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Open data
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Basic information
Entry | Database: PDB / ID: 1fwi | ||||||
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Title | KLEBSIELLA AEROGENES UREASE, H134A VARIANT | ||||||
![]() | (UREASE) x 3 | ||||||
![]() | HYDROLASE / HYDROLASE(UREA AMIDO) / MUTANT / NICKEL METALLOENZYME | ||||||
Function / homology | ![]() urease complex / urease / urease activity / urea catabolic process / nickel cation binding / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() | ||||||
![]() | Pearson, M.A. / Karplus, P.A. | ||||||
![]() | ![]() Title: Characterization of the mononickel metallocenter in H134A mutant urease. Authors: Park, I.S. / Michel, L.O. / Pearson, M.A. / Jabri, E. / Karplus, P.A. / Wang, S. / Dong, J. / Scott, R.A. / Koehler, B.P. / Johnson, M.K. / Hausinger, R.P. #1: ![]() Title: Structures of the Klebsiella Aerogenes Urease Apoenzyme and Two Active-Site Mutants Authors: Jabri, E. / Karplus, P.A. #2: ![]() Title: The Crystal Structure of Urease from Klebsiella Aerogenes Authors: Jabri, E. / Carr, M.B. / Hausinger, R.P. / Karplus, P.A. #3: ![]() Title: Site-Directed Mutagenesis of Klebsiella Aerogenes Urease: Identification of Histidine Residues that Appear to Function in Nickel Ligation, Substrate Binding, and Catalysis Authors: Park, I.S. / Hausinger, R.P. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 155.8 KB | Display | ![]() |
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PDB format | ![]() | 126.5 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 434.6 KB | Display | ![]() |
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Full document | ![]() | 439 KB | Display | |
Data in XML | ![]() | 29.2 KB | Display | |
Data in CIF | ![]() | 42.9 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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1 | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 11100.928 Da / Num. of mol.: 1 / Mutation: H(C 134)A Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
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#2: Protein | Mass: 11712.239 Da / Num. of mol.: 1 / Mutation: H(C 134)A Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
#3: Protein | Mass: 60342.289 Da / Num. of mol.: 1 / Mutation: H(C 134)A Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
#4: Chemical | ChemComp-NI / |
#5: Water | ChemComp-HOH / |
Compound details | THIS MODEL IS THAT OF THE H134A MUTANT AT 2.0 ANGSTROMS. THREE NONIDENTICAL CHAINS, GAMMA (A), BETA ...THIS MODEL IS THAT OF THE H134A MUTANT AT 2.0 ANGSTROMS. THREE NONIDENTIC |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.5 Å3/Da / Density % sol: 49 % | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | *PLUS Temperature: 25 ℃ / pH: 7 / Method: vapor diffusion, hanging drop / Details: Jabri, E., (1992) J.Mol.Biol., 227, 934. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction source | Wavelength: 1.5418 |
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Detector | Type: XUONG-HAMLIN MULTIWIRE / Detector: AREA DETECTOR |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Num. obs: 52421 / % possible obs: 96 % / Observed criterion σ(I): 0 / Redundancy: 3.3 % / Rmerge(I) obs: 0.066 |
Reflection | *PLUS Highest resolution: 2 Å |
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Processing
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Refinement | Resolution: 2→10 Å / σ(F): 0
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Refinement step | Cycle: LAST / Resolution: 2→10 Å
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Refine LS restraints |
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Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Rfactor obs: 0.17 / Rfactor Rwork: 0.17 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS |