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- PDB-1eb4: Histidine Ammonia-Lyase (HAL) Mutant F329A from Pseudomonas putida -
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Open data
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Basic information
Entry | Database: PDB / ID: 1eb4 | |||||||||
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Title | Histidine Ammonia-Lyase (HAL) Mutant F329A from Pseudomonas putida | |||||||||
![]() | HISTIDINE AMMONIA-LYASE | |||||||||
![]() | LYASE / AMMONIA-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 | ![]() | 116.5 KB | Display | ![]() |
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PDB format | ![]() | 88 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 452.9 KB | Display | ![]() |
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Full document | ![]() | 462 KB | Display | |
Data in XML | ![]() | 24.4 KB | Display | |
Data in CIF | ![]() | 36 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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1 | ![]()
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Unit cell |
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Components on special symmetry positions |
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Components
#1: Protein | Mass: 53543.129 Da / Num. of mol.: 1 / Mutation: YES Source method: isolated from a genetically manipulated source Details: ALA 142, SER 143 AND GLY 144 ARE FORMING AN 4-METHYLIDENE-IMIDAZOLE-5-ONE GROUP (MDO).THE CARBONYL CARBON OF ALA 142 IS BONDED TO THE NITROGEN OF GLY 144. THE CARBONYL OXYGEN OF ALA 142 IS ...Details: ALA 142, SER 143 AND GLY 144 ARE FORMING AN 4-METHYLIDENE-IMIDAZOLE-5-ONE GROUP (MDO).THE CARBONYL CARBON OF ALA 142 IS BONDED TO THE NITROGEN OF GLY 144. THE CARBONYL OXYGEN OF ALA 142 IS DELETED. THE SIDE CHAIN OF SER 143 IS DEHYDRATED. Source: (gene. exp.) ![]() ![]() ![]() |
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#2: Chemical | ChemComp-SO4 / |
#3: Chemical | ChemComp-GOL / |
#4: Water | ChemComp-HOH / |
Compound details | ENGINEERED |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.78 Å3/Da / Density % sol: 55.83 % | ||||||||||||||||||||||||||||||||||||
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Crystal grow | pH: 8.1 Details: 2.0 M (NH4)2 SO4, 1 % GLYCEROL, 2 % PEG 400, 0.1 M HEPES AT PH 8.1. 20 % (V/V) GLYCEROL 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: 2→25 Å / Num. obs: 39112 / % possible obs: 96 % / Redundancy: 3.8 % / Rmerge(I) obs: 0.13 / Net I/σ(I): 5.4 |
Reflection | *PLUS Rmerge(I) obs: 0.134 |
Reflection shell | *PLUS % possible obs: 99 % / Redundancy: 3.6 % / Rmerge(I) obs: 0.31 / Mean I/σ(I) obs: 2.4 |
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Processing
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Refinement | Method to determine structure: OTHER / Resolution: 2→25 Å / Cross valid method: THROUGHOUT / σ(F): 0
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Refinement step | Cycle: LAST / Resolution: 2→25 Å
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Refine LS restraints |
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Software | *PLUS Name: SHELX / Classification: refinement | |||||||||||||||||||||||||||||||||
Refinement | *PLUS Rfactor Rwork: 0.171 | |||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | |||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS |