PDBsum entry 1tbs

Serine protease

PDB id: 1tbs

Contents

Protein chain

221 a.a.

Ligands

BEN

Metals

_CA

Waters ×531

Obsolete entry

PDB id:

1tbs

Name:

Serine protease

Title:

Crystal structure determination and refinement of benzamidine-inhibited trypsin from the north atlantic salmon (salmo salar) at 1.82 angstroms resolution

Structure:

Chain: null. Engineered: yes

Source:

not given

Resolution:

1.80Å R-factor: 0.164

Authors:

A.O.Smalas

Key ref:

A.Smalås and A.Hordvik (1993). Structure determination and refinement of benzamidine-inhibited trypsin from the North Atlantic salmon (Salmo salar) at 1.82 A resolution. Acta Crystallogr D Biol Crystallogr, 49, 318-330. PubMed id: 15299521 DOI: 10.1107/S0907444992013118

Date:

10-Jul-92 Release date: 31-Jan-94

Protein chain

No UniProt id for this chain

Struc: 221 a.a.

DOI no: 10.1107/S0907444992013118

Acta Crystallogr D Biol Crystallogr 49:318-330 (1993)

PubMed id: 15299521

Structure determination and refinement of benzamidine-inhibited trypsin from the North Atlantic salmon (Salmo salar) at 1.82 A resolution.

A.Smalås, A.Hordvik.

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.

Selected figure(s)

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.

Figures were selected by an automated process.