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PDBsum entry 1qcp
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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Structure of the rwj-51084-Bovine pancreatic beta-Trypsin complex at 1.8 a.
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Authors
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R.Recacha,
M.Carson,
M.J.Costanzo,
B.Maryanoff,
L.J.Delucas,
D.Chattopadhyay.
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Ref.
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Acta Crystallogr D Biol Crystallogr, 1999,
55,
1785-1791.
[DOI no: ]
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PubMed id
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Abstract
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The three-dimensional structure of bovine pancreatic trypsin complexed with the
inhibitor RWJ-51084 has been determined at 1.8 A resolution. These crystals
belong to the trigonal space group P3(1)21, with unit-cell parameters a = b =
53.43, c = 107.76 A. The refined R and R(free) values are 0.175 and 0.237,
respectively. The carbonyl group bonded to the benzothiazole group of the
inhibitor is covalently linked to the hydroxyl O atom of Ser195, forming a
tetrahedral intermediate hemiketal structure. The other carbonyl O atom of the
inhibitor forms a hydrogen bond with the Gln192 side-chain amide group. The
benzothiazole group is oriented with the aromatic N atom of RWJ-51084 accepting
a hydrogen bond from His57 NE2. The arginine side chain of the inhibitor extends
into the deep and narrow pocket of the S1 specificity site of trypsin, forming a
network of hydrogen bonds.
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Figure 1.
Figure 1 Chemical formula of RWJ-51084.
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Figure 2.
Figure 2 Ribbon plot of the complex formed between trypsin and
RWJ-51084. Side chains of the catalytic triad residues His57,
Asp102 and Ser195 are explicitly shown, as well as the calcium
cation on the right. All figures prepared with Ribbons,
[67]http://www.cmc.uab.edu/ribbons (Carson, 1997[68] [Carson, M.
(1997). Methods Enzymol. 277, 493-505.]-[69][bluearr.gif] ).
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The above figures are
reprinted
by permission from the IUCr:
Acta Crystallogr D Biol Crystallogr
(1999,
55,
1785-1791)
copyright 1999.
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