+Open data
-Basic information
Entry | Database: PDB / ID: 1htt | ||||||
---|---|---|---|---|---|---|---|
Title | HISTIDYL-TRNA SYNTHETASE | ||||||
Components | HISTIDYL-TRNA SYNTHETASEHistidine—tRNA ligase | ||||||
Keywords | COMPLEX (TRNA SYNTHETASE/HIS-ADENYLATE) / COMPLEX (TRNA SYNTHETASE-HIS-ADENYLATE) / AMINOACYL-TRNA SYNTHASE / LIGASE / SYNTHETASE / COMPLEX (TRNA SYNTHETASE-HIS-ADENYLATE) complex | ||||||
Function / homology | Function and homology information histidine-tRNA ligase / histidine-tRNA ligase activity / histidyl-tRNA aminoacylation / protein homodimerization activity / ATP binding / cytosol Similarity search - Function | ||||||
Biological species | Escherichia coli (E. coli) | ||||||
Method | X-RAY DIFFRACTION / MIR, DENSITY AVERAGING / Resolution: 2.6 Å | ||||||
Authors | Arnez, J.G. / Harris, D.C. / Mitschler, A. / Rees, B. / Francklyn, C.S. / Moras, D. | ||||||
Citation | Journal: EMBO J. / Year: 1995 Title: Crystal structure of histidyl-tRNA synthetase from Escherichia coli complexed with histidyl-adenylate. Authors: Arnez, J.G. / Harris, D.C. / Mitschler, A. / Rees, B. / Francklyn, C.S. / Moras, D. #1: Journal: J.Mol.Biol. / Year: 1994 Title: Crystallization of Histidyl-tRNA Synthetase from Escherichia Coli Authors: Francklyn, C. / Harris, D. / Moras, D. #2: Journal: J.Biol.Chem. / Year: 1985 Title: Primary Structure of Histidine-tRNA Synthetase and Characterization of Hiss Transcripts Authors: Freedman, R. / Gibson, B. / Donovan, D. / Biemann, K. / Eisenbeis, S. / Parker, J. / Schimmel, P. | ||||||
History |
|
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
---|
-Downloads & links
-Download
PDBx/mmCIF format | 1htt.cif.gz | 295.7 KB | Display | PDBx/mmCIF format |
---|---|---|---|---|
PDB format | pdb1htt.ent.gz | 235 KB | Display | PDB format |
PDBx/mmJSON format | 1htt.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ht/1htt ftp://data.pdbj.org/pub/pdb/validation_reports/ht/1htt | HTTPS FTP |
---|
-Related structure data
Similar structure data |
---|
-Links
-Assembly
Deposited unit |
| ||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
1 |
| ||||||||||||||||
2 |
| ||||||||||||||||
Unit cell |
| ||||||||||||||||
Noncrystallographic symmetry (NCS) | NCS oper:
|
-Components
#1: Protein | Mass: 46954.121 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / Strain: JM109 / Plasmid: PHRS-7 / Gene (production host): HISS / Production host: Escherichia coli (E. coli) References: UniProt: P04804, UniProt: P60906*PLUS, histidine-tRNA ligase #2: Chemical | ChemComp-HIS / #3: Chemical | ChemComp-AMP / #4: Water | ChemComp-HOH / | |
---|
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
---|
-Sample preparation
Crystal | Density Matthews: 3.49 Å3/Da / Density % sol: 68 % | ||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Crystal grow | pH: 7.4 / Details: pH 7.4 | ||||||||||||||||||||||||||||||
Crystal grow | *PLUS Method: vapor diffusion, sitting drop | ||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
|
-Data collection
Diffraction | Mean temperature: 275 K |
---|---|
Diffraction source | Source: ROTATING ANODE / Type: SIEMENS / Wavelength: 1.5418 |
Detector | Type: MAR scanner 300 mm plate / Detector: IMAGE PLATE / Date: Feb 9, 1994 |
Radiation | Monochromator: GRAPHITE HUBER FLAT #151 / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.6→26 Å / Num. obs: 54820 / % possible obs: 69.4 % / Observed criterion σ(I): 0 / Redundancy: 1.7 % / Rmerge(I) obs: 0.057 / Net I/σ(I): 10.1 |
Reflection shell | Resolution: 2.6→2.74 Å / Redundancy: 1.5 % / Rmerge(I) obs: 0.231 / Mean I/σ(I) obs: 2.8 / % possible all: 55.7 |
-Processing
Software |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method to determine structure: MIR, DENSITY AVERAGING / Resolution: 2.6→8 Å / σ(F): 2
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 33 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine analyze | Luzzati coordinate error obs: 0.4 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.6→8 Å
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Software | *PLUS Name: X-PLOR / Version: 3.1 / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
|