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- PDB-4c46: ANDREI-N-LVPAS fused to GCN4 adaptors -

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Basic information

Entry
Database: PDB / ID: 4c46
TitleANDREI-N-LVPAS fused to GCN4 adaptors
ComponentsGENERAL CONTROL PROTEIN GCN4, GENERAL CONTROL PROTEIN GCN4
KeywordsTRANSCRIPTION / ION COORDINATION / POLAR CORE RESIDUES / FUSION PROTEIN / CHIMERA / COILED COIL / PROLINE
Function / homology
Function and homology information


protein localization to nuclear periphery / Activation of the AP-1 family of transcription factors / response to amino acid starvation / mediator complex binding / negative regulation of ribosomal protein gene transcription by RNA polymerase II / positive regulation of cellular response to amino acid starvation / nitrogen catabolite activation of transcription from RNA polymerase II promoter / TFIID-class transcription factor complex binding / amino acid biosynthetic process / positive regulation of transcription initiation by RNA polymerase II ...protein localization to nuclear periphery / Activation of the AP-1 family of transcription factors / response to amino acid starvation / mediator complex binding / negative regulation of ribosomal protein gene transcription by RNA polymerase II / positive regulation of cellular response to amino acid starvation / nitrogen catabolite activation of transcription from RNA polymerase II promoter / TFIID-class transcription factor complex binding / amino acid biosynthetic process / positive regulation of transcription initiation by RNA polymerase II / positive regulation of RNA polymerase II transcription preinitiation complex assembly / cellular response to amino acid starvation / RNA polymerase II transcription regulator complex / : / DNA-binding transcription activator activity, RNA polymerase II-specific / transcription regulator complex / RNA polymerase II-specific DNA-binding transcription factor binding / sequence-specific DNA binding / DNA-binding transcription factor activity, RNA polymerase II-specific / intracellular signal transduction / RNA polymerase II cis-regulatory region sequence-specific DNA binding / DNA-binding transcription factor activity / chromatin binding / negative regulation of transcription by RNA polymerase II / positive regulation of transcription by RNA polymerase II / identical protein binding / nucleus
Similarity search - Function
Basic region leucine zipper / Single alpha-helices involved in coiled-coils or other helix-helix interfaces - #170 / Basic-leucine zipper (bZIP) domain signature. / Basic-leucine zipper (bZIP) domain profile. / basic region leucin zipper / Basic-leucine zipper domain superfamily / Basic-leucine zipper domain / Single alpha-helices involved in coiled-coils or other helix-helix interfaces / Up-down Bundle / Mainly Alpha
Similarity search - Domain/homology
BROMIDE ION / General control transcription factor GCN4
Similarity search - Component
Biological speciesSACCHAROMYCES CEREVISIAE (brewer's yeast)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.95 Å
AuthorsAlbrecht, R. / Alva, V. / Ammelburg, M. / Baer, K. / Basina, E. / Boichenko, I. / Bonhoeffer, F. / Braun, V. / Chaubey, M. / Chauhan, N. ...Albrecht, R. / Alva, V. / Ammelburg, M. / Baer, K. / Basina, E. / Boichenko, I. / Bonhoeffer, F. / Braun, V. / Chaubey, M. / Chauhan, N. / Chellamuthu, V.R. / Coles, M. / Deiss, S. / Ewers, C.P. / Forouzan, D. / Fuchs, A. / Groemping, Y. / Hartmann, M.D. / Hernandez Alvarez, B. / Jeganantham, A. / Kalev, I. / Koenninger, U. / Koiwai, K. / Kopec, K.O. / Korycinski, M. / Laudenbach, B. / Lehmann, K. / Leo, J.C. / Linke, D. / Marialke, J. / Martin, J. / Mechelke, M. / Michalik, M. / Noll, A. / Patzer, S.I. / Scharfenberg, F. / Schueckel, M. / Shahid, S.A. / Sulz, E. / Ursinus, A. / Wuertenberger, S. / Zhu, H.
CitationJournal: J.Struct.Biol. / Year: 2014
Title: Your Personalized Protein Structure: Andrei N. Lupas Fused to GCN4 Adaptors.
Authors: Deiss, S. / Hernandez Alvarez, B. / Bar, K. / Ewers, C.P. / Coles, M. / Albrecht, R. / Hartmann, M.D.
History
DepositionAug 30, 2013Deposition site: PDBE / Processing site: PDBE
Revision 1.0Sep 11, 2013Provider: repository / Type: Initial release
Revision 1.1Jan 29, 2014Group: Database references / Structure summary
Revision 1.2Mar 19, 2014Group: Database references
Revision 1.3Jun 11, 2014Group: Database references
Revision 1.4May 8, 2019Group: Data collection / Experimental preparation / Other
Category: exptl_crystal_grow / pdbx_database_proc / pdbx_database_status
Item: _exptl_crystal_grow.method / _pdbx_database_status.recvd_author_approval
Revision 1.5Dec 20, 2023Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Other / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_database_status / pdbx_initial_refinement_model / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.status_code_sf / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: GENERAL CONTROL PROTEIN GCN4, GENERAL CONTROL PROTEIN GCN4
B: GENERAL CONTROL PROTEIN GCN4, GENERAL CONTROL PROTEIN GCN4
C: GENERAL CONTROL PROTEIN GCN4, GENERAL CONTROL PROTEIN GCN4
hetero molecules


Theoretical massNumber of molelcules
Total (without water)26,6884
Polymers26,6083
Non-polymers801
Water1,31573
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area7790 Å2
ΔGint-95 kcal/mol
Surface area13500 Å2
MethodPISA
Unit cell
Length a, b, c (Å)42.000, 41.600, 64.140
Angle α, β, γ (deg.)90.00, 95.48, 90.00
Int Tables number4
Space group name H-MP1211

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Components

#1: Protein GENERAL CONTROL PROTEIN GCN4, GENERAL CONTROL PROTEIN GCN4 / AMINO ACID BIOSYNTHESIS REGULATORY PROTEIN


Mass: 8869.462 Da / Num. of mol.: 3 / Fragment: RESIDUES 250-278,250-278 / Mutation: YES
Source method: isolated from a genetically manipulated source
Details: ANDREI-N-LVPAS FUSED TO GCN4 ADAPTORS
Source: (gene. exp.) SACCHAROMYCES CEREVISIAE (brewer's yeast)
Production host: ESCHERICHIA COLI (E. coli) / References: UniProt: P03069
#2: Chemical ChemComp-BR / BROMIDE ION / Bromide


Mass: 79.904 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Br
#3: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 73 / Source method: isolated from a natural source / Formula: H2O

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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: 2.2 Å3/Da / Density % sol: 43.5 % / Description: NONE
Crystal growMethod: vapor diffusion, sitting drop / pH: 4
Details: SITTING DROP, PROTEIN SOLUTION 50 MM NACL AND 50 MM SODIUM ACETATE PH 4.0, RESERVOUR SOLUTION 0.1 M HEPES PH 7.5 1.75 M SODIUM BROMIDE

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SLS / Beamline: X10SA / Wavelength: 1
DetectorType: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Aug 25, 2013
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 1.95→36.6 Å / Num. obs: 16104 / % possible obs: 98.7 % / Observed criterion σ(I): -3 / Redundancy: 3.28 % / Rmerge(I) obs: 0.06 / Net I/σ(I): 11.3
Reflection shellResolution: 1.95→2.07 Å / Redundancy: 3.33 % / Rmerge(I) obs: 0.58 / Mean I/σ(I) obs: 1.94 / % possible all: 97.5

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Processing

Software
NameVersionClassification
REFMAC5.7.0029refinement
XDSdata reduction
XDSdata scaling
MOLREPphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 1GCM
Resolution: 1.95→36.64 Å / Cor.coef. Fo:Fc: 0.954 / Cor.coef. Fo:Fc free: 0.945 / SU B: 12.125 / SU ML: 0.167 / Cross valid method: THROUGHOUT / ESU R: 0.227 / ESU R Free: 0.19 / Stereochemistry target values: MAXIMUM LIKELIHOOD
Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. U VALUES WITH TLS ADDED.
RfactorNum. reflection% reflectionSelection details
Rfree0.27543 803 5 %RANDOM
Rwork0.2376 ---
obs0.23962 15294 98.59 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso mean: 42.801 Å2
Baniso -1Baniso -2Baniso -3
1--2.75 Å20 Å23.68 Å2
2--1.46 Å20 Å2
3---0.92 Å2
Refinement stepCycle: LAST / Resolution: 1.95→36.64 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms1745 0 1 73 1819
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0160.0191777
X-RAY DIFFRACTIONr_bond_other_d0.0010.021838
X-RAY DIFFRACTIONr_angle_refined_deg1.7171.9792392
X-RAY DIFFRACTIONr_angle_other_deg0.85434238
X-RAY DIFFRACTIONr_dihedral_angle_1_deg5.1535218
X-RAY DIFFRACTIONr_dihedral_angle_2_deg35.0226.81269
X-RAY DIFFRACTIONr_dihedral_angle_3_deg18.32915381
X-RAY DIFFRACTIONr_dihedral_angle_4_deg6.733153
X-RAY DIFFRACTIONr_chiral_restr0.1060.2288
X-RAY DIFFRACTIONr_gen_planes_refined0.0070.021907
X-RAY DIFFRACTIONr_gen_planes_other0.0010.02332
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_mcangle_other
X-RAY DIFFRACTIONr_scbond_it
X-RAY DIFFRACTIONr_scbond_other
X-RAY DIFFRACTIONr_scangle_it
X-RAY DIFFRACTIONr_scangle_other
X-RAY DIFFRACTIONr_long_range_B_refined
X-RAY DIFFRACTIONr_long_range_B_other
X-RAY DIFFRACTIONr_rigid_bond_restr
X-RAY DIFFRACTIONr_sphericity_free
X-RAY DIFFRACTIONr_sphericity_bonded
LS refinement shellResolution: 1.95→2 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.448 46 -
Rwork0.345 1091 -
obs--94.75 %
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)
123.3684-4.4279-9.3785.89710.510714.31730.01020.27740.5287-0.00640.11190.54710.1354-0.6153-0.12210.19560.0174-0.06390.03580.00830.1242-2.21184.143218.3069
223.42126.4701-16.70919.6915-0.953520.38670.4559-1.55110.64070.7833-0.11840.31570.17580.471-0.33750.2722-0.0252-0.10770.3178-0.01310.11654.08451.604827.7594
326.6634-1.4909-8.375.10980.98585.3415-0.33130.18-0.46480.13560.17410.54160.1803-0.47280.15720.2184-0.029-0.05140.0972-0.00240.1462-1.0814-6.499320.7721
421.59842.1599-15.70470.54550.44423.7629-0.10590.63440.1962-0.0660.07290.0563-0.2364-0.20850.0330.19280.0621-0.09440.1137-0.01130.05019.81241.06658.7398
522.26062.7782-11.493413.3088-0.54286.67880.0482-0.69130.1076-0.09180.0496-0.0653-0.22110.6122-0.09790.2016-0.0519-0.05490.132-0.03440.036415.6144.525316.7967
625.36710.3417-11.659711.8455-4.31736.9308-0.277-0.0426-0.5814-0.07590.03750.1870.29290.12670.23940.22730.1042-0.03290.12440.03940.064614.3211-5.802715.0054
