[English] 日本語
Yorodumi
- PDB-3hxe: Engineered RabGGTase in complex with a peptidomimetic inhibitor (... -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 3hxe
TitleEngineered RabGGTase in complex with a peptidomimetic inhibitor (compound 37)
Components(Geranylgeranyl transferase type-2 subunit ...) x 2
KeywordsTRANSFERASE / protein prenylation inhibition
Function / homology
Function and homology information


isoprenoid binding / TP53 regulates transcription of several additional cell death genes whose specific roles in p53-dependent apoptosis remain uncertain / protein geranylgeranyltransferase type II / RAB geranylgeranylation / Rab-protein geranylgeranyltransferase complex / Rab geranylgeranyltransferase activity / protein geranylgeranylation / small GTPase binding / zinc ion binding / cytoplasm
Similarity search - Function
Rab geranylgeranyltransferase, alpha subunit, insert-domain / Rab geranylgeranyltransferase, alpha subunit, insert-domain superfamily / Rab geranylgeranyl transferase alpha-subunit, insert domain / Geranylgeranyl transferase type-2 subunit beta / Protein prenylyltransferase / Prenyltransferase subunit beta / Protein prenyltransferase, alpha subunit / Protein prenyltransferase alpha subunit repeat / Protein prenyltransferases alpha subunit repeat profile. / PFTB repeat ...Rab geranylgeranyltransferase, alpha subunit, insert-domain / Rab geranylgeranyltransferase, alpha subunit, insert-domain superfamily / Rab geranylgeranyl transferase alpha-subunit, insert domain / Geranylgeranyl transferase type-2 subunit beta / Protein prenylyltransferase / Prenyltransferase subunit beta / Protein prenyltransferase, alpha subunit / Protein prenyltransferase alpha subunit repeat / Protein prenyltransferases alpha subunit repeat profile. / PFTB repeat / Prenyltransferase and squalene oxidase repeat / Glycosyltransferase - #20 / Terpenoid cyclases/protein prenyltransferase alpha-alpha toroid / Glycosyltransferase / Alpha/alpha barrel / Leucine-rich repeat domain superfamily / Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat / Alpha Horseshoe / Mainly Alpha
Similarity search - Domain/homology
Chem-BD8 / Geranylgeranyl transferase type-2 subunit alpha / Geranylgeranyl transferase type-2 subunit beta
Similarity search - Component
Biological speciesRattus norvegicus (Norway rat)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.95 Å
AuthorsGuo, Z. / Alexandrov, K. / Waldmann, H. / Goody, R.S. / Blankenfeldt, W.
CitationJournal: J.Med.Chem. / Year: 2009
Title: Design, synthesis, and characterization of Peptide-based rab geranylgeranyl transferase inhibitors
Authors: Tan, K.T. / Guiu-Rozas, E. / Bon, R.S. / Guo, Z. / Delon, C. / Wetzel, S. / Arndt, S. / Alexandrov, K. / Waldmann, H. / Goody, R.S. / Wu, Y.W. / Blankenfeldt, W.
History
DepositionJun 20, 2009Deposition site: RCSB / Processing site: RCSB
Revision 1.0Sep 8, 2009Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Version format compliance
Revision 1.2Feb 13, 2013Group: Refinement description
Revision 1.3Jul 26, 2017Group: Refinement description / Source and taxonomy / Category: entity_src_gen / software
Revision 1.4Feb 21, 2024Group: Data collection / Database references / Derived calculations
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_struct_conn_angle / struct_conn / 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 / _pdbx_struct_conn_angle.ptnr1_auth_comp_id / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr1_label_atom_id / _pdbx_struct_conn_angle.ptnr1_label_comp_id / _pdbx_struct_conn_angle.ptnr1_label_seq_id / _pdbx_struct_conn_angle.ptnr3_auth_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_label_atom_id / _pdbx_struct_conn_angle.ptnr3_label_comp_id / _pdbx_struct_conn_angle.ptnr3_label_seq_id / _pdbx_struct_conn_angle.value / _struct_conn.pdbx_dist_value / _struct_conn.ptnr1_auth_comp_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr1_label_comp_id / _struct_conn.ptnr1_label_seq_id / _struct_conn.ptnr2_auth_comp_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id / _struct_conn.ptnr2_label_atom_id / _struct_conn.ptnr2_label_comp_id / _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: Geranylgeranyl transferase type-2 subunit alpha
B: Geranylgeranyl transferase type-2 subunit beta
hetero molecules


