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PDBsum entry 1tbs

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Serine protease PDB id
1tbs
Contents
Protein chain
221 a.a.
Ligands
BEN
Metals
_CA
Waters ×531

References listed in PDB file
Key reference
Title Structure determination and refinement of benzamidine-Inhibited trypsin from the north atlantic salmon (salmo salar) at 1.82 a resolution.
Authors A.Smalås, A.Hordvik.
Ref. Acta Crystallogr D Biol Crystallogr, 1993, 49, 318-330. [DOI no: 10.1107/S0907444992013118]
PubMed id 15299521
Abstract
The structure of the serine protease trypsin from the North Atlantic salmon (Salmo salar) has been solved by molecular replacement and refined by restrained least-squares methods to a conventional R factor of 16.4% using diffractometer data in the 6.0-1.82 A resolution range (14 443 reflections greater than 3sigma). The model comprises 1793 protein atoms and 180 solvent molecules which were given unit occupancies, and the average temperature factors for protein atoms and solvent oxygen atoms are 15.2 and 36.8 A(2), respectively. The estimated error in atomic positions is about 0.2 A. The structure of salmon trypsin was solved and refined with only a small part of the amino-acid sequence known. However, a gene sequence of salmon trypsin has later become available. Some discrepancies between this sequence and the sequence obtained from the present X-ray crystal study indicate that the mentioned sequences may correspond to isoenzymes. The structure of salmon trypsin is similar to other trypsins of known structure.
Figure 3.
Fig. 3. Unclear electron density in the region 146­149.
Figure 6.
Fig. 6. The benzamidine molecule in the active­site cleft.
The above figures are reprinted by permission from the IUCr: Acta Crystallogr D Biol Crystallogr (1993, 49, 318-330) copyright 1993.
Secondary reference #1
Title Crystallization and preliminary X-Ray crystallographic studies of benzamidine-Inhibited trypsin from the north atlantic salmon (salmo salar).
Authors A.O.Smalås, A.Hordvik, L.K.Hansen, E.Hough, K.Jynge.
Ref. J Mol Biol, 1990, 214, 355-358.
PubMed id 2380985
Abstract
Secondary reference #2
Title The geometry of the reactive site and of the peptide groups in trypsin, Trypsinogen and its complexes with inhibitors
Authors M.Marquart, J.Walter, J.Deisenhofer, W.Bode, R.Huber.
Ref. acta crystallogr ,sect b, 1983, 39, 480.
PROCHECK
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