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Iron in PDB 8a1t: Sodium Pumping Nadh-Quinone Oxidoreductase

Enzymatic activity of Sodium Pumping Nadh-Quinone Oxidoreductase

All present enzymatic activity of Sodium Pumping Nadh-Quinone Oxidoreductase:
7.2.1.1;

Other elements in 8a1t:

The structure of Sodium Pumping Nadh-Quinone Oxidoreductase also contains other interesting chemical elements:

Potassium (K) 1 atom
Sodium (Na) 1 atom

Iron Binding Sites:

The binding sites of Iron atom in the Sodium Pumping Nadh-Quinone Oxidoreductase (pdb code 8a1t). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 4 binding sites of Iron where determined in the Sodium Pumping Nadh-Quinone Oxidoreductase, PDB code: 8a1t:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in 8a1t

Go back to Iron Binding Sites List in 8a1t
Iron binding site 1 out of 4 in the Sodium Pumping Nadh-Quinone Oxidoreductase


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Sodium Pumping Nadh-Quinone Oxidoreductase within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Fe302

b:92.7
occ:1.00
FE1 D:FES302 0.0 92.7 1.0
S2 D:FES302 2.2 77.7 1.0
S1 D:FES302 2.2 76.5 1.0
SG E:CYS26 2.3 74.3 1.0
SG D:CYS112 2.3 80.7 1.0
FE2 D:FES302 2.7 88.1 1.0
HB2 E:CYS26 2.9 56.3 1.0
CB E:CYS26 3.1 59.7 1.0
HB2 D:CYS112 3.2 68.6 1.0
H D:CYS112 3.2 68.9 1.0
CB D:CYS112 3.4 71.4 1.0
H D:GLY27 3.4 55.1 1.0
H E:CYS26 3.6 54.2 1.0
HB3 E:CYS26 3.7 55.0 1.0
N D:CYS112 3.9 66.3 1.0
HA D:LEU26 4.1 56.9 1.0
HB3 D:CYS112 4.1 69.5 1.0
SG D:CYS29 4.2 62.8 1.0
CA D:CYS112 4.2 68.9 1.0
N D:GLY27 4.3 57.2 1.0
N E:CYS26 4.3 46.9 1.0
CA E:CYS26 4.4 48.9 1.0
H D:VAL28 4.4 48.0 1.0
HA D:ASN111 4.5 61.8 1.0
SG E:CYS120 4.5 64.8 1.0
HA D:CYS112 4.6 69.3 1.0
HG13 D:VAL28 4.6 47.5 1.0
H D:CYS29 4.6 53.2 1.0
O D:THR110 4.6 71.1 1.0
HB2 E:CYS120 4.6 62.4 1.0
HA2 D:GLY27 4.7 54.5 1.0
H E:THR27 4.8 47.6 1.0
O D:VAL25 4.8 54.6 1.0
HG12 D:VAL28 4.8 47.3 1.0
HA2 E:GLY24 4.9 52.3 1.0
HA E:CYS26 4.9 53.4 1.0
CA D:LEU26 5.0 55.0 1.0

Iron binding site 2 out of 4 in 8a1t

Go back to Iron Binding Sites List in 8a1t
Iron binding site 2 out of 4 in the Sodium Pumping Nadh-Quinone Oxidoreductase


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Sodium Pumping Nadh-Quinone Oxidoreductase within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Fe302

