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- PDB-1uu0: Histidinol-phosphate aminotransferase (HisC) from Thermotoga mari... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1uu0 | ||||||
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Title | Histidinol-phosphate aminotransferase (HisC) from Thermotoga maritima (Apo-form) | ||||||
![]() | HISTIDINOL-PHOSPHATE AMINOTRANSFERASE | ||||||
![]() | TRANSFERASE / HISTIDINE BIOSYNTHESIS / AMINOTRANSFERASE / PYRIDOXAL PHOSPHATE | ||||||
Function / homology | ![]() histidinol-phosphate transaminase / histidinol-phosphate transaminase activity / L-histidine biosynthetic process / pyridoxal phosphate binding / protein homodimerization activity Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Vega, M.C. / Fernandez, F.J. / Lehmann, F. / Wilmanns, M. | ||||||
![]() | ![]() Title: Structural Studies of the Catalytic Reaction Pathway of a Hyperthermophilic Histidinol-Phosphate Aminotransferase Authors: Fernandez, F.J. / Vega, M.C. / Lehmann, F. / Sandmeier, E. / Gehring, H. / Christen, P. / Wilmanns, M. #1: ![]() Title: Crystal Structure of Histidinol Phosphate Aminotransferase (Hisc) from Escherichia Coli, and its Covalent Complex with Pyridoxal-5'-Phosphate and L-Histidinol Phosphate Authors: Sivaraman, J. / Li, Y. / Larocque, R. / Schrag, J.D. / Cygler, M. / Matte, A. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 269 KB | Display | ![]() |
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PDB format | ![]() | 220.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 467.7 KB | Display | ![]() |
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Full document | ![]() | 558.1 KB | Display | |
Data in XML | ![]() | 58.8 KB | Display | |
Data in CIF | ![]() | 78.9 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1h1cSC ![]() 1uu1C ![]() 1uu2C 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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1 | ![]()
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2 | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 39350.945 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Details: PHOSPHATE ANION ATTACHED PER CHAIN / Source: (gene. exp.) ![]() ![]() ![]() ![]() References: UniProt: Q9X0D0, histidinol-phosphate transaminase #2: Chemical | ChemComp-PO4 / #3: Water | ChemComp-HOH / | Compound details | CATALYTIC ACTIVITY: L-HISTIDINOL-PHOSPHATE + 2-OXOGLUTARATE = 3- (IMIDAZOL-4-YL)-2-OXOPROPYL ...CATALYTIC ACTIVITY: L-HISTIDINOL | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.4 Å3/Da / Density % sol: 44.7 % |
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Crystal grow | pH: 7 / Details: pH 7.00 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Feb 15, 2003 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.8416 Å / Relative weight: 1 |
Reflection | Resolution: 2.85→20 Å / Num. obs: 31839 / % possible obs: 95 % / Redundancy: 2.5 % / Biso Wilson estimate: 45.8 Å2 / Rmerge(I) obs: 0.071 / Net I/σ(I): 13.5 |
Reflection shell | Resolution: 2.85→2.95 Å / Redundancy: 2.3 % / Rmerge(I) obs: 0.294 / Mean I/σ(I) obs: 3.6 / % possible all: 97.9 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 1H1C Resolution: 2.85→24.11 Å / Rfactor Rfree error: 0.005 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 0
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Solvent computation | Solvent model: FLAT MODEL / ksol: 0.25071 e/Å3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 48.1 Å2
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 2.85→24.11 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.85→3.03 Å / Rfactor Rfree error: 0.015 / Total num. of bins used: 6
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Xplor file |
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