Theoretical massNumber of molelcules
Total (without water)76,1915
Polymers75,3342
Non-polymers8573
Water6,269348
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area4220 Å2
ΔGint-26 kcal/mol
Surface area25290 Å2
MethodPISA
Unit cell
Length a, b, c (Å)67.122, 90.826, 114.727
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number19
Space group name H-MP212121

-
Components

-
Geranylgeranyl transferase type-2 subunit ... , 2 types, 2 molecules AB

#1: Protein Geranylgeranyl transferase type-2 subunit alpha / Geranylgeranyl transferase type II subunit alpha / Rab geranylgeranyltransferase subunit alpha / ...Geranylgeranyl transferase type II subunit alpha / Rab geranylgeranyltransferase subunit alpha / Rab geranyl-geranyltransferase subunit alpha / Rab GG transferase alpha / Rab GGTase alpha


Mass: 38441.598 Da / Num. of mol.: 1 / Fragment: RabGGTase ALPHA-subunit / Mutation: DELTA LRR; DELTA IG
Source method: isolated from a genetically manipulated source
Details: coexpression of engineered alpha-subunit from pGATEV and beta-subunit from pET3 0a
Source: (gene. exp.) Rattus norvegicus (Norway rat) / Plasmid: pGATEV / Production host: Escherichia coli (E. coli) / Strain (production host): BL21 Codon-Plus RIL (DE3)
References: UniProt: Q08602, protein geranylgeranyltransferase type II
#2: Protein Geranylgeranyl transferase type-2 subunit beta / Geranylgeranyl transferase type II subunit beta / GGTase-II-beta / Type II protein geranyl- ...Geranylgeranyl transferase type II subunit beta / GGTase-II-beta / Type II protein geranyl-geranyltransferase subunit beta / Rab geranylgeranyltransferase subunit beta / Rab geranyl-geranyltransferase subunit beta / Rab GG transferase beta / Rab GGTase beta


Mass: 36892.160 Da / Num. of mol.: 1 / Fragment: RABGGTase BETA-subunit
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Rattus norvegicus (Norway rat) / Plasmid: pET30a / Production host: Escherichia coli (E. coli) / Strain (production host): BL21 Codon-Plus RIL (DE3)
References: UniProt: Q08603, protein geranylgeranyltransferase type II

-
Non-polymers , 4 types, 351 molecules

#3: Chemical ChemComp-ZN / ZINC ION


Mass: 65.409 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Zn
#4: Chemical ChemComp-CA / CALCIUM ION


Mass: 40.078 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Ca
#5: Chemical ChemComp-BD8 / N-undecanoyl-L-histidyl-L-phenylalanyl-N-methyl-N-(2-pyridin-2-ylethyl)-L-tyrosinamide


Mass: 751.957 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C43H57N7O5
#6: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 348 / 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: 2.32 Å3/Da / Density % sol: 47.01 %
Crystal growTemperature: 284 K / Method: vapor diffusion, hanging drop / pH: 7.2
Details: 14% (w/v) PEG3350, 0.2 M Ca(OAc)2, 0.1 M HEPES, pH 7.2, VAPOR DIFFUSION, HANGING DROP, temperature 284K

-
Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SLS / Beamline: X10SA / Wavelength: 0.9999 Å
DetectorType: MARMOSAIC 225 mm CCD / Detector: CCD / Date: Oct 11, 2008
RadiationMonochromator: SI(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9999 Å / Relative weight: 1
ReflectionResolution: 1.95→30 Å / Num. all: 51864 / Num. obs: 51113 / % possible obs: 98.6 % / Observed criterion σ(I): 5.47 / Redundancy: 6.8 % / Biso Wilson estimate: 35.1 Å2 / Rsym value: 0.055 / Net I/σ(I): 20.09
Reflection shellResolution: 1.95→2.05 Å / Redundancy: 5 % / Mean I/σ(I) obs: 5.47 / Num. unique all: 6958 / Rsym value: 0.318 / % possible all: 97.8

