Iron in PDB 6jt2: Structure of Human Soluble Guanylate Cyclase in the No Activated State

All present enzymatic activity of Structure of Human Soluble Guanylate Cyclase in the No Activated State:
4.6.1.2;

The structure of Structure of Human Soluble Guanylate Cyclase in the No Activated State also contains other interesting chemical elements:

Magnesium

(Mg)

2 atoms

The binding sites of Iron atom in the Structure of Human Soluble Guanylate Cyclase in the No Activated State (pdb code 6jt2). 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 Structure of Human Soluble Guanylate Cyclase in the No Activated State, PDB code: 6jt2:

Iron binding site 1 out of 1 in the Structure of Human Soluble Guanylate Cyclase in the No Activated State


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Structure of Human Soluble Guanylate Cyclase in the No Activated State within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe1000 b:53.4 occ:1.00 FE B:HEM1000 0.0 53.4 1.0 NB B:HEM1000 2.0 38.8 1.0 ND B:HEM1000 2.0 31.5 1.0 NA B:HEM1000 2.0 42.9 1.0 NC B:HEM1000 2.1 34.0 1.0 C4A B:HEM1000 3.0 52.0 1.0 C1B B:HEM1000 3.0 46.1 1.0 C4D B:HEM1000 3.1 26.0 1.0 C1C B:HEM1000 3.1 35.5 1.0 C1A B:HEM1000 3.1 34.6 1.0 C4B B:HEM1000 3.1 36.8 1.0 C1D B:HEM1000 3.1 35.9 1.0 C4C B:HEM1000 3.1 32.7 1.0 CHB B:HEM1000 3.4 56.9 1.0 CHC B:HEM1000 3.4 37.1 1.0 CHA B:HEM1000 3.4 24.2 1.0 CHD B:HEM1000 3.5 34.9 1.0 NE2 B:HIS105 3.9 54.5 1.0 C3A B:HEM1000 4.2 48.1 1.0 C2B B:HEM1000 4.3 38.8 1.0 C2A B:HEM1000 4.3 43.5 1.0 C3D B:HEM1000 4.3 29.1 1.0 C2D B:HEM1000 4.3 35.3 1.0 C2C B:HEM1000 4.3 37.3 1.0 C3B B:HEM1000 4.3 37.5 1.0 C3C B:HEM1000 4.3 30.1 1.0 CD2 B:HIS105 4.4 48.6 1.0 CZ B:PHE74 4.5 71.6 1.0 CE2 B:PHE74 4.7 81.7 1.0 CD1 B:LEU108 4.8 61.8 1.0 CE1 B:HIS105 5.0 76.3 1.0

Y.Kang, R.Liu, J.X.Wu, L.Chen. Structural Insights Into the Mechanism of Human Soluble Guanylate Cyclase. Nature V. 574 206 2019.
ISSN: ESSN 1476-4687
PubMed: 31514202
DOI: 10.1038/S41586-019-1584-6