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Atomistry » Iron » PDB 4h9t-4hm6 » 4hgi | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Iron » PDB 4h9t-4hm6 » 4hgi » |
Iron in PDB 4hgi: Crystal Structure of P450 BM3 5F5 Heme Domain Variant Complexed with Styrene (Dataset II)Enzymatic activity of Crystal Structure of P450 BM3 5F5 Heme Domain Variant Complexed with Styrene (Dataset II)
All present enzymatic activity of Crystal Structure of P450 BM3 5F5 Heme Domain Variant Complexed with Styrene (Dataset II):
1.14.14.1; 1.6.2.4; Protein crystallography data
The structure of Crystal Structure of P450 BM3 5F5 Heme Domain Variant Complexed with Styrene (Dataset II), PDB code: 4hgi
was solved by
A.Shehzad,
S.Panneerselvam,
M.Bocola,
J.Mueller-Dieckmann,
M.Wilmanns,
U.Schwaneberg,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Iron Binding Sites:
The binding sites of Iron atom in the Crystal Structure of P450 BM3 5F5 Heme Domain Variant Complexed with Styrene (Dataset II)
(pdb code 4hgi). This binding sites where shown within
5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Crystal Structure of P450 BM3 5F5 Heme Domain Variant Complexed with Styrene (Dataset II), PDB code: 4hgi: Jump to Iron binding site number: 1; 2; Iron binding site 1 out of 2 in 4hgiGo back to![]() ![]()
Iron binding site 1 out
of 2 in the Crystal Structure of P450 BM3 5F5 Heme Domain Variant Complexed with Styrene (Dataset II)
![]() Mono view ![]() Stereo pair view
Iron binding site 2 out of 2 in 4hgiGo back to![]() ![]()
Iron binding site 2 out
of 2 in the Crystal Structure of P450 BM3 5F5 Heme Domain Variant Complexed with Styrene (Dataset II)
![]() Mono view ![]() Stereo pair view
Reference:
A.Shehzad,
S.Panneerselvam,
M.Linow,
M.Bocola,
D.Roccatano,
J.Mueller-Dieckmann,
M.Wilmanns,
U.Schwaneberg.
P450 BM3 Crystal Structures Reveal the Role of the Charged Surface Residue Lys/ARG184 in Inversion of Enantioselective Styrene Epoxidation. Chem.Commun.(Camb.) V. 49 4694 2013.
Page generated: Mon Aug 5 03:20:56 2024
ISSN: ISSN 1359-7345 PubMed: 23589805 DOI: 10.1039/C3CC39076D |
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