1o7p
From Proteopedia
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|PDB= 1o7p |SIZE=350|CAPTION= <scene name='initialview01'>1o7p</scene>, resolution 1.95Å | |PDB= 1o7p |SIZE=350|CAPTION= <scene name='initialview01'>1o7p</scene>, resolution 1.95Å | ||
|SITE= <scene name='pdbsite=AC1:Fe+Binding+Site+For+Chain+A'>AC1</scene> | |SITE= <scene name='pdbsite=AC1:Fe+Binding+Site+For+Chain+A'>AC1</scene> | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=NDH:(1R,+2S)-CIS+1,2+DIHYDROXY-1,2-DIHYDRONAPHTHALENE'>NDH</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Naphthalene_1,2-dioxygenase Naphthalene 1,2-dioxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.12.12 1.14.12.12] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Naphthalene_1,2-dioxygenase Naphthalene 1,2-dioxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.12.12 1.14.12.12] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1o7p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o7p OCA], [http://www.ebi.ac.uk/pdbsum/1o7p PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1o7p RCSB]</span> | ||
}} | }} | ||
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[[Category: Parales, R E.]] | [[Category: Parales, R E.]] | ||
[[Category: Ramaswamy, S.]] | [[Category: Ramaswamy, S.]] | ||
| - | [[Category: EDO]] | ||
| - | [[Category: FE]] | ||
| - | [[Category: FES]] | ||
| - | [[Category: NDH]] | ||
| - | [[Category: SO4]] | ||
[[Category: aromatic hydrocarbon catabolism oxidoreductase]] | [[Category: aromatic hydrocarbon catabolism oxidoreductase]] | ||
[[Category: enzyme-substrate complex]] | [[Category: enzyme-substrate complex]] | ||
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[[Category: oxidoreductase]] | [[Category: oxidoreductase]] | ||
| - | ''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 22:41:03 2008'' |
Revision as of 19:41, 30 March 2008
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| , resolution 1.95Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | |||||||
| Ligands: | , , , , | ||||||
| Activity: | Naphthalene 1,2-dioxygenase, with EC number 1.14.12.12 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
NAPHTHALENE 1,2-DIOXYGENASE, PRODUCT COMPLEX
Overview
Binding of oxygen to iron is exploited in several biological and chemical processes. Although computational and spectroscopic results have suggested side-on binding, only end-on binding of oxygen to iron has been observed in crystal structures. We have determined structures of naphthalene dioxygenase that show a molecular oxygen species bound to the mononuclear iron in a side-on fashion. In a complex with substrate and dioxygen, the dioxygen molecule is lined up for an attack on the double bond of the aromatic substrate. The structures reported here provide the basis for a reaction mechanism and for the high stereospecificity of the reaction catalyzed by naphthalene dioxygenase.
About this Structure
1O7P is a Protein complex structure of sequences from Pseudomonas putida. Full crystallographic information is available from OCA.
Reference
Crystal structure of naphthalene dioxygenase: side-on binding of dioxygen to iron., Karlsson A, Parales JV, Parales RE, Gibson DT, Eklund H, Ramaswamy S, Science. 2003 Feb 14;299(5609):1039-42. PMID:12586937
Page seeded by OCA on Sun Mar 30 22:41:03 2008
Categories: Naphthalene 1,2-dioxygenase | Protein complex | Pseudomonas putida | Eklund, H. | Gibson, D T. | Karlsson, A. | Parales, J V. | Parales, R E. | Ramaswamy, S. | Aromatic hydrocarbon catabolism oxidoreductase | Enzyme-substrate complex | Iron-sulfur | Non-heme iron dioxygenase | Oxidoreductase
