2SRT

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

Replaces:  1SRT

Summary for 2SRT

• Entry DOI: 10.2210/pdb2srt/pdb
• Descriptor: STROMELYSIN-1, ZINC ION, N-(R-CARBOXY-ETHYL)-ALPHA-(S)-(2-PHENYLETHYL)GLYCYL-L-ARGININE-N-PHENYLAMIDE (3 entities in total)
• Functional Keywords: metzincin, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor
• Biological source: Homo sapiens (human)
• Cellular location: Secreted, extracellular space, extracellular matrix (Probable): P08254
• Total number of polymer chains: 1
• Total formula weight: 20030.93

Authors

Gooley, P.R.,O'Connell, J.F. (deposition date: 1995-03-22, release date: 1995-07-10, Last modification date: 2024-05-22)

Primary citation

Gooley, P.R.,O'Connell, J.F.,Marcy, A.I.,Cuca, G.C.,Salowe, S.P.,Bush, B.L.,Hermes, J.D.,Esser, C.K.,Hagmann, W.K.,Springer, J.P.,Johnson, B.A.
The NMR structure of the inhibited catalytic domain of human stromelysin-1.
Nat.Struct.Biol., 1:111-118, 1994

PubMed Abstract: 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.

PubMed: 7656014
DOI: 10.1038/nsb0294-111

Experimental method

SOLUTION NMR