.24-2.5697.83.80.042182381.0471
2.56-3.2398.53.90.035184851.0841
3.23-5098.13.80.034183481.0071

-
Processing

Software
NameVersionClassificationNB
DENZOdata reduction
SCALEPACKdata scaling
REFMAC5.2.0005refinement
PDB_EXTRACT1.701data extraction
HKL-2000data reduction
SHARPphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 1.5→50 Å / Cor.coef. Fo:Fc: 0.966 / Cor.coef. Fo:Fc free: 0.952 / SU B: 2.475 / SU ML: 0.047 / TLS residual ADP flag: LIKELY RESIDUAL / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.074 / ESU R Free: 0.076 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.205 8647 5 %RANDOM
Rwork0.177 ---
all0.178 ---
obs-173578 92.35 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso mean: 18.323 Å2
Baniso -1Baniso -2Baniso -3
1-0.05 Å20.03 Å20.13 Å2
2---0.15 Å20.16 Å2
3---0.07 Å2
Refinement stepCycle: LAST / Resolution: 1.5→50 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms7829 0 100 916 8845
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.010.0228419
X-RAY DIFFRACTIONr_angle_refined_deg1.2041.99511459
X-RAY DIFFRACTIONr_dihedral_angle_1_deg4.91551062
X-RAY DIFFRACTIONr_dihedral_angle_2_deg35.62126.105421
X-RAY DIFFRACTIONr_dihedral_angle_3_deg12.628151608
X-RAY DIFFRACTIONr_dihedral_angle_4_deg24.491531
X-RAY DIFFRACTIONr_chiral_restr0.0840.21271
X-RAY DIFFRACTIONr_gen_planes_refined0.0050.026293
X-RAY DIFFRACTIONr_nbd_refined0.2050.24229
X-RAY DIFFRACTIONr_nbtor_refined0.3110.25884
X-RAY DIFFRACTIONr_xyhbond_nbd_refined0.1250.2745
X-RAY DIFFRACTIONr_symmetry_vdw_refined0.1480.2150
X-RAY DIFFRACTIONr_symmetry_hbond_refined0.1160.247
X-RAY DIFFRACTIONr_mcbond_it0.631.55131
X-RAY DIFFRACTIONr_mcangle_it1.00928171
X-RAY DIFFRACTIONr_scbond_it1.72433629
X-RAY DIFFRACTIONr_scangle_it2.6074.53235
LS refinement shellResolution: 1.502→1.541 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.305 400 -
Rwork0.253 7908 -
obs-8308 59.68 %
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)
11.2375-1.77092.39914.1096-2.65865.0318-0.23090.003-0.00130.2066-0.1608-0.1509-0.37490.38680.39170.0882-0.0053-0.02980.01940.0523-0.00328.87475.633-1.67
21.6257-0.28350.25541.3144-0.00111.0527-0.04530.0886-0.0433-0.00260.0779-0.0111-0.06760.0018-0.03260.04980.0068-0.0135-0.01140.0178-0.051713.09974.552-6.49
31.05881.0630.92122.420.82431.6701-0.0171-0.0567-0.0616-0.01360.0203-0.0745-0.0123-0.0194-0.00310.05470.0083-0.0137-0.02310.014-0.000415.59671.448-6.861
41.48570.8020.39952.2999-0.09351.5717-0.0649-0.0252-0.0182-0.0450.03950.0653-0.0992-0.06610.02540.0458-0.0018-0.0158-0.01910.009-0.017610.16475.892-15.349
51.29870.16920.38253.8112-1.95181.70780.00690.0691-0.07950.02060.0211-0.09280.0272-0.0368-0.0280.04350.0017-0.0008-0.0554-0.0161-0.004812.29868.811-17.336
60.0698-0.1266-0.67863.77232.39136.97740.0947-0.07150.0366-0.09930.0543-0.20330.25780.2641-0.1490.0851-0.0001-0.0368-0.0083-0.04-0.038314.09243.6913.544
71.2223-0.5556-0.80462.52240.82912.45060.01660.08750.0468-0.129-0.0379-0.00320.0708-0.00710.02130.05210.001-0.0191-0.0403-0.0204-0.062313.92250.07924.341
81.3134-1.3090.88993.5957-0.93261.9260.00910.0708-0.02470.0196-0.0715-0.0612-0.0032-0.01410.06240.06520.0079-0.0164-0.00410.0027-0.045616.43753.21725.955
91.3915-0.79640.01912.5437-0.42752.4755-0.0131-0.0125-0.07060.1392-0.03330.1237-0.0155-0.06490.04640.0530.0028-0.0153-0.0206-0.0004-0.044711.55259.30333.504
101.1952-0.4-1.12730.7081-0.11386.81110.04540.01210.1251-0.064-0.10120.0106-0.06610.15740.05580.0394-0.0092-0.0261-0.02130.0194-0.039715.27464.92929.073
1124.922-19.28-15.471521.93814.08614.5886-0.0444-0.72850.48780.36480.2596-0.20230.1848-0.1597-0.21520.03120.01070.00520.0012-0.00830.00138.57164.8331.111
123.83762.21292.34055.70041.55113.2605-0.18630.12790.0904-0.20020.26010.0916-0.28970.1518-0.07390.06850.0185-0.0346-0.0921-0.0038-0.00349.83846.826-11.555
