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Iron in PDB 1hpi: Molecular Structure of the Oxidized High-Potential Iron-Sulfur Protein Isolated From Ectothiorhodospira Vacuolata

Protein crystallography data

The structure of Molecular Structure of the Oxidized High-Potential Iron-Sulfur Protein Isolated From Ectothiorhodospira Vacuolata, PDB code: 1hpi was solved by M.M.Benning, T.E.Meyer, I.Rayment, H.M.Holden, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) N/A / 1.80
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 58.400, 64.700, 39.300, 90.00, 90.00, 90.00
R / Rfree (%) n/a / n/a

Iron Binding Sites:

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

Iron binding site 1 out of 4 in 1hpi

Go back to Iron Binding Sites List in 1hpi
Iron binding site 1 out of 4 in the Molecular Structure of the Oxidized High-Potential Iron-Sulfur Protein Isolated From Ectothiorhodospira Vacuolata


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Molecular Structure of the Oxidized High-Potential Iron-Sulfur Protein Isolated From Ectothiorhodospira Vacuolata within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe80

b:8.5
occ:1.00
FE1 A:SF480 0.0 8.5 1.0
S4 A:SF480 2.2 8.2 1.0
S2 A:SF480 2.2 8.8 1.0
SG A:CYS34 2.2 7.8 1.0
S3 A:SF480 2.3 7.1 1.0
FE4 A:SF480 2.7 8.3 1.0
FE3 A:SF480 2.7 9.6 1.0
FE2 A:SF480 2.7 10.3 1.0
CB A:CYS34 3.2 4.3 1.0
CA A:CYS34 3.5 7.3 1.0
S1 A:SF480 3.8 8.3 1.0
CG2 A:VAL59 4.3 6.7 1.0
N A:CYS34 4.3 6.9 1.0
CA A:TRP64 4.6 7.2 1.0
CB A:CYS37 4.7 8.6 1.0
SG A:CYS37 4.7 7.5 1.0
C A:CYS34 4.7 16.6 1.0
N A:TRP64 4.7 6.4 1.0
SG A:CYS65 4.7 7.3 1.0
N A:CYS65 4.8 8.9 1.0
SG A:CYS51 4.8 8.6 1.0
C A:TRP64 4.8 7.6 1.0
CB A:VAL59 4.9 8.4 1.0
C A:GLY63 5.0 4.4 1.0
CE1 A:TYR16 5.0 8.8 1.0
O A:CYS34 5.0 7.4 1.0

Iron binding site 2 out of 4 in 1hpi

Go back to Iron Binding Sites List in 1hpi
Iron binding site 2 out of 4 in the Molecular Structure of the Oxidized High-Potential Iron-Sulfur Protein Isolated From Ectothiorhodospira Vacuolata


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Molecular Structure of the Oxidized High-Potential Iron-Sulfur Protein Isolated From Ectothiorhodospira Vacuolata within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe80

b:10.3
occ:1.00
FE2 A:SF480 0.0 10.3 1.0
S1 A:SF480 2.2 8.3 1.0
SG A:CYS37 2.2 7.5 1.0
S3 A:SF480 2.2 7.1 1.0
S4 A:SF480 2.3 8.2 1.0
FE1 A:SF480 2.7 8.5 1.0
FE3 A:SF480 2.7 9.6 1.0
FE4 A:SF480 2.7 8.3 1.0
CB A:CYS37 3.1 8.6 1.0
S2 A:SF480 3.9 8.8 1.0
CA A:TRP68 4.2 11.8 1.0
CB A:LEU39 4.4 8.7 1.0
CD1 A:TRP68 4.5 7.1 1.0
CA A:CYS37 4.5 7.1 1.0
N A:TRP68 4.5 8.6 1.0
CA A:CYS34 4.6 7.3 1.0
O A:ALA67 4.6 7.9 1.0
SG A:CYS51 4.6 8.6 1.0
C A:ALA67 4.7 7.2 1.0
SG A:CYS65 4.7 7.3 1.0
CB A:TRP68 4.8 5.6 1.0
SG A:CYS34 4.8 7.8 1.0
N A:LEU39 4.8 9.3 1.0
CA A:LEU39 4.9 6.9 1.0
N A:TYR40 4.9 7.8 1.0
CG A:LEU39 4.9 14.4 1.0
CG A:TRP68 4.9 9.1 1.0
C A:CYS37 5.0 10.9 1.0
CB A:CYS34 5.0 4.3 1.0
C A:LEU39 5.0 8.4 1.0

Iron binding site 3 out of 4 in 1hpi

Go back to Iron Binding Sites List in 1hpi
Iron binding site 3 out of 4 in the Molecular Structure of the Oxidized High-Potential Iron-Sulfur Protein Isolated From Ectothiorhodospira Vacuolata


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Molecular Structure of the Oxidized High-Potential Iron-Sulfur Protein Isolated From Ectothiorhodospira Vacuolata within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe80

b:9.6
occ:1.00
FE3 A:SF480 0.0 9.6 1.0
SG A:CYS51 2.2 8.6 1.0
S4 A:SF480 2.3 8.2 1.0
S1 A:SF480 2.3 8.3 1.0
S2 A:SF480 2.3 8.8 1.0
FE1 A:SF480 2.7 8.5 1.0
FE4 A:SF480 2.7 8.3 1.0
FE2 A:SF480 2.7 10.3 1.0
CB A:CYS51 3.3 8.3 1.0
S3 A:SF480 3.8 7.1 1.0
CG1 A:VAL53 4.3 13.9 1.0
CD2 A:PHE54 4.5 8.6 1.0
CA A:CYS51 4.5 11.3 1.0
SG A:CYS65 4.5 7.3 1.0
CB A:LEU39 4.5 8.7 1.0
CG2 A:VAL59 4.6 6.7 1.0
SG A:CYS34 4.7 7.8 1.0
SG A:CYS37 4.7 7.5 1.0
CE2 A:PHE54 4.8 4.8 1.0
C A:LEU39 4.9 8.4 1.0
O A:LEU39 4.9 8.5 1.0
CG1 A:VAL59 4.9 13.1 1.0

Iron binding site 4 out of 4 in 1hpi

Go back to Iron Binding Sites List in 1hpi
Iron binding site 4 out of 4 in the Molecular Structure of the Oxidized High-Potential Iron-Sulfur Protein Isolated From Ectothiorhodospira Vacuolata


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Molecular Structure of the Oxidized High-Potential Iron-Sulfur Protein Isolated From Ectothiorhodospira Vacuolata within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe80

b:8.3
occ:1.00
FE4 A:SF480 0.0 8.3 1.0
S3 A:SF480 2.2 7.1 1.0
SG A:CYS65 2.2 7.3 1.0
S2 A:SF480 2.3 8.8 1.0
S1 A:SF480 2.3 8.3 1.0
FE1 A:SF480 2.7 8.5 1.0
FE3 A:SF480 2.7 9.6 1.0
FE2 A:SF480 2.7 10.3 1.0
CB A:CYS65 3.3 3.1 1.0
N A:CYS65 3.7 8.9 1.0
S4 A:SF480 3.8 8.2 1.0
CA A:CYS65 3.9 8.2 1.0
O A:CYS65 4.3 4.8 1.0
C A:CYS65 4.3 8.8 1.0
N A:TRP68 4.3 8.6 1.0
C A:TRP64 4.4 7.6 1.0
C A:ALA67 4.6 7.2 1.0
CB A:ALA67 4.7 7.0 1.0
SG A:CYS51 4.7 8.6 1.0
SG A:CYS34 4.7 7.8 1.0
N A:ALA67 4.7 9.7 1.0
CA A:TRP68 4.7 11.8 1.0
CE2 A:PHE54 4.8 4.8 1.0
SG A:CYS37 4.8 7.5 1.0
CA A:ALA67 4.9 10.3 1.0
CG1 A:VAL53 4.9 13.9 1.0
CA A:TRP64 5.0 7.2 1.0

Reference:

M.M.Benning, T.E.Meyer, I.Rayment, H.M.Holden. Molecular Structure of the Oxidized High-Potential Iron-Sulfur Protein Isolated From Ectothiorhodospira Vacuolata. Biochemistry V. 33 2476 1994.
ISSN: ISSN 0006-2960
PubMed: 8117708
DOI: 10.1021/BI00175A016
Page generated: Sun Dec 13 14:17:54 2020

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