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2but

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|PDB= 2but |SIZE=350|CAPTION= <scene name='initialview01'>2but</scene>, resolution 1.85&Aring;
|PDB= 2but |SIZE=350|CAPTION= <scene name='initialview01'>2but</scene>, resolution 1.85&Aring;
|SITE= <scene name='pdbsite=AC1:Hyd+Binding+Site+For+Chain+B'>AC1</scene>
|SITE= <scene name='pdbsite=AC1:Hyd+Binding+Site+For+Chain+B'>AC1</scene>
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|LIGAND= <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene> and <scene name='pdbligand=HYD:HYDROXY GROUP'>HYD</scene>
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|LIGAND= <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=HYD:HYDROXY+GROUP'>HYD</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Protocatechuate_3,4-dioxygenase Protocatechuate 3,4-dioxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.13.11.3 1.13.11.3]
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Protocatechuate_3,4-dioxygenase Protocatechuate 3,4-dioxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.13.11.3 1.13.11.3] </span>
|GENE=
|GENE=
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|DOMAIN=
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2but FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2but OCA], [http://www.ebi.ac.uk/pdbsum/2but PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2but RCSB]</span>
}}
}}
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[[Category: Valley, M P.]]
[[Category: Valley, M P.]]
[[Category: Vetting, M W.]]
[[Category: Vetting, M W.]]
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[[Category: FE]]
 
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[[Category: HYD]]
 
[[Category: aromatic degradation]]
[[Category: aromatic degradation]]
[[Category: aromatic hydrocarbons catabolism]]
[[Category: aromatic hydrocarbons catabolism]]
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[[Category: oxidoreductase]]
[[Category: oxidoreductase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:06:59 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:12:06 2008''

Revision as of 23:12, 30 March 2008

Image:2but.gif


PDB ID 2but

Drag the structure with the mouse to rotate
, resolution 1.85Å
Sites:
Ligands: ,
Activity: Protocatechuate 3,4-dioxygenase, with EC number 1.13.11.3
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



CRYSTAL STRUCTURE OF PROTOCATECHUATE 3,4-DIOXYGENASE FROM ACINETOBACTER SP. ADP1 MUTANT R457S- APO


Overview

The catechol dioxygenases allow a wide variety of bacteria to use aromatic compounds as carbon sources by catalyzing the key ring-opening step. These enzymes use specifically either catechol or protocatechuate (2,3-dihydroxybenozate) as their substrates; they use a bare metal ion as the sole cofactor. To learn how this family of metalloenzymes functions, a structural analysis of designed and selected mutants of these enzymes has been undertaken. Here we review the results of this analysis on the nonheme ferric iron intradiol dioxygenase protocatechuate 3,4-dioxygenase.

About this Structure

2BUT is a Protein complex structure of sequences from Acinetobacter calcoaceticus. Full crystallographic information is available from OCA.

Reference

Biophysical analyses of designed and selected mutants of protocatechuate 3,4-dioxygenase1., Brown CK, Vetting MW, Earhart CA, Ohlendorf DH, Annu Rev Microbiol. 2004;58:555-85. PMID:15487948

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