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- PDB-1h1c: Histidinol-phosphate aminotransferase (HisC) from Thermotoga maritima -
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Open data
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Basic information
Entry | Database: PDB / ID: 1h1c | ||||||
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Title | Histidinol-phosphate aminotransferase (HisC) from Thermotoga maritima | ||||||
![]() | HISTIDINOL-PHOSPHATE AMINOTRANSFERASE | ||||||
![]() | TRANSFERASE / AMINOTRANSFERASE / HISTIDINE BIOSYNTHESIS | ||||||
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. / 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 | ![]() | 268.3 KB | Display | ![]() |
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PDB format | ![]() | 227.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 474.6 KB | Display | ![]() |
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Full document | ![]() | 555.3 KB | Display | |
Data in XML | ![]() | 58.8 KB | Display | |
Data in CIF | ![]() | 78.8 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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2 | ![]()
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS oper:
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Components
#1: Protein | Mass: 39772.996 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Details: RESIDUE 202 LYSINE-PYRIDOXAL-5'-PHOSPHATE / Source: (gene. exp.) ![]() ![]() ![]() ![]() References: UniProt: Q9X0D0, histidinol-phosphate transaminase #2: Chemical | ChemComp-PLP / #3: Water | ChemComp-HOH / | Compound details | CONVERTS L-HISTIDINOL-PHOSPHATE + 2-OXOGLUTARATE TO 3- (IMIDAZOL-4-YL)-2-OXOPROPYL PHOSPHATE + L- ...CONVERTS L-HISTIDINOL | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.53 Å3/Da / Density % sol: 51 % | ||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | pH: 7 / Details: pH 7.00 | ||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 20 ℃ / pH: 7.5 / Method: vapor diffusion, sitting drop | ||||||||||||||||||||||||||||||||||||||||||
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: CCD / Date: Dec 15, 2001 | ||||||||||||
Radiation | Protocol: MAD / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | ||||||||||||
Radiation wavelength |
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Reflection | Resolution: 2.85→20 Å / Num. obs: 29624 / % possible obs: 99.8 % / Redundancy: 4.1 % / Rmerge(I) obs: 0.092 / Net I/σ(I): 6.98 | ||||||||||||
Reflection shell | Resolution: 2.85→2.95 Å / Redundancy: 3.3 % / Rmerge(I) obs: 0.381 / Mean I/σ(I) obs: 2.38 / % possible all: 95.7 | ||||||||||||
Reflection | *PLUS Highest resolution: 2.85 Å / Lowest resolution: 20 Å |
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Processing
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Refinement | Method to determine structure: ![]()
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Displacement parameters | Biso mean: 21.92 Å2
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Refinement step | Cycle: LAST / Resolution: 2.85→20 Å
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Refine LS restraints |
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Refine LS restraints NCS | NCS model details: RESTRAINTS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
LS refinement shell | Resolution: 2.85→2.914 Å / Total num. of bins used: 20 /
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Refinement | *PLUS Lowest resolution: 20 Å / % reflection Rfree: 9.3 % / Rfactor Rwork: 0.22 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS |