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Iron in PDB 1neh: High Potential Iron-Sulfur Protein

Iron Binding Sites:

The binding sites of Iron atom in the High Potential Iron-Sulfur Protein (pdb code 1neh). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 4 binding sites of Iron where determined in the High Potential Iron-Sulfur Protein, PDB code: 1neh:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in 1neh

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Iron binding site 1 out of 4 in the High Potential Iron-Sulfur Protein


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of High Potential Iron-Sulfur Protein within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe86

b:0.0
occ:1.00
FE1 A:SF486 0.0 0.0 1.0
SG A:CYS43 2.0 0.0 1.0
S3 A:SF486 2.1 0.0 1.0
S2 A:SF486 2.2 0.0 1.0
S4 A:SF486 2.2 0.0 1.0
FE2 A:SF486 2.5 0.0 1.0
FE4 A:SF486 2.5 0.0 1.0
FE3 A:SF486 2.5 0.0 1.0
HA A:CYS43 3.0 0.0 1.0
CB A:CYS43 3.1 0.0 1.0
HB3 A:CYS43 3.2 0.0 1.0
HG12 A:ILE71 3.4 0.0 1.0
CA A:CYS43 3.6 0.0 1.0
S1 A:SF486 3.6 0.0 1.0
HG23 A:ILE71 3.9 0.0 1.0
HB3 A:CYS77 4.0 0.0 1.0
HB2 A:CYS43 4.0 0.0 1.0
HB2 A:CYS46 4.1 0.0 1.0
H A:CYS77 4.1 0.0 1.0
HA A:TRP76 4.1 0.0 1.0
HB3 A:CYS46 4.1 0.0 1.0
SG A:CYS46 4.2 0.0 1.0
HB A:ILE71 4.3 0.0 1.0
N A:CYS43 4.3 0.0 1.0
SG A:CYS77 4.3 0.0 1.0
H A:CYS43 4.3 0.0 1.0
CB A:CYS46 4.4 0.0 1.0
SG A:CYS63 4.4 0.0 1.0
N A:CYS77 4.4 0.0 1.0
CG1 A:ILE71 4.4 0.0 1.0
HB2 A:CYS63 4.5 0.0 1.0
HD2 A:TYR19 4.6 0.0 1.0
CB A:CYS77 4.6 0.0 1.0
HD11 A:ILE71 4.7 0.0 1.0
HD12 A:ILE71 4.7 0.0 1.0
HD1 A:TRP80 4.8 0.0 1.0
CB A:ILE71 4.8 0.0 1.0
CG2 A:ILE71 4.8 0.0 1.0
C A:CYS43 4.8 0.0 1.0
C A:TRP76 4.8 0.0 1.0
CD1 A:ILE71 4.9 0.0 1.0
O A:PHE48 4.9 0.0 1.0
CA A:TRP76 4.9 0.0 1.0
HA A:CYS63 4.9 0.0 1.0
CB A:CYS63 4.9 0.0 1.0
HA A:TRP80 5.0 0.0 1.0

Iron binding site 2 out of 4 in 1neh

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Iron binding site 2 out of 4 in the High Potential Iron-Sulfur Protein


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of High Potential Iron-Sulfur Protein within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe86

b:0.0
occ:1.00
FE2 A:SF486 0.0 0.0 1.0
SG A:CYS46 2.0 0.0 1.0
S1 A:SF486 2.1 0.0 1.0
S3 A:SF486 2.2 0.0 1.0
S4 A:SF486 2.2 0.0 1.0
FE3 A:SF486 2.5 0.0 1.0
FE4 A:SF486 2.5 0.0 1.0
FE1 A:SF486 2.5 0.0 1.0
CB A:CYS46 3.0 0.0 1.0
HB3 A:CYS46 3.1 0.0 1.0
HB2 A:CYS46 3.1 0.0 1.0
O A:PHE48 3.3 0.0 1.0
HA A:TRP80 3.4 0.0 1.0
HB2 A:PHE48 3.4 0.0 1.0
HA A:CYS43 3.5 0.0 1.0
S2 A:SF486 3.6 0.0 1.0
O A:SER79 3.6 0.0 1.0
C A:PHE48 4.0 0.0 1.0
H A:PHE48 4.2 0.0 1.0
HB2 A:MET49 4.2 0.0 1.0
HD1 A:TRP80 4.2 0.0 1.0
SG A:CYS43 4.3 0.0 1.0
SG A:CYS77 4.3 0.0 1.0
SG A:CYS63 4.3 0.0 1.0
CB A:PHE48 4.4 0.0 1.0
CA A:CYS46 4.4 0.0 1.0
CA A:TRP80 4.4 0.0 1.0
CA A:CYS43 4.5 0.0 1.0
HB3 A:CYS43 4.5 0.0 1.0
CA A:PHE48 4.6 0.0 1.0
C A:SER79 4.6 0.0 1.0
HA A:MET49 4.6 0.0 1.0
N A:PHE48 4.6 0.0 1.0
CB A:CYS43 4.7 0.0 1.0
HB3 A:PHE48 4.7 0.0 1.0
HA A:CYS46 4.7 0.0 1.0
O A:TRP80 4.8 0.0 1.0
H A:CYS77 4.8 0.0 1.0
N A:MET49 4.8 0.0 1.0
HD2 A:PHE48 4.9 0.0 1.0
H A:GLN64 4.9 0.0 1.0
C A:CYS46 4.9 0.0 1.0
HA A:CYS63 4.9 0.0 1.0
N A:TRP80 4.9 0.0 1.0

Iron binding site 3 out of 4 in 1neh

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Iron binding site 3 out of 4 in the High Potential Iron-Sulfur Protein


