Iron in PDB 8u7y: Structural Basis of Human NOX5 Activation

Other elements in 8u7y:

The structure of Structural Basis of Human NOX5 Activation also contains other interesting chemical elements:

Zinc (Zn) 1 atom

Iron Binding Sites:

The binding sites of Iron atom in the Structural Basis of Human NOX5 Activation (pdb code 8u7y). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 4 binding sites of Iron where determined in the Structural Basis of Human NOX5 Activation, PDB code: 8u7y:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in 8u7y

Go back to Iron Binding Sites List in 8u7y
Iron binding site 1 out of 4 in the Structural Basis of Human NOX5 Activation


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Structural Basis of Human NOX5 Activation within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe805

b:53.3
occ:1.00
FE A:HEB805 0.0 53.3 1.0
NC A:HEB805 2.0 53.3 1.0
NB A:HEB805 2.1 53.3 1.0
NA A:HEB805 2.1 53.3 1.0
ND A:HEB805 2.1 53.3 1.0
NE2 A:HIS356 2.7 58.4 1.0
NE2 A:HIS268 2.7 66.7 1.0
C4C A:HEB805 3.0 53.3 1.0
C1B A:HEB805 3.0 53.3 1.0
C1D A:HEB805 3.1 53.3 1.0
C1C A:HEB805 3.1 53.3 1.0
CE1 A:HIS356 3.1 58.4 1.0
C4A A:HEB805 3.1 53.3 1.0
C4B A:HEB805 3.1 53.3 1.0
C1A A:HEB805 3.1 53.3 1.0
C4D A:HEB805 3.1 53.3 1.0
CE1 A:HIS268 3.3 66.7 1.0
CHD A:HEB805 3.4 53.3 1.0
CHB A:HEB805 3.4 53.3 1.0
CHC A:HEB805 3.4 53.3 1.0
CHA A:HEB805 3.5 53.3 1.0
CD2 A:HIS268 3.8 66.7 1.0
CD2 A:HIS356 3.9 58.4 1.0
C2B A:HEB805 4.3 53.3 1.0
C3C A:HEB805 4.3 53.3 1.0
C2C A:HEB805 4.3 53.3 1.0
C3B A:HEB805 4.3 53.3 1.0
C2D A:HEB805 4.3 53.3 1.0
C3A A:HEB805 4.3 53.3 1.0
C2A A:HEB805 4.3 53.3 1.0
C3D A:HEB805 4.3 53.3 1.0
ND1 A:HIS356 4.3 58.4 1.0
ND1 A:HIS268 4.5 66.7 1.0
CG A:HIS356 4.8 58.4 1.0
CG A:HIS268 4.8 66.7 1.0
SD A:MET335 4.9 70.3 1.0

Iron binding site 2 out of 4 in 8u7y

Go back to Iron Binding Sites List in 8u7y
Iron binding site 2 out of 4 in the Structural Basis of Human NOX5 Activation


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Structural Basis of Human NOX5 Activation within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe806

b:37.4
occ:1.00
FE A:HEB806 0.0 37.4 1.0
NC A:HEB806 2.0 37.4 1.0
NA A:HEB806 2.0 37.4 1.0
NB A:HEB806 2.1 37.4 1.0
ND A:HEB806 2.1 37.4 1.0
NE2 A:HIS369 2.3 44.1 1.0
NE2 A:HIS282 2.9 46.2 1.0
C4C A:HEB806 3.0 37.4 1.0
C1D A:HEB806 3.0 37.4 1.0
C4A A:HEB806 3.0 37.4 1.0
C1A A:HEB806 3.1 37.4 1.0
C1B A:HEB806 3.1 37.4 1.0
C1C A:HEB806 3.1 37.4 1.0
C4B A:HEB806 3.1 37.4 1.0
C4D A:HEB806 3.1 37.4 1.0
CE1 A:HIS369 3.1 44.1 1.0
CHD A:HEB806 3.4 37.4 1.0
CD2 A:HIS282 3.4 46.2 1.0
CHB A:HEB806 3.4 37.4 1.0
CHA A:HEB806 3.4 37.4 1.0
CD2 A:HIS369 3.4 44.1 1.0
CHC A:HEB806 3.4 37.4 1.0
CE1 A:HIS282 3.9 46.2 1.0
C3A A:HEB806 4.2 37.4 1.0
C2A A:HEB806 4.2 37.4 1.0
C3C A:HEB806 4.3 37.4 1.0
C2B A:HEB806 4.3 37.4 1.0
C2C A:HEB806 4.3 37.4 1.0
C3B A:HEB806 4.3 37.4 1.0
C2D A:HEB806 4.3 37.4 1.0
ND1 A:HIS369 4.3 44.1 1.0
C3D A:HEB806 4.3 37.4 1.0
CG A:HIS369 4.5 44.1 1.0
CG A:HIS282 4.6 46.2 1.0
ND1 A:HIS282 4.8 46.2 1.0