130.78230.35450.06471.8905-0.66160.98490.00240.00430.0252-0.05540.0176-0.0232-0.00430.0805-0.01990.0560.0119-0.0125-0.0325-0.0221-0.020314.84932.764-7.96
141.35340.81440.45745.05481.96061.90570.0081-0.0242-0.27050.0361-0.01360.19730.1404-0.05540.00550.05170.0118-0.03-0.0322-0.010.03339.54516.139-2.066
155.71872.6723-1.80273.96983.31918.04310.5334-0.51970.5972-0.076-0.19520.3643-0.9173-0.1748-0.33820.14780.04850.06210.0262-0.03940.05412.42624.6694.11
160.2723-0.8870.70782.9512-2.81225.9810.01310.02720.02180.0865-0.0616-0.0560.35020.08660.04840.110.0002-0.0333-0.00470.0587-0.042928.31729.858-44.668
172.0363-0.65021.31782.0212-1.16143.42380.0958-0.1013-0.17610.08790.0394-0.12090.12160.0184-0.13520.04370.0058-0.029-0.02570.0281-0.03327.02235.903-54.142
181.2460.7170.56952.38440.72462.31410.0902-0.1207-0.0862-0.06720.0706-0.0564-0.0932-0.0202-0.16090.0542-0.0087-0.0157-0.03570.02880.004726.02738.846-61.967
192.31590.27820.86262.4125-0.11552.89880.0432-0.0214-0.0072-0.1650.03680.0093-0.2002-0.1098-0.080.06240.0163-0.0118-0.05180.0285-0.033221.87543.318-69.801
202.0348-1.61491.43626.3038-3.26942.0765-0.0167-0.0162-0.23480.34470.0483-0.0206-0.1615-0.1538-0.03160.05580.0095-0.0252-0.06710.0138-0.027121.3636.804-69.102
212.48311.0497-1.55131.9734-0.7183.7615-0.0056-0.2254-0.51620.2003-0.2256-0.09950.35180.24280.23120.0921-0.03220.0219-0.005-0.00510.030321.3946.467-22.495
222.31650.365-0.10192.16390.0481.33980.0089-0.0398-0.1310.012-0.1140.0040.0341-0.05650.10510.031-0.0009-0.0092-0.0227-0.0129-0.041524.10215.522-25.216
231.067-0.3570.0211.7312-0.1780.96680.00110.0336-0.02720.0685-0.0811-0.0387-0.03140.00140.080.0484-0.0033-0.0204-0.00380.0135-0.036328.21822.645-23.267
240.9284-0.45931.06030.5186-0.43283.064-0.0222-0.20590.05360.05010.098-0.10360.0274-0.0618-0.07580.0408-0.0003-0.06580.0347-0.0014-0.045830.94526.317-4.896
256.7945-0.3827-0.68791.9426-3.840110.9306-0.13970.75930.27750.00860.1943-0.0754-0.016-0.2883-0.05460.0401-0.0474-0.00160.05570.0125-0.021325.22736.508-22.031
2612.7773-8.1338-4.886512.78821.476822.9663-0.0421-0.04880.8246-0.21860.2521-0.92990.291.3721-0.210.0454-0.0323-0.0481-0.02950.00570.026327.0929.039-59.138
273.26483.73972.01555.12912.24883.526-0.09730.24510.0735-0.05250.15330.0061-0.42070.4305-0.0560.1015-0.0495-0.0674-0.08750.01240.045826.70218.743-64.72
282.43890.5853-0.1491.91960.10571.3611-0.01750.0570.0626-0.0067-0.0352-0.0343-0.06050.17970.05270.0542-0.0166-0.0151-0.0315-0.0006-0.016827.93.711-66.841
291.23710.45860.15062.82361.10082.53340.01850.0946-0.0293-0.0657-0.03890.08870.1632-0.0080.02040.0745-0.01620.0028-0.0453-0.019-0.053820.691-8.679-66.793
308.31232.1127-1.058212.01085.46212.71760.23850.05740.23290.1548-0.28040.3639-0.5296-0.45050.04190.0664-0.0293-0.009-0.04270.0208-0.034518.14-14.449-57.494
Refinement TLS group

Refine-ID: X-RAY DIFFRACTION / Selection: ALL

IDRefine TLS-IDAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
11AA237 - 2582 - 23
22AA259 - 31324 - 78
33AA314 - 33479 - 99
44AA335 - 367100 - 132
55AA368 - 395133 - 160
66BB236 - 2671 - 32
77BB268 - 31133 - 76
88BB312 - 33577 - 100
99BB336 - 367101 - 132
1010BB368 - 394133 - 159
1111CC238 - 2423 - 7
1212CC243 - 2758 - 40
1313CC276 - 36241 - 127
1414CC363 - 390128 - 155
1515CC391 - 395156 - 160
1616DD238 - 2693 - 34
1717DD270 - 31335 - 78
1818DD314 - 33579 - 100
1919DD336 - 368101 - 133
2020DD369 - 394134 - 159
2121EE238 - 2733 - 38
2222EE274 - 31139 - 76
2323EE312 - 35877 - 123
2424EE359 - 386124 - 151
2525EE387 - 396152 - 161
2626FF238 - 2423 - 7
2727FF243 - 2808 - 45
2828FF281 - 32446 - 89
2929FF325 - 38590 - 150
3030FF386 - 395151 - 160

+
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