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of High Potential Iron-Sulfur Protein within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe86

b:0.0
occ:1.00
FE3 A:SF486 0.0 0.0 1.0
SG A:CYS63 2.0 0.0 1.0
S1 A:SF486 2.1 0.0 1.0
S2 A:SF486 2.2 0.0 1.0
S4 A:SF486 2.2 0.0 1.0
FE2 A:SF486 2.5 0.0 1.0
FE4 A:SF486 2.5 0.0 1.0
FE1 A:SF486 2.5 0.0 1.0
CB A:CYS63 3.2 0.0 1.0
O A:PHE48 3.2 0.0 1.0
HB2 A:CYS63 3.2 0.0 1.0
HA A:CYS63 3.6 0.0 1.0
S3 A:SF486 3.6 0.0 1.0
HG12 A:ILE71 3.7 0.0 1.0
HG23 A:ILE71 3.8 0.0 1.0
HD2 A:PHE66 3.8 0.0 1.0
H A:GLN64 3.8 0.0 1.0
CA A:CYS63 3.9 0.0 1.0
H A:LEU65 4.0 0.0 1.0
HB3 A:CYS63 4.1 0.0 1.0
HB2 A:LEU65 4.2 0.0 1.0
HG A:LEU65 4.2 0.0 1.0
HB2 A:PHE48 4.3 0.0 1.0
SG A:CYS77 4.3 0.0 1.0
SG A:CYS46 4.3 0.0 1.0
SG A:CYS43 4.3 0.0 1.0
HA A:MET49 4.3 0.0 1.0
HD11 A:LEU65 4.3 0.0 1.0
C A:PHE48 4.4 0.0 1.0
N A:GLN64 4.6 0.0 1.0
C A:CYS63 4.7 0.0 1.0
HB3 A:PHE48 4.7 0.0 1.0
CG1 A:ILE71 4.7 0.0 1.0
HB3 A:CYS43 4.7 0.0 1.0
CG2 A:ILE71 4.8 0.0 1.0
CD2 A:PHE66 4.8 0.0 1.0
HB3 A:CYS77 4.8 0.0 1.0
H A:PHE66 4.8 0.0 1.0
HE2 A:PHE66 4.8 0.0 1.0
HD12 A:LEU17 4.8 0.0 1.0
HB3 A:CYS46 4.9 0.0 1.0
HA A:CYS43 4.9 0.0 1.0
CB A:PHE48 4.9 0.0 1.0
CG A:LEU65 5.0 0.0 1.0
N A:LEU65 5.0 0.0 1.0
O A:SER79 5.0 0.0 1.0
CB A:LEU65 5.0 0.0 1.0

Iron binding site 4 out of 4 in 1neh

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Iron binding site 4 out of 4 in the High Potential Iron-Sulfur Protein


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of High Potential Iron-Sulfur Protein within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe86

b:0.0
occ:1.00
FE4 A:SF486 0.0 0.0 1.0
SG A:CYS77 2.0 0.0 1.0
S1 A:SF486 2.1 0.0 1.0
S3 A:SF486 2.1 0.0 1.0
S2 A:SF486 2.2 0.0 1.0
FE2 A:SF486 2.5 0.0 1.0
FE1 A:SF486 2.5 0.0 1.0
FE3 A:SF486 2.5 0.0 1.0
HB3 A:CYS77 3.0 0.0 1.0
CB A:CYS77 3.1 0.0 1.0
O A:SER79 3.6 0.0 1.0
H A:CYS77 3.6 0.0 1.0
S4 A:SF486 3.6 0.0 1.0
N A:CYS77 3.9 0.0 1.0
CA A:CYS77 3.9 0.0 1.0
HB2 A:CYS77 4.0 0.0 1.0
HB2 A:SER79 4.0 0.0 1.0
HA A:TRP80 4.1 0.0 1.0
HD12 A:LEU17 4.1 0.0 1.0
HD11 A:LEU65 4.2 0.0 1.0
C A:SER79 4.2 0.0 1.0
SG A:CYS63 4.2 0.0 1.0
SG A:CYS46 4.2 0.0 1.0
SG A:CYS43 4.2 0.0 1.0
O A:CYS77 4.3 0.0 1.0
C A:CYS77 4.3 0.0 1.0
H A:SER79 4.6 0.0 1.0
HB2 A:PHE48 4.7 0.0 1.0
HB3 A:LEU17 4.7 0.0 1.0
HD2 A:TYR19 4.8 0.0 1.0
N A:TRP80 4.8 0.0 1.0
HA A:CYS43 4.9 0.0 1.0
HE2 A:PHE66 4.9 0.0 1.0
C A:TRP76 4.9 0.0 1.0
CB A:SER79 4.9 0.0 1.0
HA A:CYS77 4.9 0.0 1.0
CA A:TRP80 4.9 0.0 1.0
HG23 A:ILE71 4.9 0.0 1.0
CA A:SER79 4.9 0.0 1.0
N A:SER79 5.0 0.0 1.0
O A:PHE48 5.0 0.0 1.0
HB2 A:CYS46 5.0 0.0 1.0
HA A:TRP76 5.0 0.0 1.0

Reference:

I.Bertini, A.Dikiy, D.H.Kastrau, C.Luchinat, P.Sompornpisut. Three-Dimensional Solution Structure of the Oxidized High Potential Iron-Sulfur Protein From Chromatium Vinosum Through uc(Nmr). Comparative Analysis with the Solution Structure of the Reduced Species. Biochemistry V. 34 9851 1995.
ISSN: ISSN 0006-2960
PubMed: 7632685
DOI: 10.1021/BI00031A005
Page generated: Wed Jul 16 18:33:30 2025

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