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Open data
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Basic information
Entry | Database: PDB / ID: 2v7g | ||||||
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Title | Crystal Structure of an Engineered Urocanase Tetramer | ||||||
![]() | UROCANATE HYDRATASE | ||||||
![]() | LYASE / HISTIDINE DEGRADATION / NAD / PROTEIN ENGINEERING / UROCANATE HYDRATASE / HISTIDINE METABOLISM | ||||||
Function / homology | ![]() urocanate hydratase / urocanate hydratase activity / L-histidine catabolic process to glutamate and formamide / L-histidine catabolic process to glutamate and formate / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Treiber, N. / Schulz, G.E. | ||||||
![]() | ![]() Title: Designed Protein-Protein Association. Authors: Grueninger, D. / Treiber, N. / Ziegler, M.O.P. / Koetter, J.W.A. / Schulze, M.-S. / Schulz, G.E. | ||||||
History |
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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 viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 446.5 KB | Display | ![]() |
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PDB format | ![]() | 365 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 1.7 MB | Display | ![]() |
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Full document | ![]() | 1.7 MB | Display | |
Data in XML | ![]() | 87.8 KB | Display | |
Data in CIF | ![]() | 127.6 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 2uyuC ![]() 2uyvC ![]() 2v9eC ![]() 2v9fC ![]() 2v9gC ![]() 2v9iC ![]() 2v9lC ![]() 2v9mC ![]() 2v9nC ![]() 2v9oC ![]() 2v9uC ![]() 1uwlS S: Starting model for refinement C: citing same article ( |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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2 | ![]()
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3 | ![]()
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4 | ![]()
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS oper:
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Components
#1: Protein | Mass: 60811.684 Da / Num. of mol.: 4 / Mutation: YES Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() #2: Chemical | ChemComp-ACT / #3: Chemical | ChemComp-GOL / #4: Chemical | ChemComp-NAD / #5: Water | ChemComp-HOH / | Sequence details | THE SEQUENCE CONFLICTS ANNOTATED BELOW IN THE SEQADV RECORDS BELOW CORRESPOND TO A KNOWN CONFLICT ...THE SEQUENCE CONFLICTS ANNOTATED BELOW IN THE SEQADV RECORDS BELOW CORRESPOND | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.3 Å3/Da / Density % sol: 47 % / Description: NONE |
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Crystal grow | pH: 6.6 Details: 10% (W/V) PEG8000, 0.2 M MGAC2, 20% (V/V) GLYCERIN, 0.1 M NA CACODYLATE PH 6.9 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARREASEARCH / Detector: CCD / Date: Nov 1, 2004 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.8853 Å / Relative weight: 1 |
Reflection | Resolution: 2→28.8 Å / Num. obs: 149793 / % possible obs: 97 % / Observed criterion σ(I): 6.6 / Redundancy: 6.3 % / Rmerge(I) obs: 0.09 / Net I/σ(I): 14.7 |
Reflection shell | Resolution: 2→2.06 Å / Redundancy: 5.9 % / Rmerge(I) obs: 0.33 / Mean I/σ(I) obs: 6.6 / % possible all: 90 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 1UWL Resolution: 2→28.81 Å / Cor.coef. Fo:Fc: 0.959 / Cor.coef. Fo:Fc free: 0.948 / SU B: 5.721 / SU ML: 0.084 / TLS residual ADP flag: LIKELY RESIDUAL / Cross valid method: THROUGHOUT / ESU R: 0.156 / ESU R Free: 0.128 / Stereochemistry target values: MAXIMUM LIKELIHOOD
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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: 26.01 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2→28.81 Å
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Refine LS restraints |
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