1trl Summary

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NMR SOLUTION STRUCTURE OF THE C-TERMINAL FRAGMENT 255-316 OF THERMOLYSIN: A DIMER FORMED BY SUBUNITS HAVING THE NATIVE STRUCTURE

The structure was published by Rico, M., Jimenez, M.A., Gonzalez, C., De Filippis, V., and Fontana, A., in 1994 in a paper entitled "NMR solution structure of the C-terminal fragment 255-316 of thermolysin: a dimer formed by subunits having the native structure." (abstract).

The structure was determined using NMR spectroscopy and deposited in 1994.

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

This PDB entry contains multiple copies of the structure of THERMOLYSIN FRAGMENT 255 - 316.

The molecule most likely forms homodimers.

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 THERMOLYSIN FRAGMENT 255 - 316 P00800 (487-548) (THER_BACTH)search Bacillus thermoproteolyticussearch < 90% 62 100%
B THERMOLYSIN FRAGMENT 255 - 316 P00800 (487-548) (THER_BACTH)search Bacillus thermoproteolyticussearch < 90% 62 100%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P00800 (487 - 548) THERMOLYSIN FRAGMENT 255 - 316 Bacillus thermoproteolyticus

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A, B C-terminal fragment of thermolysinsearch Neutral Protease Domain 2search Thermolysin metallopeptidase, alpha-helical domainsearch

Chain ID Molecular function (GO)
A, B (P00800) metalloendopeptidase activitysearch

Chain InterPro annotation
A, B Peptidase M4, C-terminalsearch