2c11
From Proteopedia
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|PDB= 2c11 |SIZE=350|CAPTION= <scene name='initialview01'>2c11</scene>, resolution 2.9Å | |PDB= 2c11 |SIZE=350|CAPTION= <scene name='initialview01'>2c11</scene>, resolution 2.9Å | ||
|SITE= <scene name='pdbsite=AC1:Cu+Binding+Site+For+Chain+D'>AC1</scene> | |SITE= <scene name='pdbsite=AC1:Cu+Binding+Site+For+Chain+D'>AC1</scene> | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=FUL:BETA-L-FUCOSE'>FUL</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=NDG:2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE'>NDG</scene>, <scene name='pdbligand=PAQ:2-OXY-4-HYDROXY-5-(2-HYDRAZINOPYRIDINE)PHENYLALANINE'>PAQ</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Amine_oxidase_(copper-containing) Amine oxidase (copper-containing)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.3.6 1.4.3.6] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Amine_oxidase_(copper-containing) Amine oxidase (copper-containing)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.3.6 1.4.3.6] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2c11 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c11 OCA], [http://www.ebi.ac.uk/pdbsum/2c11 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2c11 RCSB]</span> | ||
}} | }} | ||
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[[Category: Jakobsson, E.]] | [[Category: Jakobsson, E.]] | ||
[[Category: Kleywegt, G J.]] | [[Category: Kleywegt, G J.]] | ||
| - | [[Category: CA]] | ||
| - | [[Category: CL]] | ||
| - | [[Category: CU]] | ||
| - | [[Category: NAG]] | ||
| - | [[Category: NDG]] | ||
| - | [[Category: PAQ]] | ||
[[Category: 2-hydroxypyridine]] | [[Category: 2-hydroxypyridine]] | ||
[[Category: adhesion protein-1]] | [[Category: adhesion protein-1]] | ||
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[[Category: vascular]] | [[Category: vascular]] | ||
| - | ''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 02:14:42 2008'' |
Revision as of 23:14, 30 March 2008
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| , resolution 2.9Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | |||||||
| Ligands: | , , , , , , , , | ||||||
| Activity: | Amine oxidase (copper-containing), with EC number 1.4.3.6 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF THE 2-HYDRAZINOPYRIDINE OF SEMICARBAZIDE-SENSITIVE AMINE OXIDASE
Overview
Semicarbazide-sensitive amine oxidase (SSAO) belongs to a ubiquitous family of copper-containing amine oxidases (CuAOs). SSAO is also known as vascular adhesion protein-1 (VAP-1) and has been identified as one of the adhesion molecules involved in the leukocyte-extravasation process. The structure of a truncated soluble form of human SSAO has been solved and refined to 2.5 A. As expected, SSAO is a homodimer with a fold typical of the CuAO family. The topaquinone (TPQ) cofactor and a copper ion characteristic of CuAOs are present in the active site, with the TPQ in the active ;off-copper' conformation. The structure reveals that a leucine residue (Leu469) located adjacent to the active site could function as a gate controlling its accessibility. An RGD motif is displayed on the surface, where it could be involved in integrin binding and possibly play a role in the shedding of SSAO from the membrane. Carbohydrate moieties are observed at five of six potential N-glycosylation sites. Carbohydrates attached to Asn232 flank the active-site entrance and might influence substrate specificity. The structure of an adduct of SSAO and the irreversible inhibitor 2-hydrazinopyridine has been solved and refined to 2.9 A resolution. Together, these structures will aid efforts to identify natural substrates, provide valuable information for the design of specific inhibitors and direct further studies.
About this Structure
2C11 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structure of human semicarbazide-sensitive amine oxidase/vascular adhesion protein-1., Jakobsson E, Nilsson J, Ogg D, Kleywegt GJ, Acta Crystallogr D Biol Crystallogr. 2005 Nov;61(Pt 11):1550-62. Epub 2005, Oct 19. PMID:16239734
Page seeded by OCA on Mon Mar 31 02:14:42 2008
Categories: Amine oxidase (copper-containing) | Homo sapiens | Single protein | Jakobsson, E. | Kleywegt, G J. | 2-hydroxypyridine | Adhesion protein-1 | Cell adhesion | Copper | Glycoprotein | Metal-binding | Oxidoreductase | Polymorphism | Semicarbazide-sensitive amine oxidase | Signal-anchor | Ssao | Tpq | Transmembrane | Vap-1 | Vascular
