2srt
From Proteopedia
(New page: 200px<br /> <applet load="2srt" size="450" color="white" frame="true" align="right" spinBox="true" caption="2srt" /> '''CATALYTIC DOMAIN OF HUMAN STROMELYSIN-1 AT ...) |
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'''CATALYTIC DOMAIN OF HUMAN STROMELYSIN-1 AT PH 5.5 AND 40OC COMPLEXED WITH INHIBITOR'''<br /> | '''CATALYTIC DOMAIN OF HUMAN STROMELYSIN-1 AT PH 5.5 AND 40OC COMPLEXED WITH INHIBITOR'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The three-dimensional structure of the catalytic domain of stromelysin-1 | + | 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== | ==Disease== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2SRT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with ZN and INH as [http://en.wikipedia.org/wiki/ligands ligands]. This structure | + | 2SRT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=ZN:'>ZN</scene> and <scene name='pdbligand=INH:'>INH</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. This structure supersedes the now removed PDB entry 1SRT. Active as [http://en.wikipedia.org/wiki/Stromelysin_1 Stromelysin 1], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.17 3.4.24.17] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2SRT OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Stromelysin 1]] | [[Category: Stromelysin 1]] | ||
| - | [[Category: Connell, J | + | [[Category: Connell, J F.O.]] |
| - | [[Category: Gooley, P | + | [[Category: Gooley, P R.]] |
[[Category: INH]] | [[Category: INH]] | ||
[[Category: ZN]] | [[Category: ZN]] | ||
[[Category: metzincin]] | [[Category: metzincin]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:49:26 2008'' |
Revision as of 16:49, 21 February 2008
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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
Page seeded by OCA on Thu Feb 21 18:49:26 2008
Categories: Homo sapiens | Single protein | Stromelysin 1 | Connell, J F.O. | Gooley, P R. | INH | ZN | Metzincin
