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Iron in PDB 1kwj: Solution Structure Determination of the Fully Oxidized Double Mutant K9-10A Cytochrome C7 From Desulfuromonas Acetoxidans, Minimized Average Structure

Iron Binding Sites:

The binding sites of Iron atom in the Solution Structure Determination of the Fully Oxidized Double Mutant K9-10A Cytochrome C7 From Desulfuromonas Acetoxidans, Minimized Average Structure (pdb code 1kwj). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 3 binding sites of Iron where determined in the Solution Structure Determination of the Fully Oxidized Double Mutant K9-10A Cytochrome C7 From Desulfuromonas Acetoxidans, Minimized Average Structure, PDB code: 1kwj:
Jump to Iron binding site number: 1; 2; 3;

Iron binding site 1 out of 3 in 1kwj

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Iron binding site 1 out of 3 in the Solution Structure Determination of the Fully Oxidized Double Mutant K9-10A Cytochrome C7 From Desulfuromonas Acetoxidans, Minimized Average Structure


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Solution Structure Determination of the Fully Oxidized Double Mutant K9-10A Cytochrome C7 From Desulfuromonas Acetoxidans, Minimized Average Structure within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe130

b:10.0
occ:1.00
FE A:HEC130 0.0 10.0 1.0
NA A:HEC130 1.9 10.0 1.0
NB A:HEC130 1.9 10.0 1.0
NC A:HEC130 1.9 10.0 1.0
ND A:HEC130 2.0 10.0 1.0
NE2 A:HIS17 2.0 10.0 1.0
NE2 A:HIS30 2.0 10.0 1.0
C4A A:HEC130 2.9 10.0 1.0
C1B A:HEC130 2.9 10.0 1.0
C4B A:HEC130 2.9 10.0 1.0
C4C A:HEC130 2.9 10.0 1.0
C1A A:HEC130 2.9 10.0 1.0
C1C A:HEC130 2.9 10.0 1.0
C1D A:HEC130 2.9 10.0 1.0
C4D A:HEC130 3.0 10.0 1.0
CE1 A:HIS30 3.0 10.0 1.0
CE1 A:HIS17 3.0 10.0 1.0
CD2 A:HIS17 3.0 10.0 1.0
CD2 A:HIS30 3.1 10.0 1.0
HE1 A:HIS30 3.2 10.0 1.0
CHB A:HEC130 3.3 10.0 1.0
HD2 A:HIS17 3.3 10.0 1.0
HE1 A:HIS17 3.3 10.0 1.0
CHC A:HEC130 3.3 10.0 1.0
CHD A:HEC130 3.3 10.0 1.0
HD2 A:HIS30 3.3 10.0 1.0
CHA A:HEC130 3.4 10.0 1.0
C3A A:HEC130 4.1 10.0 1.0
C2B A:HEC130 4.1 10.0 1.0
C2A A:HEC130 4.1 10.0 1.0
C3B A:HEC130 4.1 10.0 1.0
ND1 A:HIS17 4.1 10.0 1.0
ND1 A:HIS30 4.1 10.0 1.0
C3C A:HEC130 4.2 10.0 1.0
CG A:HIS17 4.2 10.0 1.0
C2C A:HEC130 4.2 10.0 1.0
C2D A:HEC130 4.2 10.0 1.0
CG A:HIS30 4.2 10.0 1.0
C3D A:HEC130 4.2 10.0 1.0
HHB A:HEC130 4.3 10.0 1.0
HHC A:HEC130 4.4 10.0 1.0
HHD A:HEC130 4.4 10.0 1.0
HHA A:HEC130 4.4 10.0 1.0
HB2 A:PRO34 4.6 10.0 1.0
HB2 A:CYS29 4.8 10.0 1.0

Iron binding site 2 out of 3 in 1kwj

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Iron binding site 2 out of 3 in the Solution Structure Determination of the Fully Oxidized Double Mutant K9-10A Cytochrome C7 From Desulfuromonas Acetoxidans, Minimized Average Structure


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Solution Structure Determination of the Fully Oxidized Double Mutant K9-10A Cytochrome C7 From Desulfuromonas Acetoxidans, Minimized Average Structure within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe153

b:10.0
occ:1.00
FE A:HEC153 0.0 10.0 1.0
NB A:HEC153 1.9 10.0 1.0
NA A:HEC153 1.9 10.0 1.0
ND A:HEC153 1.9 10.0 1.0
NC A:HEC153 2.0 10.0 1.0
NE2 A:HIS20 2.0 10.0 1.0
NE2 A:HIS53 2.0 10.0 1.0
C4B A:HEC153 2.9 10.0 1.0
C1B A:HEC153 2.9 10.0 1.0
C1A A:HEC153 2.9 10.0 1.0
C1C A:HEC153 2.9 10.0 1.0
C1D A:HEC153 2.9 10.0 1.0
C4A A:HEC153 2.9 10.0 1.0
C4D A:HEC153 2.9 10.0 1.0
CE1 A:HIS20 3.0 10.0 1.0
C4C A:HEC153 3.0 10.0 1.0
CE1 A:HIS53 3.0 10.0 1.0
CD2 A:HIS20 3.1 10.0 1.0
CD2 A:HIS53 3.1 10.0 1.0
HE1 A:HIS53 3.2 10.0 1.0
HE1 A:HIS20 3.2 10.0 1.0
CHC A:HEC153 3.3 10.0 1.0
CHA A:HEC153 3.3 10.0 1.0
CHB A:HEC153 3.3 10.0 1.0
CHD A:HEC153 3.4 10.0 1.0
HD2 A:HIS20 3.4 10.0 1.0
HD2 A:HIS53 3.4 10.0 1.0
ND1 A:HIS20 4.1 10.0 1.0
C3B A:HEC153 4.1 10.0 1.0
C2B A:HEC153 4.1 10.0 1.0
ND1 A:HIS53 4.2 10.0 1.0
C2A A:HEC153 4.2 10.0 1.0
C3A A:HEC153 4.2 10.0 1.0
C2D A:HEC153 4.2 10.0 1.0
C3D A:HEC153 4.2 10.0 1.0
C2C A:HEC153 4.2 10.0 1.0
C3C A:HEC153 4.2 10.0 1.0
CG A:HIS20 4.2 10.0 1.0
CG A:HIS53 4.2 10.0 1.0
HHC A:HEC153 4.4 10.0 1.0
HHA A:HEC153 4.4 10.0 1.0
HHB A:HEC153 4.4 10.0 1.0
HHD A:HEC153 4.4 10.0 1.0
HB3 A:CYS49 4.8 10.0 1.0

Iron binding site 3 out of 3 in 1kwj

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Iron binding site 3 out of 3 in the Solution Structure Determination of the Fully Oxidized Double Mutant K9-10A Cytochrome C7 From Desulfuromonas Acetoxidans, Minimized Average Structure


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Solution Structure Determination of the Fully Oxidized Double Mutant K9-10A Cytochrome C7 From Desulfuromonas Acetoxidans, Minimized Average Structure within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe166

b:10.0
occ:1.00
FE A:HEC166 0.0 10.0 1.0
NA A:HEC166 1.9 10.0 1.0
NB A:HEC166 1.9 10.0 1.0
NC A:HEC166 1.9 10.0 1.0
ND A:HEC166 2.0 10.0 1.0
NE2 A:HIS45 2.0 10.0 1.0
NE2 A:HIS66 2.0 10.0 1.0
C4A A:HEC166 2.9 10.0 1.0
C1B A:HEC166 2.9 10.0 1.0
C1A A:HEC166 2.9 10.0 1.0
C1C A:HEC166 2.9 10.0 1.0
C4B A:HEC166 2.9 10.0 1.0
C1D A:HEC166 2.9 10.0 1.0
CE1 A:HIS66 2.9 10.0 1.0
C4C A:HEC166 2.9 10.0 1.0
CE1 A:HIS45 3.0 10.0 1.0
C4D A:HEC166 3.0 10.0 1.0
CD2 A:HIS45 3.1 10.0 1.0
CD2 A:HIS66 3.1 10.0 1.0
HE1 A:HIS66 3.1 10.0 1.0
HE1 A:HIS45 3.2 10.0 1.0
CHB A:HEC166 3.3 10.0 1.0
CHA A:HEC166 3.3 10.0 1.0
CHC A:HEC166 3.3 10.0 1.0
CHD A:HEC166 3.3 10.0 1.0
HD2 A:HIS45 3.4 10.0 1.0
HD2 A:HIS66 3.4 10.0 1.0
ND1 A:HIS66 4.1 10.0 1.0
ND1 A:HIS45 4.1 10.0 1.0
C3A A:HEC166 4.1 10.0 1.0
C2A A:HEC166 4.1 10.0 1.0
C2B A:HEC166 4.1 10.0 1.0
C3B A:HEC166 4.2 10.0 1.0
C2C A:HEC166 4.2 10.0 1.0
C2D A:HEC166 4.2 10.0 1.0
C3C A:HEC166 4.2 10.0 1.0
CG A:HIS45 4.2 10.0 1.0
CG A:HIS66 4.2 10.0 1.0
C3D A:HEC166 4.2 10.0 1.0
HHB A:HEC166 4.4 10.0 1.0
HHA A:HEC166 4.4 10.0 1.0
HHC A:HEC166 4.4 10.0 1.0
HHD A:HEC166 4.4 10.0 1.0
HA A:LYS41 4.9 10.0 1.0
HB2 A:CYS65 4.9 10.0 1.0
HB3 A:ALA10 4.9 10.0 1.0

Reference:

M.Assfalg, I.Bertini, P.Turano, M.Bruschi, M.C.Durand, M.T.Giudici-Orticoni, A.Dolla. A Quick Solution Structure Determination of the Fully Oxidized Double Mutant K9-10A Cytochrome C7 From Desulfuromonas Acetoxidans and Mechanistic Implications. J.Biomol.uc(Nmr) V. 22 107 2002.
ISSN: ISSN 0925-2738
PubMed: 11883773
DOI: 10.1023/A:1014202405862
Page generated: Sat Aug 3 09:30:32 2024

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