1a2v
From Proteopedia
| Line 4: | Line 4: | ||
|PDB= 1a2v |SIZE=350|CAPTION= <scene name='initialview01'>1a2v</scene>, resolution 2.40Å | |PDB= 1a2v |SIZE=350|CAPTION= <scene name='initialview01'>1a2v</scene>, resolution 2.40Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=CU:COPPER (II) ION'>CU</scene> | + | |LIGAND= <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=TPQ:5-(2-CARBOXY-2-AMINOETHYL)-2-HYDROXY-1,4-BENZOQUINONE'>TPQ</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=1a2v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a2v OCA], [http://www.ebi.ac.uk/pdbsum/1a2v PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1a2v RCSB]</span> | ||
}} | }} | ||
| Line 25: | Line 28: | ||
[[Category: Li, R.]] | [[Category: Li, R.]] | ||
[[Category: Mathews, F S.]] | [[Category: Mathews, F S.]] | ||
| - | [[Category: CU]] | ||
[[Category: amine oxidase]] | [[Category: amine oxidase]] | ||
[[Category: quinoprotein]] | [[Category: quinoprotein]] | ||
| Line 31: | Line 33: | ||
[[Category: tpq]] | [[Category: tpq]] | ||
| - | ''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 18:32:04 2008'' |
Revision as of 15:32, 30 March 2008
| |||||||
| , resolution 2.40Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Activity: | Amine oxidase (copper-containing), with EC number 1.4.3.6 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
COPPER AMINE OXIDASE FROM HANSENULA POLYMORPHA
Overview
The copper-containing amine oxidase from the yeast Hansenula polymorpha (YAO) has been crystallized and partially solved by molecular replacement. It catalyzes the oxidative deamination of primary amines by molecular oxygen to the corresponding aldehydes, ammonia and hydrogen peroxide. It contains a covalently bound redox cofactor, topa quinone, generated by post-translational modification of a single tyrosine side chain. The crystals of YAO are orthorhombic, with space-group symmetry P2(1)2(1)2(1) and unit-cell dimensions a = 138.8, b = 148.2, c = 234.0 A and diffract X-rays beyond 2.0 A resolution. Solution by molecular replacement using the E. coli amine oxidase structure [Parsons, Convery, Wilmot, Yadav, Blakeley, Corner, Philips, McPherson & Knowles (1995). Structure, 3, 1171-1184] as a search model reveals that there are three dimers in the asymmetric unit in a trigonal arrangement having 32 point-group symmetry. The solution agrees well with the self-rotation function of YAO. The non-crystallographic threefold axis lies parallel to a crystallographic twofold screw axis and each dimer has twofold symmetry. Phases from the refined model based on the molecular-replacement solution were used to solve one heavy-atom derivative. Model building from the unbiased isomorphous replacement phases is in progress.
About this Structure
1A2V is a Single protein structure of sequence from Pichia angusta. Full crystallographic information is available from OCA.
Reference
Crystallographic study of yeast copper amine oxidase., Li R, Chen L, Cai D, Klinman JP, Mathews FS, Acta Crystallogr D Biol Crystallogr. 1997 Jul 1;53(Pt 4):364-70. PMID:15299901
Page seeded by OCA on Sun Mar 30 18:32:04 2008
