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Open data
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Basic information
Entry | Database: PDB / ID: 1rnc | ||||||
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Title | NEWLY OBSERVED BINDING MODE IN PANCREATIC RIBONUCLEASE | ||||||
![]() | RIBONUCLEASE A![]() | ||||||
![]() | HYDROLASE(ENDORIBONUCLEASE) | ||||||
Function / homology | ![]() ![]() ![]() ![]() ![]() Similarity search - Function | ||||||
Biological species | ![]() ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Aguilar, C.F. / Thomas, P.J. / Mills, A. / Moss, D.S. / Palmer, R.A. | ||||||
![]() | ![]() Title: Newly observed binding mode in pancreatic ribonuclease. Authors: Aguilar, C.F. / Thomas, P.J. / Mills, A. / Moss, D.S. / Palmer, R.A. #1: ![]() Title: Novel Non-Productively Bound Ribonuclease Inhibitor Complexes-High Resolution X-Ray Refinement Studies on the Binding of Rnase-A to Cytidylyl-2',5'-Guanosine (2',5'Cpg) and Deoxycytidylyl- ...Title: Novel Non-Productively Bound Ribonuclease Inhibitor Complexes-High Resolution X-Ray Refinement Studies on the Binding of Rnase-A to Cytidylyl-2',5'-Guanosine (2',5'Cpg) and Deoxycytidylyl-3',5'-Guanosine (3',5'Dcpdg) Authors: Aguilar, C.F. / Thomas, P.J. / Moss, D.S. / Mills, A. / Palmer, R.A. #2: ![]() Title: X-Ray Refinement Study on the Binding of Cytidylic Acid (2'-Cmp) to Ribonuclease-A Authors: Howlin, B. / Harris, G.W. / Moss, D.S. / Palmer, R.A. #3: ![]() Title: An X-Ray Refinement Study on the Binding of Ribonuclease-A to Cytidine-N(3)-Oxide 2'-Phosphate Authors: Palmer, R.A. / Moss, D.S. / Haneef, I. / Borkakoti, N. #4: ![]() Title: The Refined Structure of Ribonuclease-A at 1.45 Angstroms Resolution Authors: Borkakoti, N. / Moss, D.S. / Stanford, M.J. / Palmer, R.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 | ![]() | 32.8 KB | Display | ![]() |
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PDB format | ![]() | 25 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
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Links
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Assembly
Deposited unit | ![]()
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1 |
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Unit cell |
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Atom site foot note | 1: RESIDUES PRO 93 AND PRO 114 ARE CIS PROLINES. 2: PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION GLU 111 - GLY 112: 149.724 |
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Components
#1: Protein | ![]() Mass: 13708.326 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
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#2: Chemical | ChemComp-SO4 / ![]() |
#3: Chemical | ChemComp-5GP / ![]() |
#4: Water | ChemComp-HOH / ![]() |
Compound details | THE MOST INTERESTING FEATURE IN THIS STRUCTURE IS THE MODE OF BINDING OF THE CPG INHIBITOR TO THE ...THE MOST INTERESTIN |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.18 Å3/Da / Density % sol: 43.61 % |
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Crystal grow![]() | *PLUS Method: unknown / PH range low: 5.7 / PH range high: 5.2 |
Components of the solutions | *PLUS Conc.: 47 %(v/v) / Common name: ethanol |
-Data collection
Radiation | Scattering type: x-ray |
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Radiation wavelength | Relative weight: 1 |
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Processing
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Refinement | Highest resolution: 1.5 Å Details: THE INHIBITOR AND SULFATE ANION WERE REFINED USING GROUP OCCUPANCIES.
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Refinement step | Cycle: LAST / Highest resolution: 1.5 Å
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Refine LS restraints |
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Refinement | *PLUS Highest resolution: 1.5 Å / Num. reflection obs: 17855 / Rfactor obs: 0.21 | ||||||||||||
Solvent computation | *PLUS | ||||||||||||
Displacement parameters | *PLUS | ||||||||||||
Refine LS restraints | *PLUS Type: p_angle_d / Dev ideal: 1.23 |