b:88.1
occ:1.00
FE2 D:FES302 0.0 88.1 1.0
S1 D:FES302 2.2 76.5 1.0
S2 D:FES302 2.2 77.7 1.0
SG E:CYS120 2.3 64.8 1.0
SG D:CYS29 2.3 62.8 1.0
HB2 E:CYS120 2.6 62.4 1.0
FE1 D:FES302 2.7 92.7 1.0
CB E:CYS120 2.9 62.2 1.0
HB2 D:CYS29 3.2 53.3 1.0
HB3 E:CYS120 3.3 61.2 1.0
CB D:CYS29 3.4 53.8 1.0
H E:GLY24 3.5 52.7 1.0
HB3 D:CYS29 3.9 52.8 1.0
H D:CYS29 3.9 53.2 1.0
H E:CYS120 3.9 61.6 1.0
HA2 E:GLY24 4.0 52.3 1.0
HA D:ASN111 4.1 61.8 1.0
SG E:CYS26 4.2 74.3 1.0
N E:GLY24 4.2 48.5 1.0
H E:MET25 4.2 48.2 1.0
CA E:CYS120 4.3 58.6 1.0
HG22 D:THR110 4.3 69.7 1.0
H E:CYS26 4.3 54.2 1.0
H D:CYS112 4.3 68.9 1.0
N E:CYS120 4.5 54.9 1.0
CA E:GLY24 4.5 49.0 1.0
O D:THR110 4.6 71.1 1.0
SG D:CYS112 4.6 80.7 1.0
N D:CYS29 4.6 55.6 1.0
CA D:CYS29 4.6 51.1 1.0
HA E:CYS120 4.6 62.4 1.0
N E:MET25 4.8 46.6 1.0
HA E:LEU23 4.8 53.4 1.0
HB2 E:CYS26 4.9 56.3 1.0
HG13 D:VAL28 5.0 47.5 1.0
HA D:CYS29 5.0 52.5 1.0
HB D:THR110 5.0 70.3 1.0

Iron binding site 3 out of 4 in 8a1t

Go back to Iron Binding Sites List in 8a1t
Iron binding site 3 out of 4 in the Sodium Pumping Nadh-Quinone Oxidoreductase


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Sodium Pumping Nadh-Quinone Oxidoreductase within 5.0Å range:
probe atom residue distance (Å) B Occ
F:Fe1502

b:241.4
occ:1.00
FE1 F:FES1502 0.0 241.4 1.0
HG F:CYS76 1.1 208.7 1.0
S2 F:FES1502 2.2 237.2 1.0
S1 F:FES1502 2.2 236.4 1.0
SG F:CYS76 2.3 210.3 1.0
SG F:CYS70 2.3 213.2 1.0
H F:CYS76 2.5 208.6 1.0
FE2 F:FES1502 2.7 239.6 1.0
H F:GLY77 2.7 202.5 1.0
H F:CYS70 3.1 210.2 1.0
H F:SER75 3.3 202.0 1.0
N F:CYS76 3.3 209.7 1.0
CB F:CYS76 3.5 208.3 1.0
N F:GLY77 3.5 203.1 1.0
CB F:CYS70 3.5 210.4 1.0
HB3 F:CYS70 3.6 210.3 1.0
HB3 F:CYS76 3.6 208.4 1.0
H F:ALA69 3.7 202.9 1.0
N F:CYS70 3.8 210.6 1.0
H F:GLN78 3.8 199.5 1.0
CA F:CYS76 3.8 208.8 1.0
H F:GLY71 3.9 205.0 1.0
N F:SER75 4.0 202.6 1.0
HA2 F:GLY74 4.0 200.2 1.0
O F:GLY71 4.0 206.4 1.0
CA F:CYS70 4.1 210.3 1.0
H F:GLY74 4.1 200.3 1.0
HG F:CYS111 4.2 201.7 1.0
N F:GLY71 4.2 205.0 1.0
C F:CYS76 4.2 208.0 1.0
SG F:CYS111 4.3 205.7 1.0
HB2 F:CYS76 4.3 208.3 1.0
HB2 F:CYS70 4.3 210.2 1.0
C F:CYS70 4.3 210.1 1.0
H F:CYS79 4.4 198.7 1.0
C F:SER75 4.4 202.7 1.0
N F:GLN78 4.5 199.6 1.0
HA F:SER68 4.5 195.8 1.0
N F:ALA69 4.5 203.2 1.0
HA2 F:GLY77 4.5 202.2 1.0
SG F:CYS79 4.5 199.8 1.0
CA F:GLY77 4.5 202.2 1.0
CA F:GLY74 4.6 200.5 1.0
N F:GLY74 4.6 200.9 1.0
C F:GLY74 4.6 200.2 1.0
HB2 F:SER68 4.7 195.8 1.0
CA F:SER75 4.7 202.1 1.0
HA F:CYS76 4.7 208.4 1.0
HB3 F:CYS79 4.8 198.5 1.0
HB1 F:ALA69 4.8 202.9 1.0
C F:ALA69 4.9 203.5 1.0
H F:GLY73 4.9 196.9 1.0
HB2 F:GLN78 4.9 199.2 1.0
HB3 F:SER75 4.9 201.8 1.0
HG3 F:GLN78 4.9 199.3 1.0
HD13 F:LEU109 4.9 193.7 1.0
C F:GLY71 5.0 205.4 1.0
HA F:CYS70 5.0 210.2 1.0
C F:GLY77 5.0 201.9 1.0

