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- PDB-1gk2: Histidine Ammonia-Lyase (HAL) Mutant F329G from Pseudomonas putida -
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Open data
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Basic information
Entry | Database: PDB / ID: 1gk2 | ||||||
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Title | Histidine Ammonia-Lyase (HAL) Mutant F329G from Pseudomonas putida | ||||||
![]() | HISTIDINE AMMONIA-LYASE | ||||||
![]() | LYASE / HISTIDINE DEGRADATION | ||||||
Function / homology | ![]() histidine ammonia-lyase / histidine ammonia-lyase activity / L-histidine catabolic process to glutamate and formamide / L-histidine catabolic process to glutamate and formate / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() | ||||||
![]() | Baedeker, M. / Schulz, G.E. | ||||||
![]() | ![]() Title: Autocatalytic Peptide Cyclization During Chain Folding of Histidine Ammonia-Lyase. Authors: Baedeker, M. / Schulz, G.E. #1: ![]() Title: Crystal Structure of Histidine Ammonia-Lyase Revealing a Novel Polypeptide Modification as the Catalytic Electrophile Authors: Schwede, T.F. / Retey, J. / Schulz, G.E. #2: Journal: Protein Eng. / Year: 1999 Title: Homogenization and Crystallization of Histidine Ammonia-Lyase by Exchange of a Surface Cysteine Residue Authors: Schwede, T.F. / Baedeker, M. / Langer, M. / Retey, J. / Schulz, G.E. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 395.4 KB | Display | ![]() |
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PDB format | ![]() | 324.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 483.9 KB | Display | ![]() |
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Full document | ![]() | 522 KB | Display | |
Data in XML | ![]() | 82.5 KB | Display | |
Data in CIF | ![]() | 117.7 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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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS oper:
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Components
#1: Protein | Mass: 53565.133 Da / Num. of mol.: 4 / Mutation: YES Source method: isolated from a genetically manipulated source Details: THIS MUTANT DOES NOT CONTAIN A 4-METHYLIDENE-IMIDAZOLE-5-ONE GROUP. Source: (gene. exp.) ![]() ![]() ![]() #2: Chemical | ChemComp-GOL / #3: Chemical | ChemComp-SO4 / #4: Water | ChemComp-HOH / | Compound details | CHAIN A, B, C, D ENGINEERED MUTATION CYS273ALA, PHE329GLY MUTANT F329G IS UNABLE TO FORM THE ...CHAIN A, B, C, D ENGINEERED | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.75 Å3/Da / Density % sol: 55.29 % | ||||||||||||||||||||||||||||||||||||
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Crystal grow | pH: 8.1 Details: CRYSTALLIZED FROM 2.0 M (NH4)2SO4, 1 % GLYCEROL, 2 % PEG 400, 0.1 M HEPES AT PH 8.1. 20 % (V/V) GLYCEROL WERE USED AS CRYOPROTECTANT | ||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS pH: 3.85 / Method: vapor diffusion, hanging drop / Details: Schwede, T.F., (1999) Protein Eng., 12, 151. | ||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE |
Radiation | Monochromator: GRAPHITE CRYSTAL / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 1.9→25 Å / Num. obs: 138987 / % possible obs: 77 % / Redundancy: 2.5 % / Rmerge(I) obs: 0.045 / Net I/σ(I): 12.6 |
Reflection shell | *PLUS % possible obs: 51 % / Redundancy: 2.5 % / Rmerge(I) obs: 0.12 / Mean I/σ(I) obs: 6.4 |
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Processing
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Refinement | Method to determine structure: OTHER / Resolution: 1.9→25 Å / Cross valid method: THROUGHOUT / σ(F): 0 / Details: RESIDUES 271-276 NOT VISIBLE IN ELECTRON DENSITY
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Refinement step | Cycle: LAST / Resolution: 1.9→25 Å
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Refine LS restraints |
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Software | *PLUS Name: SHELX / Classification: refinement | |||||||||||||||||||||||||||||||||
Refinement | *PLUS Rfactor obs: 0.17 / Rfactor Rwork: 0.17 | |||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | |||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS |