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Open data
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Basic information
Entry | Database: PDB / ID: 2c44 | ||||||
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Title | Crystal Structure of E. coli Tryptophanase | ||||||
![]() | TRYPTOPHANASE | ||||||
![]() | LYASE / PYRIDOXAL PHOSPHATE / TRYPTOPHAN CATABOLISM | ||||||
Function / homology | ![]() indole metabolic process / tryptophanase activity / tryptophanase / cell pole / L-cysteine desulfhydrase activity / tryptophan catabolic process / potassium ion binding / pyridoxal phosphate binding / protein-containing complex / identical protein binding ...indole metabolic process / tryptophanase activity / tryptophanase / cell pole / L-cysteine desulfhydrase activity / tryptophan catabolic process / potassium ion binding / pyridoxal phosphate binding / protein-containing complex / identical protein binding / membrane / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Ku, S.-Y. / Yip, P. / Howell, P.L. | ||||||
![]() | ![]() Title: Structure of Escherichia Coli Tryptophanase Authors: Ku, S.-Y. / Yip, P. / Howell, P.L. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 366.9 KB | Display | ![]() |
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PDB format | ![]() | 298.5 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 471 KB | Display | ![]() |
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Full document | ![]() | 504.3 KB | Display | |
Data in XML | ![]() | 70.9 KB | Display | |
Data in CIF | ![]() | 97 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1ax4S S: Starting model for refinement |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS domain:
NCS domain segments:
NCS oper:
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Components
#1: Protein | Mass: 52850.266 Da / Num. of mol.: 4 / Source method: isolated from a natural source Details: ONE SULFATE IN THE PLP BINDING SITE, AND THE OTHER SULFATE IN THE TRYPTOPHAN BINDING SITE Source: (natural) ![]() ![]() References: UniProt: Q8XB34, UniProt: P0A853*PLUS, tryptophanase #2: Chemical | ChemComp-SO4 / #3: Chemical | ChemComp-K / #4: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.96 Å3/Da / Density % sol: 58.4 % |
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Crystal grow | pH: 7.9 Details: 1.6M AMMONIUM SULFATE, 0.5%(V/V)PEG400, 0.1M SODIUM HEPES PH 7.9 |
-Data collection
Diffraction | Mean temperature: 110 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC CCD / Detector: CCD / Date: Jul 31, 2002 / Details: RH-COATED FUSED SILICA COLLIMATING MIRROR |
Radiation | Monochromator: SI (111) DOUBLE-CRYSTAL MONOCHROMATOR / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 2.8→500 Å / Num. obs: 62257 / % possible obs: 99.3 % / Observed criterion σ(I): 0 / Redundancy: 6.6 % / Rmerge(I) obs: 0.09 / Net I/σ(I): 26.9 |
Reflection shell | Resolution: 2.8→2.91 Å / Rmerge(I) obs: 0.24 / Mean I/σ(I) obs: 8.7 / % possible all: 98.8 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 1AX4 Resolution: 2.8→500 Å / Cor.coef. Fo:Fc: 0.935 / Cor.coef. Fo:Fc free: 0.858 / SU B: 11.546 / SU ML: 0.228 / Cross valid method: THROUGHOUT / ESU R Free: 0.346 / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. DISORDERED REGIONS WERE NOT MODELED. RESIDUES WITH DISORDERED SIDE CHAINS WERE MODELED AS ALANINE (ALA).
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 8.8 Å2
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Refinement step | Cycle: LAST / Resolution: 2.8→500 Å
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Refine LS restraints |
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