724.03361.7077-14.94861.0962-1.582611.3749-0.23170.4994-0.4863-0.0976-0.06590.0078-0.0029-0.19240.29760.13920.014-0.06040.2139-0.02950.044422.2075-1.60810.652
821.92781.1477-16.13456.84815.534517.88830.6018-0.37890.9421-0.11050.2273-0.1655-0.51280.5319-0.82920.27290.00580.01040.2520.05360.124226.01625.61015.8139
926.9752-0.8946-8.08415.746-0.9358.251-0.3391-0.4019-0.7470.12260.02310.00450.56770.60270.3160.19340.0079-0.05060.19370.03490.06127.7598-4.57378.2078
1023.3736-8.1963-8.58745.63353.12073.1641-0.16430.8375-0.92970.0064-0.1452-0.00860.0919-0.31680.30950.3207-0.0165-0.09560.3694-0.07920.159835.1619-4.2362-7.9475
1114.12262.5236-7.7410.4566-1.38414.24330.79440.92441.14550.1588-0.02350.1993-0.5191-0.4983-0.77090.56190.08630.13090.48190.07850.253537.18785.5726-5.8698
1234.78916.8367-9.78811.3502-1.87523.89760.0978-0.5856-0.79440.041-0.1501-0.1834-0.26990.43730.05230.3078-0.0686-0.10450.45880.06460.147341.3042-1.4895-0.237
1323.71733.2748-11.04219.7861-1.362912.66020.0676-0.6266-0.40610.3794-0.27890.56090.0681-0.30770.21140.16190.0057-0.06640.0752-0.020.105749.4014-6.3615-15.1378
1424.315-5.4707-2.44612.4251-1.18462.77020.0124-0.14120.10440.0370.23630.1466-0.0772-0.3072-0.24870.28270.04430.01240.097-0.00770.162548.34314.5683-17.3637
159.63463.2379-12.59754.75471.400625.3681-0.0585-0.5746-0.1920.2255-0.26630.01930.41220.33930.32480.22810.0255-0.07250.41460.08430.071954.91471.0923-9.3239
1629.26143.0652-12.17635.9053-4.72587.7603-0.5590.3498-0.8932-0.16310.09220.15770.6326-0.45230.46680.3031-0.1490.08690.1463-0.14560.197463.2744-6.2303-22.2333
1724.646-0.4182-13.74212.26024.714716.57740.6360.88741.4037-0.1303-0.17890.1444-0.6082-0.8097-0.45710.27310.0734-0.04220.11750.0470.117959.63782.1486-27.5833
1825.69055.8987-24.60373.5072-3.715925.44410.0991-1.27870.1950.3660.1198-0.11450.14961.5262-0.21890.25090.0055-0.09450.2168-0.0780.093666.04013.7999-19.1707
1922.7629-1.7224-8.27343.2615-1.692911.033-0.3169-0.0752-0.7364-0.0865-0.0743-0.80140.51010.59650.39120.24230.0167-0.03960.23170.0460.332777.8144-4.8103-28.4041
2023.255-0.6471-11.9119.69910.517913.36030.0250.8121-0.4706-0.2948-0.2017-0.2468-0.03470.04940.17670.19440.0058-0.05740.1953-0.03720.043271.912-1.5664-36.5471
2110.72810.2994-11.36312.3265-1.688918.0840.4767-0.21670.8497-0.1147-0.0153-0.5249-0.26360.8111-0.46140.2637-0.0673-0.0190.16590.00810.160275.89285.6538-30.4363
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A0 - 10
2X-RAY DIFFRACTION2B-1 - 10
3X-RAY DIFFRACTION3C-2 - 10
4X-RAY DIFFRACTION4A11 - 20
5X-RAY DIFFRACTION5B11 - 20
6X-RAY DIFFRACTION6C11 - 20
7X-RAY DIFFRACTION7A21 - 30
8X-RAY DIFFRACTION8B21 - 30
9X-RAY DIFFRACTION9C21 - 30
10X-RAY DIFFRACTION10A31 - 40
11X-RAY DIFFRACTION11B31 - 40
12X-RAY DIFFRACTION12C31 - 40
13X-RAY DIFFRACTION13A41 - 50
14X-RAY DIFFRACTION14B41 - 50
15X-RAY DIFFRACTION15C41 - 50
16X-RAY DIFFRACTION16A51 - 60
17X-RAY DIFFRACTION17B51 - 60
18X-RAY DIFFRACTION18C51 - 60
19X-RAY DIFFRACTION19A61 - 71
20X-RAY DIFFRACTION20B61 - 71
21X-RAY DIFFRACTION21C61 - 71

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