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Open data
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Basic information
Entry | Database: PDB / ID: 4bir | ||||||
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Title | RIBONUCLEASE T1: FREE HIS92GLN MUTANT | ||||||
![]() | GUANYL-SPECIFIC RIBONUCLEASE T1 | ||||||
![]() | ENDORIBONUCLEASE / HYDROLASE / RIBONUCLEASE / HIS TO GLN MUTANT | ||||||
Function / homology | ![]() hyphal tip / ribonuclease T1 activity / ribonuclease T1 / cell septum / endonuclease activity / lyase activity / RNA binding Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Doumen, J. / Steyaert, J. | ||||||
![]() | ![]() Title: Role of histidine-40 in ribonuclease T1 catalysis: three-dimensionalstructures of the partially active His40Lys mutant. Authors: Zegers, I. / Verhelst, P. / Choe, H.W. / Steyaert, J. / Heinemann, U. / Saenger, W. / Wyns, L. #1: ![]() Title: His92Ala Mutation in Ribonuclease T1 Induces Segmental Flexibility. An X-Ray Study Authors: Koellner, G. / Choe, H.W. / Heinemann, U. / Grunert, H.P. / Zouni, A. / Hahn, U. / Saenger, W. #2: ![]() Title: Three-Dimensional Structure of the Ribonuclease T1 2'-Gmp Complex at 1.9-A Resolution Authors: Arni, R. / Heinemann, U. / Tokuoka, R. / Saenger, W. #3: ![]() Title: Specific Protein-Nucleic Acid Recognition in Ribonuclease T1-2'-Guanylic Acid Complex. An X-Ray Study Authors: Heinemann, U. / Saenger, W. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 34.8 KB | Display | ![]() |
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PDB format | ![]() | 25 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 362 KB | Display | ![]() |
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Full document | ![]() | 377 KB | Display | |
Data in XML | ![]() | 5.7 KB | Display | |
Data in CIF | ![]() | 8.2 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 2aadC ![]() 2aaeC ![]() 1rgaS 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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Unit cell |
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Components
#1: Protein | Mass: 11084.676 Da / Num. of mol.: 1 / Mutation: H92Q Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
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#2: Chemical | ChemComp-CA / |
#3: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.11 Å3/Da / Density % sol: 41.71 % |
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Crystal grow | pH: 4.2 / Details: pH 4.2 |
-Data collection
Diffraction | Mean temperature: 293 K |
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Diffraction source | Type: ENRAF-NONIUS / Wavelength: 1.5418 |
Detector | Type: ENRAF-NONIUS FAST / Detector: DIFFRACTOMETER / Date: May 5, 1994 / Details: COLLIMATOR |
Radiation | Monochromator: GRAPHITE(002) / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 1.7→15 Å / Num. obs: 10404 / % possible obs: 93.9 % / Observed criterion σ(I): 3 / Redundancy: 4.6 % / Rsym value: 0.079 / Net I/σ(I): 6.5 |
Reflection shell | Resolution: 1.68→1.73 Å / Redundancy: 2.18 % / Mean I/σ(I) obs: 3 / Rsym value: 0.257 / % possible all: 51.3 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 1RGA Resolution: 1.7→10 Å / Cross valid method: THROUGHOUT / σ(F): 0
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Refinement step | Cycle: LAST / Resolution: 1.7→10 Å
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Refine LS restraints |
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