+Open data
-Basic information
Entry | Database: PDB / ID: 2hoh | ||||||
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Title | RIBONUCLEASE T1 (N9A MUTANT) COMPLEXED WITH 2'GMP | ||||||
Components | PROTEIN (RIBONUCLEASE T1) | ||||||
Keywords | HYDROLASE / ENDORIBONUCLEASE / RIBONUCLEASE / ENDONUCLEASE | ||||||
Function / homology | Function and homology information hyphal tip / ribonuclease T1 activity / ribonuclease T1 / cell septum / endonuclease activity / lyase activity / RNA binding Similarity search - Function | ||||||
Biological species | Aspergillus oryzae (mold) | ||||||
Method | X-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 1.9 Å | ||||||
Authors | Langhorst, U. / Loris, R. / Denisov, V.P. / Doumen, J. / Roose, P. / Maes, D. / Halle, B. / Steyaert, J. | ||||||
Citation | Journal: Protein Sci. / Year: 1999 Title: Dissection of the structural and functional role of a conserved hydration site in RNase T1. Authors: Langhorst, U. / Loris, R. / Denisov, V.P. / Doumen, J. / Roose, P. / Maes, D. / Halle, B. / Steyaert, J. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2hoh.cif.gz | 98 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2hoh.ent.gz | 75.8 KB | Display | PDB format |
PDBx/mmJSON format | 2hoh.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ho/2hoh ftp://data.pdbj.org/pub/pdb/validation_reports/ho/2hoh | HTTPS FTP |
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-Related structure data
Related structure data | 1bviC 3hohC 4hohC 5hohC 1rgaS S: Starting model for refinement C: citing same article (ref.) |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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2 |
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3 |
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4 |
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS oper:
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-Components
-Protein , 1 types, 4 molecules ABCD
#1: Protein | Mass: 11051.670 Da / Num. of mol.: 4 / Mutation: N9A Source method: isolated from a genetically manipulated source Details: COMPLEXED WITH GUANOSINE-2'-MONOPHOSPHATE / Source: (gene. exp.) Aspergillus oryzae (mold) / Production host: Escherichia coli (E. coli) / Strain (production host): WK6 / References: UniProt: P00651, EC: 3.1.27.3 |
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-Non-polymers , 5 types, 220 molecules
#2: Chemical | ChemComp-2GP / #3: Chemical | ChemComp-NA / | #4: Chemical | ChemComp-PO4 / | #5: Chemical | #6: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.06 Å3/Da / Density % sol: 40.19 % |
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Crystal grow | pH: 4.2 / Details: 25 MM NAAC PH 4.2 6.25 MM CACL2 45.0 % MPD |
-Data collection
Diffraction | Mean temperature: 293 K |
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Diffraction source | Source: ROTATING ANODE / Type: RIGAKU RU200 / Wavelength: 1.5418 |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Nov 15, 1997 / Details: DUAL SLITS |
Radiation | Monochromator: GRAPHITE / 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→15 Å / Num. obs: 28731 / % possible obs: 98 % / Redundancy: 7.1 % / Rsym value: 0.124 / Net I/σ(I): 13.34 |
Reflection shell | Resolution: 1.9→1.99 Å / Redundancy: 3.9 % / Mean I/σ(I) obs: 4.38 / Rsym value: 0.38 / % possible all: 93 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 1RGA Resolution: 1.9→15 Å / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 0
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Refinement step | Cycle: LAST / Resolution: 1.9→15 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.9→1.99 Å / Total num. of bins used: 8
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Xplor file |
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