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Atomistry » Iron » PDB 6fmo-6g5t » 6g0a | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Iron » PDB 6fmo-6g5t » 6g0a » |
Iron in PDB 6g0a: The Crystal Structure of the POL2 Catalytic Domain of Dna Polymerase Epsilon Carrying A P301R Substitution.Enzymatic activity of The Crystal Structure of the POL2 Catalytic Domain of Dna Polymerase Epsilon Carrying A P301R Substitution.
All present enzymatic activity of The Crystal Structure of the POL2 Catalytic Domain of Dna Polymerase Epsilon Carrying A P301R Substitution.:
2.7.7.7; Protein crystallography data
The structure of The Crystal Structure of the POL2 Catalytic Domain of Dna Polymerase Epsilon Carrying A P301R Substitution., PDB code: 6g0a
was solved by
V.Parkash,
E.Johansson,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 6g0a:
The structure of The Crystal Structure of the POL2 Catalytic Domain of Dna Polymerase Epsilon Carrying A P301R Substitution. also contains other interesting chemical elements:
Iron Binding Sites:
The binding sites of Iron atom in the The Crystal Structure of the POL2 Catalytic Domain of Dna Polymerase Epsilon Carrying A P301R Substitution.
(pdb code 6g0a). 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 The Crystal Structure of the POL2 Catalytic Domain of Dna Polymerase Epsilon Carrying A P301R Substitution., PDB code: 6g0a: Iron binding site 1 out of 1 in 6g0aGo back to![]() ![]()
Iron binding site 1 out
of 1 in the The Crystal Structure of the POL2 Catalytic Domain of Dna Polymerase Epsilon Carrying A P301R Substitution.
![]() Mono view ![]() Stereo pair view
Reference:
V.Parkash,
Y.Kulkarni,
J.Ter Beek,
P.V.Shcherbakova,
S.C.L.Kamerlin,
E.Johansson.
Structural Consequence of the Most Frequently Recurring Cancer-Associated Substitution in Dna Polymerase Epsilon. Nat Commun V. 10 373 2019.
Page generated: Tue Aug 6 18:50:07 2024
ISSN: ESSN 2041-1723 PubMed: 30670696 DOI: 10.1038/S41467-018-08114-9 |
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