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- PDB-2jhs: CRYSTAL STRUCTURE OF RHOGDI K135H,K138H,K141H MUTANT -

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Basic information

Entry
Database: PDB / ID: 2jhs
TitleCRYSTAL STRUCTURE OF RHOGDI K135H,K138H,K141H MUTANT
ComponentsRHO GDP-DISSOCIATION INHIBITOR 1
KeywordsINHIBITOR / SURFACE ENTROPY REDUCTION / GTPASE ACTIVATION / CRYSTAL ENGINEERING
Function / homology
Function and homology information


Rho GDP-dissociation inhibitor activity / Axonal growth inhibition (RHOA activation) / Axonal growth stimulation / regulation of Rho protein signal transduction / regulation of synaptic vesicle cycle / RHOC GTPase cycle / semaphorin-plexin signaling pathway / CDC42 GTPase cycle / RHOH GTPase cycle / immunological synapse ...Rho GDP-dissociation inhibitor activity / Axonal growth inhibition (RHOA activation) / Axonal growth stimulation / regulation of Rho protein signal transduction / regulation of synaptic vesicle cycle / RHOC GTPase cycle / semaphorin-plexin signaling pathway / CDC42 GTPase cycle / RHOH GTPase cycle / immunological synapse / RHOG GTPase cycle / RHOA GTPase cycle / RAC2 GTPase cycle / Rho protein signal transduction / RAC1 GTPase cycle / GTPase activator activity / Schaffer collateral - CA1 synapse / regulation of protein localization / cytoskeleton / negative regulation of apoptotic process / extracellular exosome / nucleus / membrane / cytosol
Similarity search - Function
Coagulation Factor XIII, subunit A, domain 1 / Rho protein GDP-dissociation inhibitor / Rho GDP-dissociation inhibitor domain superfamily / RHO protein GDP dissociation inhibitor / Coagulation Factor XIII; Chain A, domain 1 / Distorted Sandwich / Immunoglobulin E-set / Mainly Beta
Similarity search - Domain/homology
CITRATE ANION / Rho GDP-dissociation inhibitor 1
Similarity search - Component
Biological speciesHOMO SAPIENS (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.95 Å
AuthorsCooper, D.R. / Zawadzki, M. / Derewenda, Z.S.
CitationJournal: Acta Crystallogr.,Sect.D / Year: 2007
Title: Protein Crystallization by Surface Entropy Reduction: Optimization of the Ser Strategy
Authors: Cooper, D.R. / Boczek, T. / Grelewska, K. / Pinkowska, M. / Sikorska, M. / Zawadzki, M. / Derewenda, Z.S.
History
DepositionFeb 23, 2007Deposition site: PDBE / Processing site: PDBE
Revision 1.0May 8, 2007Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Advisory / Version format compliance
Revision 1.2Dec 13, 2023Group: Data collection / Database references ...Data collection / Database references / 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
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.status_code_sf
Remark 700 SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN ... SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW, TWO SHEETS ARE DEFINED.

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: RHO GDP-DISSOCIATION INHIBITOR 1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)16,0122
Polymers15,8231
Non-polymers1891
Water2,396133
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPQS
Unit cell
Length a, b, c (Å)75.316, 75.316, 91.283
Angle α, β, γ (deg.)90.00, 90.00, 120.00
Int Tables number154
Space group name H-MP3221
Components on special symmetry positions
IDModelComponents
11A-2055-

HOH

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Components

#1: Protein RHO GDP-DISSOCIATION INHIBITOR 1 / RHO GDI 1 / RHO-GDI ALPHA


Mass: 15822.951 Da / Num. of mol.: 1 / Fragment: ISOPRENYL-BINDING DOMAIN, RESIDUES 66-201 / Mutation: YES
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) HOMO SAPIENS (human) / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: P52565
#2: Chemical ChemComp-FLC / CITRATE ANION


Mass: 189.100 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C6H5O7
#3: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 133 / Source method: isolated from a natural source / Formula: H2O
Compound detailsENGINEERED RESIDUE IN CHAIN A, LYS 134 TO HIS ENGINEERED RESIDUE IN CHAIN A, LYS 137 TO HIS ...ENGINEERED RESIDUE IN CHAIN A, LYS 134 TO HIS ENGINEERED RESIDUE IN CHAIN A, LYS 137 TO HIS ENGINEERED RESIDUE IN CHAIN A, LYS 140 TO HIS
Sequence detailsMUTATIONS ENGINEERED TO FACILITATE CRYSTALLIZATION

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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: 5 Å3/Da / Density % sol: 75 %
Crystal growpH: 7.5 / Details: 1.4 M SODIUM CITRATE, 100 MM HEPES PH 7.5

