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Iron in PDB 6jt0: Structure of Human Soluble Guanylate Cyclase in the Unliganded State

Enzymatic activity of Structure of Human Soluble Guanylate Cyclase in the Unliganded State

All present enzymatic activity of Structure of Human Soluble Guanylate Cyclase in the Unliganded State:
4.6.1.2;

Iron Binding Sites:

The binding sites of Iron atom in the Structure of Human Soluble Guanylate Cyclase in the Unliganded State (pdb code 6jt0). 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 Unliganded State, PDB code: 6jt0:

Iron binding site 1 out of 1 in 6jt0

Go back to Iron Binding Sites List in 6jt0
Iron binding site 1 out of 1 in the Structure of Human Soluble Guanylate Cyclase in the Unliganded 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 Unliganded State within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe1000

b:94.0
occ:1.00
FE B:HEM1000 0.0 94.0 1.0
NB B:HEM1000 2.0 80.3 1.0
NA B:HEM1000 2.0 77.3 1.0
ND B:HEM1000 2.0 76.0 1.0
NC B:HEM1000 2.0 75.0 1.0
C1B B:HEM1000 3.0 78.1 1.0
C4B B:HEM1000 3.0 69.5 1.0
C1C B:HEM1000 3.0 70.9 1.0
C4A B:HEM1000 3.1 64.0 1.0
C1A B:HEM1000 3.1 83.2 1.0
C1D B:HEM1000 3.1 70.7 1.0
C4C B:HEM1000 3.1 73.8 1.0
C4D B:HEM1000 3.1 77.5 1.0
CHC B:HEM1000 3.4 65.3 1.0
CHB B:HEM1000 3.4 69.1 1.0
CHD B:HEM1000 3.4 74.0 1.0
CHA B:HEM1000 3.4 93.6 1.0
NE2 B:HIS105 3.6 61.8 1.0
CZ B:PHE74 3.7 69.3 1.0
CE1 B:PHE74 3.9 70.0 1.0
C2B B:HEM1000 4.2 72.9 1.0
C3B B:HEM1000 4.2 64.9 1.0
C2C B:HEM1000 4.3 72.1 1.0
C3D B:HEM1000 4.3 64.8 1.0
C2A B:HEM1000 4.3 75.0 1.0
C3C B:HEM1000 4.3 71.6 1.0
C3A B:HEM1000 4.3 66.7 1.0
C2D B:HEM1000 4.3 71.3 1.0
CD2 B:HIS105 4.3 62.7 1.0
CE1 B:HIS105 4.4 64.5 1.0
CE2 B:PHE74 4.8 81.8 1.0

Reference:

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
Page generated: Sun Dec 13 16:36:05 2020

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