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- PDB-1xk9: Pseudomanas exotoxin A in complex with the PJ34 inhibitor -

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Basic information

Entry
Database: PDB / ID: 1xk9
TitlePseudomanas exotoxin A in complex with the PJ34 inhibitor
ComponentsExotoxin A
KeywordsTRANSFERASE / toxin / ADP-ribosylation / inhibitor
Function / homology
Function and homology information


NAD+-diphthamide ADP-ribosyltransferase / NAD+-diphthamide ADP-ribosyltransferase activity / nucleotidyltransferase activity / toxin activity
Similarity search - Function
Exotoxin A catalytic domain / Exotoxin A, binding / Exotoxin A, middle domain / Exotoxin A, middle domain superfamily / Exotoxin A catalytic / Exotoxin A binding / Exotoxin A, targeting / Diphtheria Toxin; domain 1 / Diphtheria Toxin, domain 1 / Concanavalin A-like lectin/glucanase domain superfamily ...Exotoxin A catalytic domain / Exotoxin A, binding / Exotoxin A, middle domain / Exotoxin A, middle domain superfamily / Exotoxin A catalytic / Exotoxin A binding / Exotoxin A, targeting / Diphtheria Toxin; domain 1 / Diphtheria Toxin, domain 1 / Concanavalin A-like lectin/glucanase domain superfamily / Alpha-Beta Complex / Alpha Beta
Similarity search - Domain/homology
Chem-P34 / Exotoxin A
Similarity search - Component
Biological speciesPseudomonas aeruginosa (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.1 Å
AuthorsYates, S.P. / Taylor, P.J. / Joergensen, R. / Ferrraris, D. / Zhang, J. / Andersen, G.R. / Merrill, A.R.
CitationJournal: BIOCHEM.J. / Year: 2005
Title: Structure-function analysis of water-soluble inhibitors of the catalytic domain of exotoxin A from Pseudomonas aeruginosa
Authors: Yates, S.P. / Taylor, P.J. / Joergensen, R. / Ferrraris, D. / Zhang, J. / Andersen, G.R. / Merrill, A.R.
History
DepositionSep 28, 2004Deposition site: RCSB / Processing site: PDBJ
Revision 1.0May 17, 2005Provider: repository / Type: Initial release
Revision 1.1Apr 30, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3May 23, 2018Group: Data collection / Category: diffrn_source / Item: _diffrn_source.pdbx_synchrotron_site
Revision 1.4Nov 10, 2021Group: Database references / Derived calculations / Category: 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
Revision 1.5Oct 25, 2023Group: Data collection / Refinement description
Category: chem_comp_atom / chem_comp_bond / pdbx_initial_refinement_model

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: Exotoxin A
B: Exotoxin A
hetero molecules


Theoretical massNumber of molelcules
Total (without water)47,5174
Polymers46,9262
Non-polymers5912
Water7,224401
1
A: Exotoxin A
hetero molecules


Theoretical massNumber of molelcules
Total (without water)23,7582
Polymers23,4631
Non-polymers2951
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
B: Exotoxin A
hetero molecules


Theoretical massNumber of molelcules
Total (without water)23,7582
Polymers23,4631
Non-polymers2951
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)56.040, 78.680, 91.690
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number19
Space group name H-MP212121

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Components

#1: Protein Exotoxin A / NAD-dependent ADP-ribosyltransferase


Mass: 23463.156 Da / Num. of mol.: 2 / Fragment: catalytic fragment, PE24H
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Pseudomonas aeruginosa (bacteria) / Plasmid: PE(delta)5-399 / Production host: Escherichia coli (E. coli) / Strain (production host): BB101
References: UniProt: P11439, NAD+-diphthamide ADP-ribosyltransferase
#2: Chemical ChemComp-P34 / N~2~,N~2~-DIMETHYL-N~1~-(6-OXO-5,6-DIHYDROPHENANTHRIDIN-2-YL)GLYCINAMIDE


Mass: 295.336 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C17H17N3O2
#3: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 401 / 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: 2.5 Å3/Da / Density % sol: 64 %
Crystal growTemperature: 293 K / Method: vapor diffusion, sitting drop / pH: 7.5
Details: sodium citrate, DTT, NaAzid, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: MAX II / Beamline: I911-2 / Wavelength: 1.046 Å
DetectorType: MARRESEARCH / Detector: CCD / Date: Nov 20, 2003
RadiationMonochromator: Bent germanium crystal, horizontally focusing
Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.046 Å / Relative weight: 1
ReflectionResolution: 2.1→35 Å / Num. all: 24276 / Num. obs: 24276 / % possible obs: 99.8 % / Observed criterion σ(F): -3 / Observed criterion σ(I): -3 / Redundancy: 6.8 % / Biso Wilson estimate: 20 Å2 / Rmerge(I) obs: 0.108 / Net I/σ(I): 13.35
Reflection shellResolution: 2.1→2.3 Å / Redundancy: 6.8 % / Rmerge(I) obs: 0.236 / Mean I/σ(I) obs: 7.7 / Num. unique all: 5718 / % possible all: 100

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Processing

Software
NameClassification
XDSdata scaling
XSCALEdata scaling
CNSrefinement
XDSdata reduction
CNSphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB entry 1AER
Resolution: 2.1→35 Å / Cross valid method: THROUGHOUT / σ(F): 0 / Stereochemistry target values: Engh & Huber
RfactorNum. reflectionSelection details
Rfree0.235 1236 random
Rwork0.213 --
all0.214 24316 -
obs0.213 24275 -
Refinement stepCycle: LAST / Resolution: 2.1→35 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms3090 0 44 401 3535
Refine LS restraints
Refine-IDTypeDev ideal
X-RAY DIFFRACTIONc_bond_d0.008
X-RAY DIFFRACTIONc_angle_deg1.5

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