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 22-BM / Wavelength: 1
DetectorType: MARRESEARCH / Detector: CCD / Date: Nov 4, 2005
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 1.95→50 Å / Num. obs: 22205 / % possible obs: 99.7 % / Redundancy: 6 % / Rmerge(I) obs: 0.04 / Net I/σ(I): 35.6
Reflection shellResolution: 1.95→2.02 Å / Redundancy: 5.6 % / Rmerge(I) obs: 0.34 / Mean I/σ(I) obs: 4.9 / % possible all: 99.8

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Processing

Software
NameVersionClassification
REFMAC5.2.0019refinement
HKL-2000data reduction
HKL-2000data scaling
AMoREphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 2BXW

2bxw


Resolution: 1.95→65.23 Å / Cor.coef. Fo:Fc: 0.966 / Cor.coef. Fo:Fc free: 0.955 / SU B: 4.509 / SU ML: 0.069 / TLS residual ADP flag: LIKELY RESIDUAL / Cross valid method: THROUGHOUT / ESU R: 0.099 / ESU R Free: 0.101 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS.
RfactorNum. reflection% reflectionSelection details
Rfree0.209 1043 4.7 %RANDOM
Rwork0.178 ---
obs0.179 21112 99.5 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: MASK
Displacement parametersBiso mean: 44.62 Å2
Baniso -1Baniso -2Baniso -3
1-0.52 Å20.26 Å20 Å2
2--0.52 Å20 Å2
3----0.78 Å2
Refinement stepCycle: LAST / Resolution: 1.95→65.23 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms1108 0 13 133 1254
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0110.0221157
X-RAY DIFFRACTIONr_bond_other_d0.0010.02798
X-RAY DIFFRACTIONr_angle_refined_deg2.3281.9651567
X-RAY DIFFRACTIONr_angle_other_deg1.51931938
X-RAY DIFFRACTIONr_dihedral_angle_1_deg5.4925138
X-RAY DIFFRACTIONr_dihedral_angle_2_deg31.20523.20853
X-RAY DIFFRACTIONr_dihedral_angle_3_deg12.33315203
X-RAY DIFFRACTIONr_dihedral_angle_4_deg17.797158
X-RAY DIFFRACTIONr_chiral_restr0.10.2167
X-RAY DIFFRACTIONr_gen_planes_refined0.0040.021268
X-RAY DIFFRACTIONr_gen_planes_other0.0010.02241
X-RAY DIFFRACTIONr_nbd_refined0.1950.2146
X-RAY DIFFRACTIONr_nbd_other0.1720.2751
X-RAY DIFFRACTIONr_nbtor_refined0.1740.2530
X-RAY DIFFRACTIONr_nbtor_other0.0830.2641
X-RAY DIFFRACTIONr_xyhbond_nbd_refined0.1280.282
X-RAY DIFFRACTIONr_xyhbond_nbd_other
X-RAY DIFFRACTIONr_metal_ion_refined
X-RAY DIFFRACTIONr_metal_ion_other
X-RAY DIFFRACTIONr_symmetry_vdw_refined0.1380.26
X-RAY DIFFRACTIONr_symmetry_vdw_other0.2640.224
X-RAY DIFFRACTIONr_symmetry_hbond_refined0.1550.28
X-RAY DIFFRACTIONr_symmetry_hbond_other
X-RAY DIFFRACTIONr_symmetry_metal_ion_refined
X-RAY DIFFRACTIONr_symmetry_metal_ion_other
X-RAY DIFFRACTIONr_mcbond_it1.1661.5885
X-RAY DIFFRACTIONr_mcbond_other
X-RAY DIFFRACTIONr_mcangle_it1.33621111
X-RAY DIFFRACTIONr_mcangle_other
X-RAY DIFFRACTIONr_scbond_it2.4283564
X-RAY DIFFRACTIONr_scbond_other
X-RAY DIFFRACTIONr_scangle_it3.2884.5455
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
Rfree0.303 79
Rwork0.246 1531
Refinement TLS params.Method: refined / Origin x: -24.556 Å / Origin y: -14.159 Å / Origin z: 32.318 Å
111213212223313233
T-0.3359 Å20.0134 Å2-0.0246 Å2--0.3848 Å20.0005 Å2---0.3427 Å2
L2.4757 °2-2.1642 °22.0187 °2-2.2893 °2-1.9373 °2--2.337 °2
S-0.065 Å °0.0994 Å °0.1451 Å °0.0697 Å °-0.103 Å °-0.1058 Å °-0.1961 Å °0.0878 Å °0.168 Å °

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