Iron in PDB 6jsc: Crystal Structure of the H434A Variant of the C-Terminal Domain of Htaa From Corynebacterium Glutamicum

The structure of Crystal Structure of the H434A Variant of the C-Terminal Domain of Htaa From Corynebacterium Glutamicum, PDB code: 6jsc was solved by N.Muraki, S.Aono, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	36.19 / 1.40
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	39.040, 43.150, 199.440, 90.00, 90.00, 90.00
R / Rfree (%)	18.1 / 20.2

The structure of Crystal Structure of the H434A Variant of the C-Terminal Domain of Htaa From Corynebacterium Glutamicum also contains other interesting chemical elements:

Sodium

(Na)

4 atoms

The binding sites of Iron atom in the Crystal Structure of the H434A Variant of the C-Terminal Domain of Htaa From Corynebacterium Glutamicum (pdb code 6jsc). 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 the H434A Variant of the C-Terminal Domain of Htaa From Corynebacterium Glutamicum, PDB code: 6jsc:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Crystal Structure of the H434A Variant of the C-Terminal Domain of Htaa From Corynebacterium Glutamicum


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Crystal Structure of the H434A Variant of the C-Terminal Domain of Htaa From Corynebacterium Glutamicum within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe201 b:14.3 occ:1.00 FE A:HEM201 0.0 14.3 1.0 NA A:HEM201 2.1 14.4 1.0 NC A:HEM201 2.1 13.5 1.0 ND A:HEM201 2.1 14.4 1.0 NB A:HEM201 2.1 13.4 1.0 OH A:TYR383 2.1 16.1 1.0 CZ A:TYR383 3.0 13.0 1.0 C1A A:HEM201 3.1 13.5 1.0 C1C A:HEM201 3.1 12.7 1.0 C4B A:HEM201 3.1 14.9 1.0 C4D A:HEM201 3.1 14.0 1.0 C4A A:HEM201 3.1 16.8 1.0 C1D A:HEM201 3.1 15.2 1.0 C4C A:HEM201 3.1 13.9 1.0 C1B A:HEM201 3.1 14.1 1.0 CHC A:HEM201 3.4 13.2 1.0 CHA A:HEM201 3.4 13.9 1.0 CHD A:HEM201 3.5 13.7 1.0 CHB A:HEM201 3.5 15.6 1.0 CZ A:PHE511 3.6 16.8 1.0 CE1 A:PHE511 3.6 14.2 1.0 CE2 A:TYR383 3.7 12.5 1.0 O A:HOH601 3.7 25.1 1.0 CE1 A:TYR383 3.7 15.1 1.0 CE2 A:PHE511 4.1 17.5 1.0 CD1 A:PHE511 4.2 14.3 1.0 C2A A:HEM201 4.3 18.9 1.0 C3A A:HEM201 4.3 17.6 1.0 C3B A:HEM201 4.3 15.9 1.0 C2C A:HEM201 4.3 14.2 1.0 C3D A:HEM201 4.3 14.5 1.0 C2D A:HEM201 4.3 14.7 1.0 C3C A:HEM201 4.3 13.8 1.0 C2B A:HEM201 4.4 14.8 1.0 CD2 A:PHE511 4.6 15.2 1.0 CG A:PHE511 4.6 16.1 1.0 CD1 A:LEU438 4.8 14.3 1.0 CD2 A:TYR383 4.9 12.7 1.0 CD1 A:TYR383 4.9 13.8 1.0

Iron binding site 2 out of 2 in the Crystal Structure of the H434A Variant of the C-Terminal Domain of Htaa From Corynebacterium Glutamicum


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Crystal Structure of the H434A Variant of the C-Terminal Domain of Htaa From Corynebacterium Glutamicum within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe201 b:16.0 occ:1.00 FE B:HEM201 0.0 16.0 1.0 NA B:HEM201 2.1 16.0 1.0 ND B:HEM201 2.1 14.2 1.0 NC B:HEM201 2.1 15.7 1.0 NB B:HEM201 2.1 14.5 1.0 OH B:TYR383 2.1 16.4 1.0 CZ B:TYR383 3.0 15.8 1.0 C1A B:HEM201 3.1 16.5 1.0 C4D B:HEM201 3.1 15.8 1.0 C4A B:HEM201 3.1 18.8 1.0 C1D B:HEM201 3.1 13.9 1.0 C4B B:HEM201 3.1 16.6 1.0 C4C B:HEM201 3.1 14.5 1.0 C1C B:HEM201 3.1 16.5 1.0 C1B B:HEM201 3.2 17.1 1.0 CHA B:HEM201 3.4 16.7 1.0 CHD B:HEM201 3.5 13.6 1.0 CHC B:HEM201 3.5 17.3 1.0 CHB B:HEM201 3.5 17.7 1.0 CZ B:PHE511 3.5 17.1 1.0 CE1 B:PHE511 3.6 17.0 1.0 CE2 B:TYR383 3.7 12.0 1.0 CE1 B:TYR383 3.7 14.1 1.0 CE2 B:PHE511 4.0 19.5 1.0 CD1 B:PHE511 4.1 17.3 1.0 C2A B:HEM201 4.3 20.2 1.0 C3A B:HEM201 4.3 17.2 1.0 C2D B:HEM201 4.3 16.0 1.0 C3D B:HEM201 4.3 16.6 1.0 C3B B:HEM201 4.3 20.7 1.0 C3C B:HEM201 4.3 13.9 1.0 C2B B:HEM201 4.4 19.2 1.0 C2C B:HEM201 4.4 15.2 1.0 CD2 B:PHE511 4.5 16.8 1.0 CG B:PHE511 4.6 16.8 1.0 CD1 B:LEU438 4.9 14.4 1.0 CD2 B:TYR383 4.9 13.0 1.0 CD1 B:TYR383 4.9 14.8 1.0

N.Muraki, C.Kitatsuji, Y.Okamoto, T.Uchida, K.Ishimori, S.Aono. Structural Basis For the Heme Transfer Reaction in Heme Uptake Machinery From Corynebacteria. Chem.Commun.(Camb.) V. 55 13864 2019.
ISSN: ESSN 1364-548X
PubMed: 31670736
DOI: 10.1039/C9CC07369H