Iron binding site 3 out of 4 in 8u7y

Go back to Iron Binding Sites List in 8u7y
Iron binding site 3 out of 4 in the Structural Basis of Human NOX5 Activation


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Structural Basis of Human NOX5 Activation within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe805

b:52.5
occ:1.00
FE B:HEB805 0.0 52.5 1.0
NC B:HEB805 2.0 52.5 1.0
NB B:HEB805 2.1 52.5 1.0
NA B:HEB805 2.1 52.5 1.0
ND B:HEB805 2.1 52.5 1.0
NE2 B:HIS356 2.7 57.3 1.0
NE2 B:HIS268 2.7 66.8 1.0
C4C B:HEB805 3.0 52.5 1.0
C1B B:HEB805 3.0 52.5 1.0
C1D B:HEB805 3.1 52.5 1.0
C1C B:HEB805 3.1 52.5 1.0
CE1 B:HIS356 3.1 57.3 1.0
C4A B:HEB805 3.1 52.5 1.0
C4B B:HEB805 3.1 52.5 1.0
C1A B:HEB805 3.1 52.5 1.0
C4D B:HEB805 3.1 52.5 1.0
CE1 B:HIS268 3.3 66.8 1.0
CHD B:HEB805 3.4 52.5 1.0
CHB B:HEB805 3.4 52.5 1.0
CHC B:HEB805 3.4 52.5 1.0
CHA B:HEB805 3.5 52.5 1.0
CD2 B:HIS268 3.8 66.8 1.0
CD2 B:HIS356 3.9 57.3 1.0
C2B B:HEB805 4.3 52.5 1.0
C3C B:HEB805 4.3 52.5 1.0
C2C B:HEB805 4.3 52.5 1.0
C3B B:HEB805 4.3 52.5 1.0
C2D B:HEB805 4.3 52.5 1.0
C3A B:HEB805 4.3 52.5 1.0
C2A B:HEB805 4.3 52.5 1.0
C3D B:HEB805 4.3 52.5 1.0
ND1 B:HIS356 4.3 57.3 1.0
ND1 B:HIS268 4.5 66.8 1.0
CG B:HIS356 4.8 57.3 1.0
CG B:HIS268 4.8 66.8 1.0
SD B:MET335 4.9 69.2 1.0

Iron binding site 4 out of 4 in 8u7y

Go back to Iron Binding Sites List in 8u7y
Iron binding site 4 out of 4 in the Structural Basis of Human NOX5 Activation


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Structural Basis of Human NOX5 Activation within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe806

b:35.5
occ:1.00
FE B:HEB806 0.0 35.5 1.0
NC B:HEB806 2.0 35.5 1.0
NA B:HEB806 2.0 35.5 1.0
NB B:HEB806 2.1 35.5 1.0
ND B:HEB806 2.1 35.5 1.0
NE2 B:HIS369 2.3 43.6 1.0
NE2 B:HIS282 2.9 45.5 1.0
C4C B:HEB806 3.0 35.5 1.0
C1D B:HEB806 3.0 35.5 1.0
C4A B:HEB806 3.0 35.5 1.0
C1A B:HEB806 3.1 35.5 1.0
C1B B:HEB806 3.1 35.5 1.0
C1C B:HEB806 3.1 35.5 1.0
C4B B:HEB806 3.1 35.5 1.0
C4D B:HEB806 3.1 35.5 1.0
CE1 B:HIS369 3.1 43.6 1.0
CHD B:HEB806 3.4 35.5 1.0
CD2 B:HIS282 3.4 45.5 1.0
CHB B:HEB806 3.4 35.5 1.0
CHA B:HEB806 3.4 35.5 1.0
CD2 B:HIS369 3.4 43.6 1.0
CHC B:HEB806 3.4 35.5 1.0
CE1 B:HIS282 3.9 45.5 1.0
C3A B:HEB806 4.2 35.5 1.0
C2A B:HEB806 4.2 35.5 1.0
C3C B:HEB806 4.3 35.5 1.0
C2B B:HEB806 4.3 35.5 1.0
C2C B:HEB806 4.3 35.5 1.0
C3B B:HEB806 4.3 35.5 1.0
C2D B:HEB806 4.3 35.5 1.0
ND1 B:HIS369 4.3 43.6 1.0
C3D B:HEB806 4.3 35.5 1.0
CG B:HIS369 4.5 43.6 1.0
CG B:HIS282 4.6 45.5 1.0
ND1 B:HIS282 4.8 45.5 1.0

Reference:

C.Cui, M.Jiang, J.Sun. Structural Basis of Human NOX5 Activation To Be Published.
Page generated: Sat Aug 10 18:25:58 2024

Last articles

Zn in 9J0N
Zn in 9J0O
Zn in 9J0P
Zn in 9FJX
Zn in 9EKB
Zn in 9C0F
Zn in 9CAH
Zn in 9CH0
Zn in 9CH3
Zn in 9CH1
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy