2srt
From Proteopedia
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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 ZN and INH as ligands. This structure superseeds 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
Page seeded by OCA on Mon Nov 12 23:38:13 2007
Categories: Homo sapiens | Single protein | Stromelysin 1 | Connell, J.F.O. | Gooley, P.R. | INH | ZN | Metzincin
