1srn: Difference between revisions

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|PDB= 1srn |SIZE=350|CAPTION= <scene name='initialview01'>1srn</scene>, resolution 1.8&Aring;
|PDB= 1srn |SIZE=350|CAPTION= <scene name='initialview01'>1srn</scene>, resolution 1.8&Aring;
|SITE=  
|SITE=  
|LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene>
|LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>
|ACTIVITY= [http://en.wikipedia.org/wiki/Pancreatic_ribonuclease Pancreatic ribonuclease], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.27.5 3.1.27.5]  
|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Pancreatic_ribonuclease Pancreatic ribonuclease], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.27.5 3.1.27.5] </span>
|GENE=  
|GENE=  
|DOMAIN=
|RELATEDENTRY=
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1srn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1srn OCA], [http://www.ebi.ac.uk/pdbsum/1srn PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1srn RCSB]</span>
}}
}}


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[[Category: Edwards, B F.P.]]
[[Category: Edwards, B F.P.]]
[[Category: Martin, P D.]]
[[Category: Martin, P D.]]
[[Category: SO4]]
[[Category: hydrolase (nucleic acid,rna)]]
[[Category: hydrolase (nucleic acid]]
[[Category: rna)]]


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Revision as of 23:46, 30 March 2008

File:1srn.gif


PDB ID 1srn

Drag the structure with the mouse to rotate
, resolution 1.8Å
Ligands:
Activity: Pancreatic ribonuclease, with EC number 3.1.27.5
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



THE REFINED CRYSTAL STRUCTURE OF A FULLY ACTIVE SEMISYNTHETIC RIBONUCLEASE AT 1.8 ANGSTROMS RESOLUTION


OverviewOverview

A fully active, semisynthetic analog of bovine ribonuclease A, comprised of residues 1-118 of the molecule in a noncovalent complex with the synthetic peptide analog of residues 111-124, has been crystallized in space group P3(2)21 from a solution of 1.3 M ammonium sulfate and 3.0 M cesium chloride at pH 5.2. The crystallographic structure was determined by rotation and translation searches utilizing the coordinates for ribonuclease A reported by Wlodawer and Sjolin (Wlodawer, A., and Sjolin, L. (1983) Biochemistry 22, 2720-2728) and has been refined at 1.8-A resolution to an agreement factor of 0.204. Most of the structure of the semisynthetic enzyme closely resembles that found in ribonuclease A with the synthetic peptide replacing the C-terminal elements of the naturally occurring enzyme. No redundant structure is seen; residues 114-118 of the larger chain and residues 111-113 of the peptide do not appear in our map. The positions of those residues at or near the active site are very similar to, if not identical with, those previously reported by others, except for histidine 119, which occupies predominantly the B position seen as a minor site by Borkakoti et al. (Borkakoti, N., Moss, D. S., and Palmer, R. A. (1982) Acta Crystallogr. Sect. B Struct. Crystallogr. Cryst. Chem. 38,2210-2217) and not at all by Wlodawer and Sjolin (1983).

About this StructureAbout this Structure

1SRN is a Protein complex structure of sequences from Bos taurus. Full crystallographic information is available from OCA.

ReferenceReference

The refined crystal structure of a fully active semisynthetic ribonuclease at 1.8-A resolution., Martin PD, Doscher MS, Edwards BF, J Biol Chem. 1987 Nov 25;262(33):15930-8. PMID:3680234

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