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Ligands
Code Name Style Show Link
4NC 4-nitrocatechol
CA Calcium ion
CL Chloride ion
FE2 Fe (II) ion
P6G Hexaethylene glycol
Non-standard Residues
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Glycosylation
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Code : 4Z6V   PDBj   RCSB PDB   PDBe
Header : OXIDOREDUCTASE
Title : Structure of H200Q variant of Homoprotocatechuate 2,3-Dioxygenase from B.fuscum in complex with 4-nitrocatechol at 1.37 Ang resolution
Release Data : 2015-08-26
Compound :
mol_id molecule chains
1 Homoprotocatechuate 2,3-dioxygenase A,B,C,D
mutation: H200Q
Source :
mol_id organism_scientific expression_system
1 Brevibacterium fuscum  (taxid:47914) Escherichia coli  (taxid:562)
atcc: 15993
expression_system_strain: Jm109
expression_system_vector_type: plasmid
expression_system_plasmid: pYZW204
Authors : Kovaleva, E.G., Lipscomb, J.D.
Keywords : Dioxygenase, 2-His-1-carboxylate facial triad, oxygen activation, acid-base catalysis, Oxidoreductase
Exp. method : X-RAY DIFFRACTION ( 1.3700 Å )
Citation :

Structural Basis for Substrate and Oxygen Activation in Homoprotocatechuate 2,3-Dioxygenase: Roles of Conserved Active Site Histidine 200.

Kovaleva, E.G.,Rogers, M.S.,Lipscomb, J.D.
(2015)  Biochemistry  54 : 5329 - 5339

PubMed: 26267790
DOI: 10.1021/acs.biochem.5b00709

Chain : A, B, C, D
UniProt : Q45135 (Q45135_9MICO)
Reaction : -