Iron binding site 4 out of 4 in 8a1t

Go back to Iron Binding Sites List in 8a1t
Iron binding site 4 out of 4 in the Sodium Pumping Nadh-Quinone Oxidoreductase


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Sodium Pumping Nadh-Quinone Oxidoreductase within 5.0Å range:
probe atom residue distance (Å) B Occ
F:Fe1502

b:239.6
occ:1.00
FE2 F:FES1502 0.0 239.6 1.0
HG F:CYS111 1.8 201.7 1.0
S2 F:FES1502 2.2 237.2 1.0
S1 F:FES1502 2.2 236.4 1.0
SG F:CYS111 2.3 205.7 1.0
SG F:CYS79 2.3 199.8 1.0
FE1 F:FES1502 2.7 241.4 1.0
HB3 F:CYS111 3.1 201.6 1.0
CB F:CYS111 3.3 202.1 1.0
HB3 F:LEU109 3.4 193.8 1.0
H F:CYS111 3.4 201.5 1.0
HB3 F:CYS79 3.5 198.5 1.0
HA2 F:GLY74 3.5 200.2 1.0
CB F:CYS79 3.6 198.7 1.0
HG F:CYS76 3.6 208.7 1.0
O F:GLY71 3.8 206.4 1.0
H F:CYS79 3.8 198.7 1.0
H F:GLY74 3.9 200.3 1.0
HB2 F:CYS111 4.0 201.5 1.0
H F:GLY77 4.0 202.5 1.0
HD13 F:LEU109 4.1 193.7 1.0
N F:CYS111 4.2 202.1 1.0
H F:GLN112 4.2 194.6 1.0
HB2 F:CYS79 4.2 198.6 1.0
HD22 F:LEU109 4.2 193.8 1.0
SG F:CYS70 4.3 213.2 1.0
CA F:CYS111 4.3 201.5 1.0
CA F:GLY74 4.4 200.5 1.0
CB F:LEU109 4.4 193.9 1.0
N F:CYS79 4.5 198.6 1.0
N F:GLY74 4.5 200.9 1.0
SG F:CYS76 4.5 210.3 1.0
CA F:CYS79 4.6 198.6 1.0
HA2 F:GLY77 4.7 202.2 1.0
H F:SER75 4.7 202.0 1.0
HB3 F:SER68 4.7 195.7 1.0
N F:GLN112 4.8 195.0 1.0
HB2 F:SER68 4.8 195.8 1.0
H F:CYS76 4.8 208.6 1.0
N F:GLY77 4.8 203.1 1.0
HB2 F:LEU109 4.8 193.7 1.0
H F:GLN78 4.9 199.5 1.0
H F:ALA110 4.9 194.6 1.0
HA F:LEU109 4.9 193.6 1.0
HA F:SER68 4.9 195.8 1.0
H F:GLY73 4.9 196.9 1.0
HD22 F:LEU56 4.9 190.9 1.0
CD1 F:LEU109 4.9 193.3 1.0
C F:GLY71 5.0 205.4 1.0
HA3 F:GLY74 5.0 200.1 1.0

Reference:

J.-L.Hau, J.-L.Hau, S.Kaltwasser, J.Vonck, G.Fritz, J.Steuber. N/A N/A.
Page generated: Fri Aug 9 16:02:19 2024

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