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Atomistry » Iron » PDB 6xai-6xyv » 6xv4 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Iron » PDB 6xai-6xyv » 6xv4 » |
Iron in PDB 6xv4: Neutron Structure of Ferric Ascorbate Peroxidase-Ascorbate ComplexEnzymatic activity of Neutron Structure of Ferric Ascorbate Peroxidase-Ascorbate Complex
All present enzymatic activity of Neutron Structure of Ferric Ascorbate Peroxidase-Ascorbate Complex:
1.11.1.11; Protein crystallography data
The structure of Neutron Structure of Ferric Ascorbate Peroxidase-Ascorbate Complex, PDB code: 6xv4
was solved by
H.Kwon,
J.Basran,
J.M.Devos,
T.E.Schrader,
A.Ostermann,
M.P.Blakeley,
E.L.Raven,
P.C.E.Moody,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 6xv4:
The structure of Neutron Structure of Ferric Ascorbate Peroxidase-Ascorbate Complex also contains other interesting chemical elements:
Iron Binding Sites:
The binding sites of Iron atom in the Neutron Structure of Ferric Ascorbate Peroxidase-Ascorbate Complex
(pdb code 6xv4). This binding sites where shown within
5.0 Angstroms radius around Iron atom.
In total only one binding site of Iron was determined in the Neutron Structure of Ferric Ascorbate Peroxidase-Ascorbate Complex, PDB code: 6xv4: Iron binding site 1 out of 1 in 6xv4Go back to![]() ![]()
Iron binding site 1 out
of 1 in the Neutron Structure of Ferric Ascorbate Peroxidase-Ascorbate Complex
![]() Mono view ![]() Stereo pair view
Reference:
H.Kwon,
J.Basran,
J.M.Devos,
R.Suardiaz,
M.W.Van Der Kamp,
A.J.Mulholland,
T.E.Schrader,
A.Ostermann,
M.P.Blakeley,
P.C.E.Moody,
E.L.Raven.
Visualizing the Protons in A Metalloenzyme Electron Proton Transfer Pathway. Proc.Natl.Acad.Sci.Usa 2020.
Page generated: Wed Aug 7 15:41:56 2024
ISSN: ESSN 1091-6490 PubMed: 32152099 DOI: 10.1073/PNAS.1918936117 |
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