1vnc
From Proteopedia
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|PDB= 1vnc |SIZE=350|CAPTION= <scene name='initialview01'>1vnc</scene>, resolution 2.1Å | |PDB= 1vnc |SIZE=350|CAPTION= <scene name='initialview01'>1vnc</scene>, resolution 2.1Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=AZI:AZIDE+ION'>AZI</scene>, <scene name='pdbligand=VO4:VANADATE+ION'>VO4</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Chloride_peroxidase Chloride peroxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.11.1.10 1.11.1.10] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Chloride_peroxidase Chloride peroxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.11.1.10 1.11.1.10] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1vnc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vnc OCA], [http://www.ebi.ac.uk/pdbsum/1vnc PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1vnc RCSB]</span> | ||
}} | }} | ||
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[[Category: Messerschmidt, A.]] | [[Category: Messerschmidt, A.]] | ||
[[Category: Wever, R.]] | [[Category: Wever, R.]] | ||
| - | [[Category: AZI]] | ||
| - | [[Category: VO4]] | ||
[[Category: oxidoreductase]] | [[Category: oxidoreductase]] | ||
[[Category: vanadium-containing haloperoxidase]] | [[Category: vanadium-containing haloperoxidase]] | ||
| - | ''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 00:26:29 2008'' |
Revision as of 21:26, 30 March 2008
| |||||||
| , resolution 2.1Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Activity: | Chloride peroxidase, with EC number 1.11.1.10 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CHLOROPEROXIDASE FROM THE FUNGUS CURVULARIA INAEQUALIS
Overview
The chloroperoxidase (EC 1.11.1.-) from the fungus Curvularia inaequalis belongs to a class of vanadium enzymes that oxidize halides in the presence of hydrogen peroxide to the corresponding hypohalous acids. The 2.1 A crystal structure (R = 20%) of an azide chloroperoxidase complex reveals the geometry of the catalytic vanadium center. Azide coordinates directly to the metal center, resulting in a structure with azide, three nonprotein oxygens, and a histidine as ligands. In the native state vanadium will be bound as hydrogen vanadate(V) in a trigonal bipyramidal coordination with the metal coordinated to three oxygens in the equatorial plane, to the OH group at one apical position, and to the epsilon 2 nitrogen of a histidine at the other apical position. The protein fold is mainly alpha-helical with two four-helix bundles as main structural motifs and an overall structure different from other structures. The helices pack together to a compact molecule, which explains the high stability of the protein. An amino acid sequence comparison with vanadium-containing bromoperoxidase from the seaweed Ascophyllum nodosum shows high similarities in the regions of the metal binding site, with all hydrogen vanadate(V) interacting residues conserved except for lysine-353, which is an asparagine.
About this Structure
1VNC is a Single protein structure of sequence from Curvularia inaequalis. Full crystallographic information is available from OCA.
Reference
X-ray structure of a vanadium-containing enzyme: chloroperoxidase from the fungus Curvularia inaequalis., Messerschmidt A, Wever R, Proc Natl Acad Sci U S A. 1996 Jan 9;93(1):392-6. PMID:8552646
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