1ose
From Proteopedia
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|PDB= 1ose |SIZE=350|CAPTION= <scene name='initialview01'>1ose</scene>, resolution 2.30Å | |PDB= 1ose |SIZE=350|CAPTION= <scene name='initialview01'>1ose</scene>, resolution 2.30Å | ||
|SITE= <scene name='pdbsite=AS1:Active+Site,+Sugar+Binding+Site'>AS1</scene>, <scene name='pdbsite=AS2:Active+Site,+Sugar+Binding+Site'>AS2</scene>, <scene name='pdbsite=AS3:Active+Site,+Sugar+Binding+Site'>AS3</scene>, <scene name='pdbsite=AS4:Active+Site,+Sugar+Binding+Site'>AS4</scene>, <scene name='pdbsite=AS5:Active+Site,+Sugar+Binding+Site'>AS5</scene>, <scene name='pdbsite=CAL:Ca+Binding+Site'>CAL</scene> and <scene name='pdbsite=CLO:Chloride+Binding+Site.+There+Are+Six+Bound+Sugar+Rings.+...'>CLO</scene> | |SITE= <scene name='pdbsite=AS1:Active+Site,+Sugar+Binding+Site'>AS1</scene>, <scene name='pdbsite=AS2:Active+Site,+Sugar+Binding+Site'>AS2</scene>, <scene name='pdbsite=AS3:Active+Site,+Sugar+Binding+Site'>AS3</scene>, <scene name='pdbsite=AS4:Active+Site,+Sugar+Binding+Site'>AS4</scene>, <scene name='pdbsite=AS5:Active+Site,+Sugar+Binding+Site'>AS5</scene>, <scene name='pdbsite=CAL:Ca+Binding+Site'>CAL</scene> and <scene name='pdbsite=CLO:Chloride+Binding+Site.+There+Are+Six+Bound+Sugar+Rings.+...'>CLO</scene> | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=AC1:6-METHYL-5-(4,5,6-TRIHYDROXY-3-HYDROXYMETHYL-CYCLOHEX-2-ENYLAMINO)-TETRAHYDRO-PYRAN-2,3,4-TRIOL'>AC1</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GLC:GLUCOSE'>GLC</scene>, <scene name='pdbligand=PCA:PYROGLUTAMIC+ACID'>PCA</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Alpha-amylase Alpha-amylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.1 3.2.1.1] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Alpha-amylase Alpha-amylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.1 3.2.1.1] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ose FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ose OCA], [http://www.ebi.ac.uk/pdbsum/1ose PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ose RCSB]</span> | ||
}} | }} | ||
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[[Category: Gilles, C.]] | [[Category: Gilles, C.]] | ||
[[Category: Payan, F.]] | [[Category: Payan, F.]] | ||
| - | [[Category: CA]] | ||
| - | [[Category: CL]] | ||
| - | [[Category: GLC]] | ||
[[Category: acarbose]] | [[Category: acarbose]] | ||
[[Category: alpha-amylase]] | [[Category: alpha-amylase]] | ||
| Line 33: | Line 33: | ||
[[Category: hydrolase (o-glycosyl)]] | [[Category: hydrolase (o-glycosyl)]] | ||
| - | ''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 22:49:46 2008'' |
Revision as of 19:49, 30 March 2008
| |||||||
| , resolution 2.30Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | , , , , , and | ||||||
| Ligands: | , , , , | ||||||
| Activity: | Alpha-amylase, with EC number 3.2.1.1 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
PORCINE PANCREATIC ALPHA-AMYLASE COMPLEXED WITH ACARBOSE
Overview
Two different crystal forms of pig pancreatic alpha-amylase isoenzyme II (PPAII), free and complexed to a carbohydrate inhibitor (acarbose), have been compared together and to previously reported structures of PPAI. A crystal form obtained at 4 degrees C, containing nearly 72% solvent, made it possible to obtain a new complex with acarbose, different from a previous one obtained at 20 degrees C [Qian, M., Buisson, G., Duee, E., Haser, H. & Payan, F. (1994) Biochemistry 33, 6284-6294]. In the present form, six contiguous subsites of the enzyme active site are occupied by the carbohydrate ligand; the structural data indicate that the binding site is capable of holding more than the five glucose units of the scheme proposed through kinetic studies. A monosaccharide ring bridging two protein molecules related by the crystal packing is located on the surface, at a distance of 2.0 nm from the reducing end of the inhibitor ligand; the symmetry-related glucose ring in the crystal lattice is found 1.5 nm away from the non-reducing end of the inhibitor ligand.
About this Structure
1OSE is a Single protein structure of sequence from Sus scrofa. Full crystallographic information is available from OCA.
Reference
Crystal structure of pig pancreatic alpha-amylase isoenzyme II, in complex with the carbohydrate inhibitor acarbose., Gilles C, Astier JP, Marchis-Mouren G, Cambillau C, Payan F, Eur J Biochem. 1996 Jun 1;238(2):561-9. PMID:8681972
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