2ckf
From Proteopedia
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| - | [[Image:2ckf.jpg|left|200px]] | + | [[Image:2ckf.jpg|left|200px]] |
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| - | '''CRYSTAL STRUCTURE OF THE TERMINAL COMPONENT OF THE PAH-HYDROXYLATING DIOXYGENASE FROM SPHINGOMONAS SP CHY-1''' | + | {{Structure |
| + | |PDB= 2ckf |SIZE=350|CAPTION= <scene name='initialview01'>2ckf</scene>, resolution 1.85Å | ||
| + | |SITE= <scene name='pdbsite=AC1:Fe+Binding+Site+For+Chain+E'>AC1</scene> | ||
| + | |LIGAND= <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene> and <scene name='pdbligand=FES:FE2/S2 (INORGANIC) CLUSTER'>FES</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''CRYSTAL STRUCTURE OF THE TERMINAL COMPONENT OF THE PAH-HYDROXYLATING DIOXYGENASE FROM SPHINGOMONAS SP CHY-1''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2CKF is a [ | + | 2CKF is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Sphingomonas_sp._chy-1 Sphingomonas sp. chy-1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CKF OCA]. |
==Reference== | ==Reference== | ||
| - | The catalytic pocket of the ring-hydroxylating dioxygenase from Sphingomonas CHY-1., Jakoncic J, Jouanneau Y, Meyer C, Stojanoff V, Biochem Biophys Res Commun. 2007 Jan 26;352(4):861-6. Epub 2006 Dec 4. PMID:[http:// | + | The catalytic pocket of the ring-hydroxylating dioxygenase from Sphingomonas CHY-1., Jakoncic J, Jouanneau Y, Meyer C, Stojanoff V, Biochem Biophys Res Commun. 2007 Jan 26;352(4):861-6. Epub 2006 Dec 4. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17157819 17157819] |
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Sphingomonas sp. chy-1]] | [[Category: Sphingomonas sp. chy-1]] | ||
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[[Category: FE]] | [[Category: FE]] | ||
[[Category: FES]] | [[Category: FES]] | ||
| - | [[Category: high-molecular-weight polycyclic aromatic | + | [[Category: high-molecular-weight polycyclic aromatic hydrocarbon]] |
[[Category: oxidoreductase]] | [[Category: oxidoreductase]] | ||
[[Category: pyrene dioxygenase]] | [[Category: pyrene dioxygenase]] | ||
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[[Category: ring-hydroxylating dioxygenase]] | [[Category: ring-hydroxylating dioxygenase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:16:31 2008'' |
Revision as of 14:16, 20 March 2008
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| , resolution 1.85Å | |||||||
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF THE TERMINAL COMPONENT OF THE PAH-HYDROXYLATING DIOXYGENASE FROM SPHINGOMONAS SP CHY-1
Overview
Ring-hydroxylating dioxygenases are multicomponent bacterial enzymes that catalyze the first step in the oxidative degradation of aromatic hydrocarbons. The dioxygenase from Sphingomonas CHY-1 is unique in that it can oxidize a wide range of polycyclic aromatic hydrocarbons (PAHs). With a crystal structure similar to that of the seven other known dioxygenases, its catalytic domain features the largest hydrophobic substrate binding cavity characterized so far. Molecular modeling studies indicated that the catalytic cavity is large enough to accommodate a five-ring benzo[a]pyrene molecule. The predicted positions of this and other PAHs in the substrate binding pocket are consistent with the product regio- and stereo-selectivity of the enzyme.
About this Structure
2CKF is a Protein complex structure of sequences from Sphingomonas sp. chy-1. Full crystallographic information is available from OCA.
Reference
The catalytic pocket of the ring-hydroxylating dioxygenase from Sphingomonas CHY-1., Jakoncic J, Jouanneau Y, Meyer C, Stojanoff V, Biochem Biophys Res Commun. 2007 Jan 26;352(4):861-6. Epub 2006 Dec 4. PMID:17157819
Page seeded by OCA on Thu Mar 20 16:16:31 2008