-
Processing

Software
NameVersionClassification
PHASERphasing
REFMAC5.2.0005refinement
XDSdata reduction
XSCALEdata scaling
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 1.95→29.4 Å / Cor.coef. Fo:Fc: 0.966 / Cor.coef. Fo:Fc free: 0.934 / SU B: 7.19 / SU ML: 0.095 / Cross valid method: THROUGHOUT / ESU R: 1.813 / ESU R Free: 0.143 / Stereochemistry target values: MAXIMUM LIKELIHOOD
Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS; TLS-REFINEMENT WAS USED
RfactorNum. reflection% reflectionSelection details
Rfree0.21524 2567 5 %RANDOM
Rwork0.15449 ---
obs0.15749 48530 98.56 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: BABINET MODEL WITH MASK
Displacement parametersBiso mean: 31.086 Å2
Baniso -1Baniso -2Baniso -3
1-1.55 Å20 Å20 Å2
2---2.1 Å20 Å2
3---0.54 Å2
Refinement stepCycle: LAST / Resolution: 1.95→29.4 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms4943 0 57 348 5348
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0210.0225153
X-RAY DIFFRACTIONr_bond_other_d00.024632
X-RAY DIFFRACTIONr_angle_refined_deg1.781.9657007
X-RAY DIFFRACTIONr_angle_other_deg3.7783.00210677
X-RAY DIFFRACTIONr_dihedral_angle_1_deg6.3095640
X-RAY DIFFRACTIONr_dihedral_angle_2_deg35.87624.017229
X-RAY DIFFRACTIONr_dihedral_angle_3_deg16.03915840
X-RAY DIFFRACTIONr_dihedral_angle_4_deg16.6711528
X-RAY DIFFRACTIONr_chiral_restr0.1260.2776
X-RAY DIFFRACTIONr_gen_planes_refined0.0080.025743
X-RAY DIFFRACTIONr_gen_planes_other0.0120.021054
X-RAY DIFFRACTIONr_nbd_refined0.2250.21197
X-RAY DIFFRACTIONr_nbd_other0.2320.24320
X-RAY DIFFRACTIONr_nbtor_refined0.1880.22562
X-RAY DIFFRACTIONr_nbtor_other0.1090.22542
X-RAY DIFFRACTIONr_xyhbond_nbd_refined0.1670.2269
X-RAY DIFFRACTIONr_metal_ion_refined0.2030.24
X-RAY DIFFRACTIONr_symmetry_vdw_refined0.1760.29
X-RAY DIFFRACTIONr_symmetry_vdw_other0.280.232
X-RAY DIFFRACTIONr_symmetry_hbond_refined0.1850.217
X-RAY DIFFRACTIONr_symmetry_metal_ion_refined0.120.23
X-RAY DIFFRACTIONr_mcbond_it1.2671.53163
X-RAY DIFFRACTIONr_mcbond_other1.851.51283
X-RAY DIFFRACTIONr_mcangle_it2.40325066
X-RAY DIFFRACTIONr_scbond_it3.8431990
X-RAY DIFFRACTIONr_scangle_it4.744.51934
LS refinement shellResolution: 1.95→2 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.249 178 -
Rwork0.163 3484 -
obs--97.78 %
Refinement TLS params.

Method: refined / Refine-ID: X-RAY DIFFRACTION

IDL11 (°2)L12 (°2)L13 (°2)L22 (°2)L23 (°2)L33 (°2)S11 (Å °)S12 (Å °)S13 (Å °)S21 (Å °)S22 (Å °)S23 (Å °)S31 (Å °)S32 (Å °)S33 (Å °)T11 (Å2)T12 (Å2)T13 (Å2)T22 (Å2)T23 (Å2)T33 (Å2)Origin x (Å)Origin y (Å)Origin z (Å)
10.00150.00030.00360.0020.00240.0099-0.00060-0.0003-0.0001-0.00050-0.000200.0010.00270.000400.00810.0001-0.001114.12616.538115.9771
20.00070.00180.0020.00470.00470.00670.0005-0.0009-0.0002-0.0004-0.0015-0.0002-0.0009-0.00230.00110.00270.000400.0081-0.0003-0.0013.012226.183617.8862
30000000000000000.00290.0002-0.00010.002700.0021-0.52717.010923.4551
4000000000000000000000-8.338943.820729.0979
53.54051.2915-1.81681.8654-0.49320.95290.0429-0.10980.1099-0.017-0.06670.08850.10980.3140.0238-0.00060.00070.00040.00020.000204.618922.482524.3451
60.00010.0001-0.00030.0002-0.00040.0008-0.00010.000300.0002-0.0003-0.0002-0.0001-0.00040.00040.00280.000100.0079-0.0002-0.00098.9216.89515.3074
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A18 - 330
2X-RAY DIFFRACTION2B5 - 331
3X-RAY DIFFRACTION3B332
4X-RAY DIFFRACTION4B333
5X-RAY DIFFRACTION5B334
6X-RAY DIFFRACTION6A331 - 487
7X-RAY DIFFRACTION6B335 - 525

+
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