1amh

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|PDB= 1amh |SIZE=350|CAPTION= <scene name='initialview01'>1amh</scene>, resolution 2.5&Aring;
|PDB= 1amh |SIZE=350|CAPTION= <scene name='initialview01'>1amh</scene>, resolution 2.5&Aring;
|SITE= <scene name='pdbsite=CAA:Catalytic+Site'>CAA</scene> and <scene name='pdbsite=CAB:Catalytic+Site'>CAB</scene>
|SITE= <scene name='pdbsite=CAA:Catalytic+Site'>CAA</scene> and <scene name='pdbsite=CAB:Catalytic+Site'>CAB</scene>
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|LIGAND= <scene name='pdbligand=CA:CALCIUM ION'>CA</scene>
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|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Trypsin Trypsin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.4 3.4.21.4]
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Trypsin Trypsin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.4 3.4.21.4] </span>
|GENE=
|GENE=
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|DOMAIN=
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1amh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1amh OCA], [http://www.ebi.ac.uk/pdbsum/1amh PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1amh RCSB]</span>
}}
}}
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[[Category: Naray-Szabo, G.]]
[[Category: Naray-Szabo, G.]]
[[Category: Szabo, E.]]
[[Category: Szabo, E.]]
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[[Category: CA]]
 
[[Category: activation domain]]
[[Category: activation domain]]
[[Category: serine protease]]
[[Category: serine protease]]
[[Category: substrate specificity hydrolase]]
[[Category: substrate specificity hydrolase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 09:59:32 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:43:21 2008''

Revision as of 15:43, 30 March 2008


PDB ID 1amh

Drag the structure with the mouse to rotate
, resolution 2.5Å
Sites: and
Ligands:
Activity: Trypsin, with EC number 3.4.21.4
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



UNCOMPLEXED RAT TRYPSIN MUTANT WITH ASP 189 REPLACED WITH SER (D189S)


Overview

Structure-based mutational analysis of serine protease specificity has produced a large database of information useful in addressing biological function and in establishing a basis for targeted design efforts. Critical issues examined include the function of water molecules in providing strength and specificity of binding, the extent to which binding subsites are interdependent, and the roles of polypeptide chain flexibility and distal structural elements in contributing to specificity profiles. The studies also provide a foundation for exploring why specificity modification can be either straightforward or complex, depending on the particular system.

About this Structure

1AMH is a Single protein structure of sequence from Rattus rattus. Full crystallographic information is available from OCA.

Reference

Structural basis of substrate specificity in the serine proteases., Perona JJ, Craik CS, Protein Sci. 1995 Mar;4(3):337-60. PMID:7795518

Page seeded by OCA on Sun Mar 30 18:43:21 2008

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