2srt
From Proteopedia
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|PDB= 2srt |SIZE=350|CAPTION= <scene name='initialview01'>2srt</scene> | |PDB= 2srt |SIZE=350|CAPTION= <scene name='initialview01'>2srt</scene> | ||
|SITE= | |SITE= | ||
| - | |LIGAND= | + | |LIGAND= <scene name='pdbligand=INH:N-(R-CARBOXY-ETHYL)-ALPHA-(S)-(2-PHENYLETHYL)GLYCYL-L-ARGININE-N-PHENYLAMIDE'>INH</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> |
| - | |ACTIVITY= [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] | + | |ACTIVITY= <span class='plainlinks'>[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] </span> |
|GENE= HUMAN STROMELYSIN-1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | |GENE= HUMAN STROMELYSIN-1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2srt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2srt OCA], [http://www.ebi.ac.uk/pdbsum/2srt PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2srt RCSB]</span> | ||
}} | }} | ||
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==Overview== | ==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. | 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. | ||
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| - | ==Disease== | ||
| - | Known diseases associated with this structure: Coronary heart disease, susceptibility to OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=185250 185250]] | ||
==About this Structure== | ==About this Structure== | ||
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[[Category: Connell, J F.O.]] | [[Category: Connell, J F.O.]] | ||
[[Category: Gooley, P R.]] | [[Category: Gooley, P R.]] | ||
| - | [[Category: INH]] | ||
| - | [[Category: ZN]] | ||
[[Category: metzincin]] | [[Category: metzincin]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:03:22 2008'' |
Revision as of 02:03, 31 March 2008
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| Ligands: | , | ||||||
| Gene: | HUMAN STROMELYSIN-1 (Homo sapiens) | ||||||
| Activity: | Stromelysin 1, with EC number 3.4.24.17 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CATALYTIC DOMAIN OF HUMAN STROMELYSIN-1 AT PH 5.5 AND 40OC COMPLEXED WITH INHIBITOR
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.
About this Structure
2SRT is a Single protein structure of sequence from Homo sapiens. This structure supersedes the now removed PDB entry 1SRT. 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 Mar 31 05:03:22 2008
