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- PDB-1xa6: Crystal Structure of the Human Beta2-Chimaerin -

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Basic information

Entry
Database: PDB / ID: 1xa6
TitleCrystal Structure of the Human Beta2-Chimaerin
ComponentsBeta2-chimaerin
KeywordsSIGNALING PROTEIN / Beta2-chimaerin / RacGAP / C1
Function / homology
Function and homology information


: / regulation of small GTPase mediated signal transduction / regulation of GTPase activity / GTPase activator activity / intracellular signal transduction / synapse / membrane / metal ion binding / cytosol
Similarity search - Function
Chimaerin / Chimaerin, SH2 domain / Chimaerin, RhoGAP domain / Phosphatidylinositol 3-kinase; Chain A / Rho GTPase activation protein / Wheat Germ Agglutinin (Isolectin 2); domain 1 - #20 / Rho GTPase-activating protein domain / RhoGAP domain / Rho GTPase-activating proteins domain profile. / GTPase-activator protein for Rho-like GTPases ...Chimaerin / Chimaerin, SH2 domain / Chimaerin, RhoGAP domain / Phosphatidylinositol 3-kinase; Chain A / Rho GTPase activation protein / Wheat Germ Agglutinin (Isolectin 2); domain 1 - #20 / Rho GTPase-activating protein domain / RhoGAP domain / Rho GTPase-activating proteins domain profile. / GTPase-activator protein for Rho-like GTPases / Diacylglycerol/phorbol-ester binding / Wheat Germ Agglutinin (Isolectin 2); domain 1 / Phorbol esters/diacylglycerol binding domain (C1 domain) / Rho GTPase activation protein / SH2 domain / SHC Adaptor Protein / Zinc finger phorbol-ester/DAG-type signature. / Zinc finger phorbol-ester/DAG-type profile. / Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains) / Protein kinase C-like, phorbol ester/diacylglycerol-binding domain / SH2 domain / Src homology 2 (SH2) domain profile. / Src homology 2 domains / SH2 domain / SH2 domain superfamily / 2-Layer Sandwich / Orthogonal Bundle / Mainly Alpha / Alpha Beta
Similarity search - Domain/homology
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / SAD / Resolution: 3.2 Å
AuthorsCanagarajah, B. / Leskow, F.C. / Ho, J.Y. / Mischak, H. / Saidi, L.F. / Kazanietz, M.G. / Hurley, J.H.
CitationJournal: Cell(Cambridge,Mass.) / Year: 2004
Title: Structural mechanism for lipid activation of the Rac-specific GAP, beta2-chimaerin.
Authors: Canagarajah, B. / Leskow, F.C. / Ho, J.Y. / Mischak, H. / Saidi, L.F. / Kazanietz, M.G. / Hurley, J.H.
History
DepositionAug 25, 2004Deposition site: RCSB / Processing site: RCSB
Revision 1.0Nov 23, 2004Provider: repository / Type: Initial release
Revision 1.1Apr 30, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Feb 14, 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_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_conn.ptnr2_label_seq_id / _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

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Assembly

Deposited unit
A: Beta2-chimaerin
hetero molecules


Theoretical massNumber of molelcules
Total (without water)54,0873
Polymers53,9571
Non-polymers1312
Water0
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)131.090, 131.090, 288.750
Angle α, β, γ (deg.)90.00, 90.00, 120.00
Int Tables number178
Space group name H-MP6122

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Components

#1: Protein Beta2-chimaerin / Beta-chimerin / Rho-GTPase-activating protein 3


Mass: 53956.582 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Production host: Spodoptera frugiperda (fall armyworm) / References: UniProt: P52757
#2: Chemical ChemComp-ZN / ZINC ION


Mass: 65.409 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Zn

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 2

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Sample preparation

CrystalDensity Matthews: 6.7 Å3/Da / Density % sol: 80 %
Crystal growTemperature: 282 K / Method: vapor diffusion, hanging drop / pH: 6.8
Details: sodium/potassium phosphate, sodium cloride, ethanol, pH 6.8, VAPOR DIFFUSION, HANGING DROP, temperature 282.0K

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Data collection

Diffraction
IDMean temperature (K)Crystal-ID
1951
21
Diffraction source
SourceSiteBeamlineIDWavelength (Å)
SYNCHROTRONAPS 19-ID11.28
SYNCHROTRONNSLS X2521.1
Detector
TypeIDDetectorDate
ADSC QUANTUM 41CCDAug 6, 2003
2CCDMar 26, 2000
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength
IDWavelength (Å)Relative weight
11.281
21.11
ReflectionResolution: 3.2→50 Å / Num. obs: 26206 / % possible obs: 99.5 % / Observed criterion σ(F): 1 / Observed criterion σ(I): 2 / Rmerge(I) obs: 0.058
Reflection shellResolution: 3.2→3.3 Å / % possible all: 98.8

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Processing

Software
NameVersionClassification
DENZOdata reduction
SCALEPACKdata scaling
SOLVEphasing
CNS1refinement
RefinementMethod to determine structure: SAD / Resolution: 3.2→20 Å / σ(F): 0 / Stereochemistry target values: Engh & Huber
RfactorNum. reflectionSelection details
Rfree0.298 1188 RANDOM
Rwork0.252 --
all0.26 23767 -
obs0.26 23767 -
Refinement stepCycle: LAST / Resolution: 3.2→20 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms3254 0 2 0 3256
LS refinement shellResolution: 3.2→3.25 Å /
RfactorNum. reflection
Rfree0.555 46
Rwork0.5 -
obs-801

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