2srt

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2srt

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CATALYTIC DOMAIN OF HUMAN STROMELYSIN-1 AT PH 5.5 AND 40OC COMPLEXED WITH INHIBITOR

Contents

Overview

The three-dimensional structure of the catalytic domain of stromelysin-1 complexed with an N-carboxyl alkyl inhibitor has been determined by NMR methods. The global fold consists of three helices, a five stranded beta-sheet and a methionine located in a turn near the catalytic histidines, classifying stromelysin-1 as a metzincin. Stromelysin-1 is unique in having two independent zinc binding sites: a catalytic site and a structural site. The inhibitor binds in an extended conformation. The S1' subsite is a deep hydrophobic pocket, whereas S2' appears shallow and S3' open.

Disease

Known diseases associated with this structure: Coronary heart disease, susceptibility to OMIM:[185250]

About this Structure

2SRT is a Single protein structure of sequence from Homo sapiens with and as ligands. This structure supersedes the now removed PDB entry 1SRT. Active as Stromelysin 1, with EC number 3.4.24.17 Full crystallographic information is available from OCA.

Reference

The NMR structure of the inhibited catalytic domain of human stromelysin-1., Gooley PR, O'Connell JF, Marcy AI, Cuca GC, Salowe SP, Bush BL, Hermes JD, Esser CK, Hagmann WK, Springer JP, et al., Nat Struct Biol. 1994 Feb;1(2):111-8. PMID:7656014

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