1slu
From Proteopedia
| Line 4: | Line 4: | ||
|PDB= 1slu |SIZE=350|CAPTION= <scene name='initialview01'>1slu</scene>, resolution 1.8Å | |PDB= 1slu |SIZE=350|CAPTION= <scene name='initialview01'>1slu</scene>, resolution 1.8Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Trypsin Trypsin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.4 3.4.21.4] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Trypsin Trypsin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.4 3.4.21.4] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1slu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1slu OCA], [http://www.ebi.ac.uk/pdbsum/1slu PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1slu RCSB]</span> | ||
}} | }} | ||
| Line 26: | Line 29: | ||
[[Category: Brinen, L S.]] | [[Category: Brinen, L S.]] | ||
[[Category: Fletterick, R J.]] | [[Category: Fletterick, R J.]] | ||
| - | [[Category: ACT]] | ||
| - | [[Category: CA]] | ||
[[Category: complex]] | [[Category: complex]] | ||
[[Category: inhibitor]] | [[Category: inhibitor]] | ||
| Line 36: | Line 37: | ||
[[Category: serine protease]] | [[Category: serine protease]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:43:48 2008'' |
Revision as of 20:43, 30 March 2008
| |||||||
| , resolution 1.8Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Activity: | Trypsin, with EC number 3.4.21.4 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
RAT ANIONIC N143H, E151H TRYPSIN COMPLEXED TO A86H ECOTIN
Overview
The three-dimensional structures of complexes of trypsin N143H, E151H bound to ecotin A86H are determined at 2.0 A resolution via X-ray crystallography in the absence and presence of the transition metals Zn2+, Ni2+, and Cu2+. The binding site for these transition metals was constructed by substitution of key amino acids with histidine at the trypsin-ecotin interface in the S2'/P2' pocket. Three histidine side chains, two on trypsin at positions 143 and 151 and one on ecotin at position 86, anchor the metals and provide extended catalytic recognition for substrates with His in the P2' pocket. Comparisons of the three-dimensional structures show the different geometries that result upon the binding of metal in the engineered tridentate site and suggest a structural basis for the kinetics of the metal-regulated catalysis. Of the three metals, the binding of zinc results in the most favorable binding geometry, not dissimilar to those observed in naturally occurring zinc binding proteins.
About this Structure
1SLU is a Protein complex structure of sequences from Escherichia coli and Rattus norvegicus. Full crystallographic information is available from OCA.
Reference
X-ray structures of a designed binding site in trypsin show metal-dependent geometry., Brinen LS, Willett WS, Craik CS, Fletterick RJ, Biochemistry. 1996 May 14;35(19):5999-6009. PMID:8634241
Page seeded by OCA on Sun Mar 30 23:43:48 2008
