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PDBe Entry: 1f1x 
CRYSTAL STRUCTURE OF HOMOPROTOCATECHUATE 2,3-DIOXYGENASE FROM BREVIBACTERIUM FUSCUM
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OXIDOREDUCTASE
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X-RAY DIFFRACTION
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Resolution: 1.6 Å, R-factor: 16.8%, Free R-factor: 19.5%, Spacegroup: I 41
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10/06/2003, deposition: 20/05/2000, last revision: 24/02/2009
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Vetting, M.W.; Lipscomb, J.D.; Wackett, L.P.; Que Jr., L.; Ohlendorf, D.H.
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Crystallographic comparison of manganese- and iron-dependent homoprotocatechuate 2,3-dioxygenases.
J.BACTERIOL. vol:186, pag:1945-1958 (2004) [PubMed ID 15028678 ]
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Dioxygenase, Extradiol, Iron, Biodegradation, Aromatic, OXIDOREDUCTASE
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Brevibacterium fuscum 47914(A B C D)
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Homoprotocatechuate 2,3-dioxygenase Q45135 (A B C D)
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A, B, C, D
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1f1r, 1f1u, 1f1v, 1f1y
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| A, B, C, D |
HOMOPROTOCATECHUATE 2,3-DIOXYGENASE |
Protein |
Q45135 (Q45135_9MICO)
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322 |
99% |
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| A, B, C, D |
HYDRATED FE |
FEL
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