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1hym
From Proteopedia
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|PDB= 1hym |SIZE=350|CAPTION= <scene name='initialview01'>1hym</scene> | |PDB= 1hym |SIZE=350|CAPTION= <scene name='initialview01'>1hym</scene> | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=ACE:ACETYL GROUP'>ACE</scene> | + | |LIGAND= <scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1hym FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hym OCA], [http://www.ebi.ac.uk/pdbsum/1hym PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1hym RCSB]</span> | ||
}} | }} | ||
| Line 26: | Line 29: | ||
[[Category: Krishnamoorthi, R.]] | [[Category: Krishnamoorthi, R.]] | ||
[[Category: Prakash, O.]] | [[Category: Prakash, O.]] | ||
| - | [[Category: ACE]] | ||
[[Category: hydrolase (serine proteinase)]] | [[Category: hydrolase (serine proteinase)]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:12:04 2008'' |
Revision as of 18:12, 30 March 2008
| |||||||
| Ligands: | |||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
HYDROLYZED TRYPSIN INHIBITOR (CMTI-V, MINIMIZED AVERAGE NMR STRUCTURE)
Overview
Reactive-site (Lys44-Asp45 peptide bond) hydrolyzed Cucurbita maxima trypsin inhibitor-V (CMTI-V*) was prepared and characterized: In comparison to the intact form, CMTI-V* exhibited markedly reduced inhibitory properties and binding affinities toward trypsin and human blood coagulation factor XIIa. The equilibrium constant of trypsin-catalyzed hydrolysis, Khyd, defined as [CMTI-V*]/[CMTI-V], was measured to be approximately 9.4 at 25 degrees C (delta G degrees = -1.3 kcal.mol-1). From the temperature dependence of delta G degrees, the following thermodynamic parameters were estimated: delta H degrees = 1.6 kcal.mol-1 and delta S degrees = 9.8 eu. In order to understand the functional and thermodynamic differences between the two forms, the three-dimensional solution structure of CMTI-V* was determined by a combined approach of NMR, distance geometry, and simulated annealing methods. Thus, following sequence-specific and stereospecific resonance assignments, including those of beta-, gamma-, delta-, and epsilon-hydrogens and valine methyl hydrogens, 809 interhydrogen distances and 123 dihedral angle constraints were determined, resulting in the computation and energy-minimization of 20 structures for CMTI-V*. The average root mean squared deviation in position for equivalent atoms between the 20 individual structures and the mean structure obtained by averaging their coordinates is 0.67 +/- 0.15 A for the main chain atoms and 1.19 +/- 0.23 A for all the non-hydrogen atoms of residues 5-40 and residues 48-67.(ABSTRACT TRUNCATED AT 250 WORDS)
About this Structure
1HYM is a Protein complex structure of sequences from Cucurbita maxima. Full crystallographic information is available from OCA.
Reference
Reactive-site hydrolyzed Cucurbita maxima trypsin inhibitor-V: function, thermodynamic stability, and NMR solution structure., Cai M, Gong Y, Prakash O, Krishnamoorthi R, Biochemistry. 1995 Sep 26;34(38):12087-94. PMID:7547948
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