1a0j Summary



The structure was published by Schroder, H.K., Willassen, N.P., and Smalas, A.O., in 1998 in a paper entitled "Structure of a non-psychrophilic trypsin from a cold-adapted fish species." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.7 Å and deposited in 1997.

The experimental data on which the structure is based was also deposited.

This PDB entry contains multiple copies of the structure of TRYPSIN.

It also contains one or more heterogenic compounds (e.g., ligands, co-factors, ions, modified amino acids, etc.); see here for a complete list.

The molecule has more than one probable quaternary state observed. For more details see the quaternary structure page.

The following tables show cross-reference information to other databases (to obtain a list of all PDB entries sharing the same property or classification, click on the magnifying glass icon):

Chain Name UniProt Name of source organism % of UniProt sequence present in the sample Residues in the sample molecules % of residues observed
A TRYPSIN P35033 (16-238) (TRY3_SALSA)search Salmo salarsearch 97% 223 100%
B TRYPSIN P35033 (16-238) (TRY3_SALSA)search Salmo salarsearch 97% 223 100%
C TRYPSIN P35033 (16-238) (TRY3_SALSA)search Salmo salarsearch 97% 223 100%
D TRYPSIN P35033 (16-238) (TRY3_SALSA)search Salmo salarsearch 97% 223 100%

This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P35033 (16 - 238) TRYPSIN Salmo salar

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A, B, C, D (P35033) Eukaryotic proteasessearch Trypsin-like serine proteasessearch PF00089: Trypsinsearch

Chain ID Molecular function (GO) Cellular component (GO) Biological process (GO)
A, B, C, D (P35033) catalytic activitysearch serine-type endopeptidase activitysearch peptidase activitysearch serine-type peptidase activitysearch hydrolase activitysearch metal ion bindingsearch extracellular regionsearch proteolysissearch digestionsearch

Chain InterPro annotation
A, B, C, D Peptidase S1search Peptidase S1A, chymotrypsin-typesearch Trypsin-like cysteine/serine peptidase domainsearch Peptidase S1, trypsin family, active sitesearch