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- PDB-3zxo: CRYSTAL STRUCTURE OF THE MUTANT ATP-BINDING DOMAIN OF MYCOBACTERI... -
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Basic information
Entry | Database: PDB / ID: 3zxo | ||||||
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Title | CRYSTAL STRUCTURE OF THE MUTANT ATP-BINDING DOMAIN OF MYCOBACTERIUM TUBERCULOSIS DOSS | ||||||
![]() | REDOX SENSOR HISTIDINE KINASE RESPONSE REGULATOR DEVS | ||||||
![]() | TRANSFERASE | ||||||
Function / homology | ![]() detection of redox state / carbon monoxide binding / nitric oxide binding / oxygen sensor activity / response to redox state / histidine kinase / phosphorelay sensor kinase activity / peptidoglycan-based cell wall / oxygen binding / protein autophosphorylation ...detection of redox state / carbon monoxide binding / nitric oxide binding / oxygen sensor activity / response to redox state / histidine kinase / phosphorelay sensor kinase activity / peptidoglycan-based cell wall / oxygen binding / protein autophosphorylation / membrane => GO:0016020 / protein dimerization activity / protein kinase activity / heme binding / magnesium ion binding / ATP binding / metal ion binding / plasma membrane / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Cho, H.Y. / Cho, H.J. / Kang, B.S. | ||||||
![]() | ![]() Title: Activation of ATP Binding for the Autophosphorylation of Doss, a Mycobacterium Tuberculosis Histidine Kinase Lacking an ATP-Lid Motif. Authors: Cho, H.Y. / Lee, Y.H. / Bae, Y.S. / Kim, E. / Kang, B.S. #1: Journal: J.Mol.Biol. / Year: 2005 Title: A Gaf Domain in the Hypoxia/No-Inducible Mycobacterium Tuberculosis Doss Protein Binds Haem. Authors: Sardiwal, S. / Kendall, S.L. / Movahedzadeh, F. / Rison, S.C.G. / Stoker, N.G. / Djordjevic, S. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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PDBx/mmCIF format | ![]() | 62.8 KB | Display | ![]() |
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PDB format | ![]() | 51.3 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-Validation report
Summary document | ![]() | 464.5 KB | Display | ![]() |
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Full document | ![]() | 467.7 KB | Display | |
Data in XML | ![]() | 14.6 KB | Display | |
Data in CIF | ![]() | 20.3 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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Links
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Assembly
Deposited unit | ![]()
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2 | ![]()
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Unit cell |
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Components on special symmetry positions |
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Components
#1: Protein | Mass: 13716.783 Da / Num. of mol.: 2 / Fragment: ATP-BINDING DOMAIN, RESIDUES 454-578 / Mutation: YES Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() References: UniProt: P95194, UniProt: P9WGK3*PLUS, Transferases; Transferring phosphorus-containing groups; Phosphotransferases with a nitrogenous group as acceptor, histidine kinase #2: Chemical | #3: Chemical | ChemComp-ACT / #4: Chemical | ChemComp-GOL / | #5: Water | ChemComp-HOH / | Compound details | ENGINEERED RESIDUE IN CHAIN A, LYS 509 TO ALA ENGINEERED RESIDUE IN CHAIN A, LEU 534 TO MET ...ENGINEERED | Sequence details | ADDITIONAL | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.42 Å3/Da / Density % sol: 49.12 % / Description: NONE |
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Crystal grow | pH: 6 Details: PROTEIN WAS CRYSTALLIZED FROM 15% PEG 1500, 200 MM ZINC ACETATE, 100 MM CITRATE, PH 6.0 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() |
Detector | Type: BRUKER PROTEUM 300 / Detector: CCD / Date: Jan 14, 2010 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.97908 Å / Relative weight: 1 |
Reflection | Resolution: 1.9→50 Å / Num. obs: 25671 / % possible obs: 99.9 % / Observed criterion σ(I): -2 / Redundancy: 22.3 % / Rmerge(I) obs: 0.08 / Net I/σ(I): 55.97 |
Reflection shell | Resolution: 1.83→1.9 Å / Redundancy: 20.8 % / Rmerge(I) obs: 0.46 / Mean I/σ(I) obs: 8.26 / % possible all: 99.9 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: NONE Resolution: 1.9→46.08 Å / Cor.coef. Fo:Fc: 0.95 / Cor.coef. Fo:Fc free: 0.916 / SU B: 3.303 / SU ML: 0.098 / Cross valid method: THROUGHOUT / ESU R: 0.158 / ESU R Free: 0.15 / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. T454 TO Q578 OF DOSS WITH ADDITIONAL V SEQUENCE AT THE N- -TERMINUS DUE TO CLONING PROCEDURE
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 22.668 Å2
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Refinement step | Cycle: LAST / Resolution: 1.9→46.08 Å
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Refine LS restraints |
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