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Iron in PDB 1noe: uc(Nmr) Study of Reduced High Potential Iron Sulfur Protein

Iron Binding Sites:

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

Iron binding site 1 out of 4 in 1noe

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Iron binding site 1 out of 4 in the uc(Nmr) Study of Reduced 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 uc(Nmr) Study of Reduced 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 2.2 0.0 1.0
S3 A:SF486 2.2 0.0 1.0
S4 A:SF486 2.2 0.0 1.0
S2 A:SF486 2.2 0.0 1.0
FE2 A:SF486 2.6 0.0 1.0
FE4 A:SF486 2.6 0.0 1.0
FE3 A:SF486 2.7 0.0 1.0
HG13 A:ILE71 3.0 0.0 1.0
HA A:CYS43 3.1 0.0 1.0
CB A:CYS43 3.2 0.0 1.0
HB3 A:CYS43 3.3 0.0 1.0
CA A:CYS43 3.7 0.0 1.0
S1 A:SF486 3.8 0.0 1.0
HA A:TRP76 3.9 0.0 1.0
CG1 A:ILE71 4.0 0.0 1.0
HB3 A:SER77 4.1 0.0 1.0
HG12 A:ILE71 4.1 0.0 1.0
H A:SER77 4.1 0.0 1.0
HB2 A:CYS63 4.1 0.0 1.0
HB2 A:CYS46 4.1 0.0 1.0
HB2 A:CYS43 4.2 0.0 1.0
HD13 A:ILE71 4.2 0.0 1.0
HD1 A:TYR19 4.2 0.0 1.0
N A:SER77 4.4 0.0 1.0
HB3 A:CYS46 4.4 0.0 1.0
HD1 A:TRP80 4.4 0.0 1.0
H A:CYS43 4.4 0.0 1.0
N A:CYS43 4.4 0.0 1.0
HG23 A:ILE71 4.4 0.0 1.0
SG A:CYS46 4.5 0.0 1.0
OG A:SER77 4.5 0.0 1.0
CB A:CYS46 4.6 0.0 1.0
SG A:CYS63 4.6 0.0 1.0
HE1 A:TYR19 4.7 0.0 1.0
CD1 A:ILE71 4.7 0.0 1.0
CB A:SER77 4.7 0.0 1.0
C A:TRP76 4.7 0.0 1.0
CA A:TRP76 4.7 0.0 1.0
HB A:ILE71 4.8 0.0 1.0
HA A:TRP80 4.8 0.0 1.0
C A:CYS43 4.9 0.0 1.0
CB A:CYS63 4.9 0.0 1.0
CD1 A:TYR19 4.9 0.0 1.0
HG3 A:MET49 5.0 0.0 1.0
CB A:ILE71 5.0 0.0 1.0

Iron binding site 2 out of 4 in 1noe

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Iron binding site 2 out of 4 in the uc(Nmr) Study of Reduced 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 uc(Nmr) Study of Reduced 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 2.1 0.0 1.0
S1 A:SF486 2.2 0.0 1.0
S4 A:SF486 2.2 0.0 1.0
S3 A:SF486 2.2 0.0 1.0
FE3 A:SF486 2.6 0.0 1.0
FE1 A:SF486 2.6 0.0 1.0
FE4 A:SF486 2.6 0.0 1.0
CB A:CYS46 3.1 0.0 1.0
HA A:TRP80 3.1 0.0 1.0
HB2 A:CYS46 3.1 0.0 1.0
HB3 A:CYS46 3.2 0.0 1.0
HA A:CYS43 3.6 0.0 1.0
HB2 A:PHE48 3.7 0.0 1.0
S2 A:SF486 3.7 0.0 1.0
HD2 A:PHE48 3.8 0.0 1.0
HD1 A:TRP80 3.9 0.0 1.0
CA A:TRP80 4.2 0.0 1.0
O A:SER79 4.2 0.0 1.0
HB2 A:MET49 4.3 0.0 1.0
O A:TRP80 4.3 0.0 1.0
CA A:CYS46 4.4 0.0 1.0
SG A:CYS63 4.5 0.0 1.0
SG A:CYS43 4.5 0.0 1.0
OG A:SER77 4.6 0.0 1.0
H A:PHE48 4.6 0.0 1.0
HB2 A:TRP80 4.6 0.0 1.0
CA A:CYS43 4.7 0.0 1.0
HA A:CYS46 4.7 0.0 1.0
CD1 A:TRP80 4.7 0.0 1.0
HB3 A:CYS43 4.7 0.0 1.0
C A:TRP80 4.7 0.0 1.0
CB A:PHE48 4.8 0.0 1.0
H A:MET49 4.8 0.0 1.0
CD2 A:PHE48 4.8 0.0 1.0
HA A:MET49 4.8 0.0 1.0
HG A:SER79 4.8 0.0 1.0
CB A:TRP80 4.9 0.0 1.0
C A:SER79 4.9 0.0 1.0
CB A:CYS43 4.9 0.0 1.0
N A:TRP80 4.9 0.0 1.0
N A:MET49 4.9 0.0 1.0
H A:SER77 4.9 0.0 1.0

