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Iron in PDB 1czj: Cytochrome C of Class III (Ambler) 26 Kd

Protein crystallography data

The structure of Cytochrome C of Class III (Ambler) 26 Kd, PDB code: 1czj was solved by M.Czjzek, R.Haser, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 12.00 / 2.16
Space group P 31 2 1
Cell size a, b, c (Å), α, β, γ (°) 73.710, 73.710, 57.250, 90.00, 90.00, 120.00
R / Rfree (%) 20.4 / 26.3

Iron Binding Sites:

The binding sites of Iron atom in the Cytochrome C of Class III (Ambler) 26 Kd (pdb code 1czj). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 4 binding sites of Iron where determined in the Cytochrome C of Class III (Ambler) 26 Kd, PDB code: 1czj:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in 1czj

Go back to Iron Binding Sites List in 1czj
Iron binding site 1 out of 4 in the Cytochrome C of Class III (Ambler) 26 Kd


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Cytochrome C of Class III (Ambler) 26 Kd within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe119

b:10.8
occ:1.00
FE A:HEM119 0.0 10.8 1.0
NA A:HEM119 1.9 10.9 1.0
NE2 A:HIS30 2.0 7.9 1.0
NC A:HEM119 2.0 8.0 1.0
ND A:HEM119 2.0 9.7 1.0
NB A:HEM119 2.0 12.2 1.0
NE2 A:HIS42 2.0 6.8 1.0
CE1 A:HIS30 2.9 7.5 1.0
C4A A:HEM119 3.0 10.2 1.0
CE1 A:HIS42 3.0 8.8 1.0
C1D A:HEM119 3.0 10.0 1.0
C4C A:HEM119 3.0 9.2 1.0
C1A A:HEM119 3.0 14.4 1.0
C4D A:HEM119 3.0 10.5 1.0
CD2 A:HIS30 3.0 8.0 1.0
C1C A:HEM119 3.0 9.1 1.0
C1B A:HEM119 3.1 12.2 1.0
C4B A:HEM119 3.1 11.8 1.0
CD2 A:HIS42 3.1 10.3 1.0
CHD A:HEM119 3.4 7.9 1.0
CHB A:HEM119 3.4 11.0 1.0
CHA A:HEM119 3.4 12.7 1.0
CHC A:HEM119 3.4 11.5 1.0
ND1 A:HIS30 4.1 9.8 1.0
ND1 A:HIS42 4.1 10.3 1.0
CG A:HIS30 4.2 7.8 1.0
C3A A:HEM119 4.2 9.9 1.0
CG A:HIS42 4.2 8.2 1.0
C2D A:HEM119 4.2 13.3 1.0
C3D A:HEM119 4.2 15.2 1.0
C3C A:HEM119 4.2 9.1 1.0
C2C A:HEM119 4.2 5.3 1.0
C2A A:HEM119 4.3 14.4 1.0
C2B A:HEM119 4.3 11.8 1.0
C3B A:HEM119 4.3 13.8 1.0
CE2 A:PHE28 4.6 7.2 1.0

Iron binding site 2 out of 4 in 1czj

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Iron binding site 2 out of 4 in the Cytochrome C of Class III (Ambler) 26 Kd


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Cytochrome C of Class III (Ambler) 26 Kd within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe120

b:19.1
occ:1.00
FE A:HEM120 0.0 19.1 1.0
NA A:HEM120 2.0 17.4 1.0
ND A:HEM120 2.0 21.0 1.0
NB A:HEM120 2.0 19.0 1.0
NC A:HEM120 2.0 15.2 1.0
NE2 A:HIS60 2.0 19.8 1.0
NE2 A:HIS43 2.0 19.6 1.0
CE1 A:HIS43 2.9 18.2 1.0
CE1 A:HIS60 3.0 22.7 1.0
C1A A:HEM120 3.0 19.2 1.0
C4B A:HEM120 3.0 18.0 1.0
C4D A:HEM120 3.0 18.6 1.0
C1D A:HEM120 3.0 18.3 1.0
C1C A:HEM120 3.0 15.8 1.0
C4A A:HEM120 3.0 16.8 1.0
C4C A:HEM120 3.0 18.5 1.0
CD2 A:HIS60 3.1 20.8 1.0
C1B A:HEM120 3.1 16.1 1.0
CD2 A:HIS43 3.1 13.6 1.0
CHA A:HEM120 3.3 18.7 1.0
CHC A:HEM120 3.4 16.2 1.0
CHD A:HEM120 3.4 17.4 1.0
CHB A:HEM120 3.5 14.8 1.0
ND1 A:HIS43 4.1 16.7 1.0
ND1 A:HIS60 4.1 20.4 1.0
CG A:HIS60 4.2 21.6 1.0
CG A:HIS43 4.2 14.7 1.0
C2A A:HEM120 4.2 21.8 1.0
C2D A:HEM120 4.2 18.2 1.0
C3D A:HEM120 4.2 19.4 1.0
C3B A:HEM120 4.3 16.1 1.0
C3A A:HEM120 4.3 16.6 1.0
C2B A:HEM120 4.3 16.1 1.0
C2C A:HEM120 4.3 13.0 1.0
C3C A:HEM120 4.3 17.5 1.0
CE A:LYS84 4.8 8.1 1.0
CG2 A:THR44 5.0 4.0 1.0

Iron binding site 3 out of 4 in 1czj

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Iron binding site 3 out of 4 in the Cytochrome C of Class III (Ambler) 26 Kd


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Cytochrome C of Class III (Ambler) 26 Kd within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe121

b:13.0
occ:1.00
FE A:HEM121 0.0 13.0 1.0
ND A:HEM121 2.0 9.2 1.0
NC A:HEM121 2.0 6.6 1.0
NA A:HEM121 2.0 8.4 1.0
NB A:HEM121 2.0 10.3 1.0
NE2 A:HIS90 2.0 7.8 1.0
NE2 A:HIS33 2.0 10.6 1.0
CE1 A:HIS90 2.9 10.4 1.0
C1D A:HEM121 3.0 13.7 1.0
C4C A:HEM121 3.0 12.4 1.0
CD2 A:HIS33 3.0 6.3 1.0
C1A A:HEM121 3.0 8.6 1.0
C1C A:HEM121 3.0 7.1 1.0
C4A A:HEM121 3.0 8.6 1.0
C4B A:HEM121 3.0 6.8 1.0
C4D A:HEM121 3.0 3.3 1.0
CE1 A:HIS33 3.1 8.7 1.0
C1B A:HEM121 3.1 9.4 1.0
CD2 A:HIS90 3.1 8.7 1.0
CHD A:HEM121 3.4 12.5 1.0
CHA A:HEM121 3.4 8.1 1.0
CHC A:HEM121 3.4 2.4 1.0
CHB A:HEM121 3.4 9.7 1.0
ND1 A:HIS90 4.1 7.3 1.0
CG A:HIS33 4.2 6.4 1.0
ND1 A:HIS33 4.2 6.8 1.0
CG A:HIS90 4.2 10.8 1.0
C2D A:HEM121 4.2 10.9 1.0
C2A A:HEM121 4.2 10.8 1.0
C3A A:HEM121 4.2 9.7 1.0
C3C A:HEM121 4.2 9.6 1.0
C2C A:HEM121 4.3 8.9 1.0
C3D A:HEM121 4.3 11.6 1.0
C3B A:HEM121 4.3 11.9 1.0
C2B A:HEM121 4.3 9.9 1.0

Iron binding site 4 out of 4 in 1czj

Go back to Iron Binding Sites List in 1czj
Iron binding site 4 out of 4 in the Cytochrome C of Class III (Ambler) 26 Kd


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Cytochrome C of Class III (Ambler) 26 Kd within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe122

b:21.2
occ:1.00
FE A:HEM122 0.0 21.2 1.0
NB A:HEM122 1.9 24.5 1.0
NC A:HEM122 2.0 20.4 1.0
NE2 A:HIS109 2.0 16.7 1.0
NE2 A:HIS77 2.0 16.0 1.0
NA A:HEM122 2.0 24.8 1.0
ND A:HEM122 2.0 22.3 1.0
CE1 A:HIS109 2.8 14.2 1.0
CE1 A:HIS77 2.9 13.0 1.0
C4B A:HEM122 3.0 22.5 1.0
C1B A:HEM122 3.0 25.6 1.0
C1C A:HEM122 3.0 22.8 1.0
C4C A:HEM122 3.0 20.8 1.0
CD2 A:HIS77 3.0 14.0 1.0
C4A A:HEM122 3.0 28.1 1.0
C1D A:HEM122 3.1 21.3 1.0
C1A A:HEM122 3.1 28.7 1.0
C4D A:HEM122 3.1 25.2 1.0
CD2 A:HIS109 3.1 18.0 1.0
CHC A:HEM122 3.4 21.7 1.0
CHB A:HEM122 3.4 26.0 1.0
CHD A:HEM122 3.4 19.0 1.0
CHA A:HEM122 3.5 27.3 1.0
ND1 A:HIS109 4.0 11.8 1.0
ND1 A:HIS77 4.1 15.9 1.0
CG A:HIS77 4.2 9.8 1.0
C3B A:HEM122 4.2 25.9 1.0
CG A:HIS109 4.2 16.4 1.0
C2B A:HEM122 4.2 28.0 1.0
C3C A:HEM122 4.2 23.7 1.0
C2C A:HEM122 4.3 21.4 1.0
C3A A:HEM122 4.3 29.8 1.0
C2D A:HEM122 4.3 24.4 1.0
C2A A:HEM122 4.3 30.9 1.0
C3D A:HEM122 4.3 25.1 1.0

Reference:

M.Czjzek, F.Guerlesquin, M.Bruschi, R.Haser. Crystal Structure of A Dimeric Octaheme Cytochrome C3 (M(R) 26,000) From Desulfovibrio Desulfuricans Norway. Structure V. 4 395 1996.
ISSN: ISSN 0969-2126
PubMed: 8740362
DOI: 10.1016/S0969-2126(96)00045-7
Page generated: Wed Jul 16 13:07:45 2025

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