8tln Summary

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PDB entry 8tln (supersedes 3tln)

STRUCTURAL COMPARISON SUGGESTS THAT THERMOLYSIN AND RELATED NEUTRAL PROTEASES UNDERGO HINGE-BENDING MOTION DURING CATALYSIS

The structure was published by Holland, D.R., Tronrud, D.E., Pley, H.W., et al., Jansonius, J.N., McKay, D.B., and Matthews, B.W., in 1992 in a paper entitled "Structural comparison suggests that thermolysin and related neutral proteases undergo hinge-bending motion during catalysis." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.6 Å and deposited in 1993.

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

The PDB entry contains the structure of THERMOLYSIN. This molecule has the UniProt identifier P00800 (THER_BACTH)search. The sample contained 316 residues which is < 90% of the natural sequence. Out of 316 residues 316 were observed and are deposited in the PDB.

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 is most likely monomeric.

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
E THERMOLYSIN P00800 (233-548) (THER_BACTH)search Bacillus thermoproteolyticussearch < 90% 316 100%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P00800 (233 - 548) THERMOLYSIN Bacillus thermoproteolyticus

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
E Thermolysin-likesearch Elastase; domain 1search, Neutral Protease Domain 2search Thermolysin metallopeptidase, catalytic domainsearch, Thermolysin metallopeptidase, alpha-helical domainsearch

Chain ID Molecular function (GO) Biological process (GO)
E (P00800) metalloendopeptidase activitysearch proteolysissearch

Chain InterPro annotation
E Peptidase M4, C-terminalsearch Peptidase M4 domainsearch Peptidase M4search