Iron binding site 3 out of 4 in 1noe

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Iron binding site 3 out of 4 in the uc(Nmr) Study of Reduced 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 uc(Nmr) Study of Reduced 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 2.1 0.0 1.0
S1 A:SF486 2.2 0.0 1.0
S2 A:SF486 2.2 0.0 1.0
S4 A:SF486 2.2 0.0 1.0
FE4 A:SF486 2.6 0.0 1.0
FE2 A:SF486 2.6 0.0 1.0
FE1 A:SF486 2.7 0.0 1.0
HB2 A:CYS63 2.9 0.0 1.0
CB A:CYS63 3.1 0.0 1.0
S3 A:SF486 3.7 0.0 1.0
HG13 A:ILE71 3.8 0.0 1.0
HE1 A:PHE66 3.8 0.0 1.0
HA A:CYS63 3.9 0.0 1.0
HB3 A:CYS63 3.9 0.0 1.0
CA A:CYS63 4.1 0.0 1.0
HD11 A:LEU17 4.1 0.0 1.0
HG23 A:ILE71 4.1 0.0 1.0
HB2 A:PHE48 4.4 0.0 1.0
HD1 A:PHE66 4.5 0.0 1.0
OG A:SER77 4.5 0.0 1.0
SG A:CYS46 4.5 0.0 1.0
CE1 A:PHE66 4.5 0.0 1.0
H A:GLN64 4.5 0.0 1.0
HD13 A:ILE71 4.6 0.0 1.0
HA A:MET49 4.6 0.0 1.0
SG A:CYS43 4.7 0.0 1.0
HG3 A:MET49 4.8 0.0 1.0
CG1 A:ILE71 4.8 0.0 1.0
CD1 A:PHE66 4.8 0.0 1.0
HB3 A:SER77 4.8 0.0 1.0
H A:LEU65 4.9 0.0 1.0
HD11 A:ILE71 4.9 0.0 1.0
C A:CYS63 5.0 0.0 1.0
HD13 A:LEU17 5.0 0.0 1.0

Iron binding site 4 out of 4 in 1noe

Go back to Iron Binding Sites List in 1noe
Iron binding site 4 out of 4 in the uc(Nmr) Study of Reduced 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 uc(Nmr) Study of Reduced 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
OG A:SER77 2.1 0.0 1.0
S1 A:SF486 2.2 0.0 1.0
S3 A:SF486 2.2 0.0 1.0
S2 A:SF486 2.2 0.0 1.0
FE3 A:SF486 2.6 0.0 1.0
FE1 A:SF486 2.6 0.0 1.0
FE2 A:SF486 2.6 0.0 1.0
HB3 A:SER77 3.0 0.0 1.0
CB A:SER77 3.1 0.0 1.0
HD11 A:LEU17 3.4 0.0 1.0
H A:SER77 3.6 0.0 1.0
HA A:TRP80 3.7 0.0 1.0
S4 A:SF486 3.7 0.0 1.0
HG A:SER79 3.8 0.0 1.0
N A:SER77 3.8 0.0 1.0
CA A:SER77 3.9 0.0 1.0
HB2 A:SER77 4.0 0.0 1.0
O A:SER79 4.1 0.0 1.0
C A:SER77 4.3 0.0 1.0
HD12 A:LEU17 4.3 0.0 1.0
CD1 A:LEU17 4.3 0.0 1.0
HB2 A:TRP80 4.4 0.0 1.0
HE1 A:PHE66 4.4 0.0 1.0
HB3 A:LEU17 4.4 0.0 1.0
C A:SER79 4.4 0.0 1.0
O A:SER77 4.5 0.0 1.0
SG A:CYS63 4.5 0.0 1.0
OG A:SER79 4.5 0.0 1.0
H A:SER79 4.5 0.0 1.0
SG A:CYS43 4.5 0.0 1.0
SG A:CYS46 4.5 0.0 1.0
CA A:TRP80 4.6 0.0 1.0
HD1 A:TYR19 4.6 0.0 1.0
N A:TRP80 4.7 0.0 1.0
HD13 A:LEU17 4.8 0.0 1.0
C A:TRP76 4.8 0.0 1.0
HA A:SER77 4.9 0.0 1.0
HA A:TRP76 4.9 0.0 1.0
HB2 A:TYR19 4.9 0.0 1.0
HD1 A:TRP80 5.0 0.0 1.0
N A:SER79 5.0 0.0 1.0
N A:ALA78 5.0 0.0 1.0

Reference:

D.Bentrop, I.Bertini, F.Capozzi, A.Dikiy, L.Eltis, C.Luchinat. Three-Dimensional Structure of the Reduced C77S Mutant of the Chromatium Vinosum High-Potential Iron-Sulfur Protein Through Nuclear Magnetic Resonance: Comparison with the Solution Structure of the Wild-Type Protein. Biochemistry V. 35 5928 1996.
ISSN: ISSN 0006-2960
PubMed: 8639555
DOI: 10.1021/BI9528513
Page generated: Sat Aug 3 11:57:18 2024

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