Iron in PDB 1f22: A Proton-uc(Nmr) Investigation of the Fully Reduced Cytochrome C7 From Desulfuromonas Acetoxidans. Comparison Between the Reduced and the Oxidized Forms.

The binding sites of Iron atom in the A Proton-uc(Nmr) Investigation of the Fully Reduced Cytochrome C7 From Desulfuromonas Acetoxidans. Comparison Between the Reduced and the Oxidized Forms. (pdb code 1f22). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 3 binding sites of Iron where determined in the A Proton-uc(Nmr) Investigation of the Fully Reduced Cytochrome C7 From Desulfuromonas Acetoxidans. Comparison Between the Reduced and the Oxidized Forms., PDB code: 1f22:
Jump to Iron binding site number: 1; 2; 3;

Iron binding site 1 out of 3 in the A Proton-uc(Nmr) Investigation of the Fully Reduced Cytochrome C7 From Desulfuromonas Acetoxidans. Comparison Between the Reduced and the Oxidized Forms.


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of A Proton-uc(Nmr) Investigation of the Fully Reduced Cytochrome C7 From Desulfuromonas Acetoxidans. Comparison Between the Reduced and the Oxidized Forms. within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe69 b:0.0 occ:1.00 FE A:HEC69 0.0 0.0 1.0 NE2 A:HIS17 1.9 0.0 1.0 NE2 A:HIS30 1.9 0.0 1.0 NB A:HEC69 2.0 0.0 1.0 NC A:HEC69 2.0 0.0 1.0 ND A:HEC69 2.0 0.0 1.0 NA A:HEC69 2.0 0.0 1.0 CE1 A:HIS17 2.9 0.0 1.0 CD2 A:HIS30 2.9 0.0 1.0 CD2 A:HIS17 3.0 0.0 1.0 CE1 A:HIS30 3.0 0.0 1.0 C1B A:HEC69 3.0 0.0 1.0 C1C A:HEC69 3.0 0.0 1.0 C4B A:HEC69 3.0 0.0 1.0 C4C A:HEC69 3.0 0.0 1.0 C4A A:HEC69 3.0 0.0 1.0 C1D A:HEC69 3.0 0.0 1.0 C4D A:HEC69 3.0 0.0 1.0 C1A A:HEC69 3.0 0.0 1.0 HD2 A:HIS30 3.1 0.0 1.0 HE1 A:HIS17 3.1 0.0 1.0 HE1 A:HIS30 3.2 0.0 1.0 HD2 A:HIS17 3.3 0.0 1.0 CHC A:HEC69 3.4 0.0 1.0 CHB A:HEC69 3.4 0.0 1.0 CHD A:HEC69 3.4 0.0 1.0 CHA A:HEC69 3.4 0.0 1.0 ND1 A:HIS17 4.0 0.0 1.0 CG A:HIS17 4.1 0.0 1.0 CG A:HIS30 4.1 0.0 1.0 ND1 A:HIS30 4.1 0.0 1.0 C2B A:HEC69 4.2 0.0 1.0 C3B A:HEC69 4.2 0.0 1.0 C2C A:HEC69 4.2 0.0 1.0 C3C A:HEC69 4.2 0.0 1.0 C3D A:HEC69 4.2 0.0 1.0 C2D A:HEC69 4.2 0.0 1.0 C3A A:HEC69 4.2 0.0 1.0 C2A A:HEC69 4.3 0.0 1.0 HB2 A:PRO34 4.4 0.0 1.0 HD11 A:ILE37 4.4 0.0 1.0 HHC A:HEC69 4.5 0.0 1.0 HHB A:HEC69 4.5 0.0 1.0 HHD A:HEC69 4.5 0.0 1.0 HHA A:HEC69 4.5 0.0 1.0 HB3 A:PRO34 4.5 0.0 1.0 H3 A:ALA1 4.5 0.0 1.0 HB2 A:CYS29 4.7 0.0 1.0 HG13 A:ILE37 4.8 0.0 1.0 HD1 A:HIS17 4.9 0.0 1.0 CB A:PRO34 5.0 0.0 1.0

Iron binding site 2 out of 3 in the A Proton-uc(Nmr) Investigation of the Fully Reduced Cytochrome C7 From Desulfuromonas Acetoxidans. Comparison Between the Reduced and the Oxidized Forms.


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of A Proton-uc(Nmr) Investigation of the Fully Reduced Cytochrome C7 From Desulfuromonas Acetoxidans. Comparison Between the Reduced and the Oxidized Forms. within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe70 b:0.0 occ:1.00 FE A:HEC70 0.0 0.0 1.0 NE2 A:HIS20 2.0 0.0 1.0 NE2 A:HIS53 2.0 0.0 1.0 NB A:HEC70 2.0 0.0 1.0 NA A:HEC70 2.0 0.0 1.0 ND A:HEC70 2.0 0.0 1.0 NC A:HEC70 2.1 0.0 1.0 CE1 A:HIS53 3.0 0.0 1.0 CE1 A:HIS20 3.0 0.0 1.0 C1B A:HEC70 3.0 0.0 1.0 C4B A:HEC70 3.0 0.0 1.0 C1A A:HEC70 3.0 0.0 1.0 C4A A:HEC70 3.0 0.0 1.0 C4D A:HEC70 3.0 0.0 1.0 C1D A:HEC70 3.0 0.0 1.0 C1C A:HEC70 3.0 0.0 1.0 C4C A:HEC70 3.1 0.0 1.0 CD2 A:HIS20 3.1 0.0 1.0 CD2 A:HIS53 3.1 0.0 1.0 HE1 A:HIS53 3.2 0.0 1.0 HE1 A:HIS20 3.2 0.0 1.0 HD2 A:HIS53 3.3 0.0 1.0 HD2 A:HIS20 3.3 0.0 1.0 CHB A:HEC70 3.4 0.0 1.0 CHA A:HEC70 3.4 0.0 1.0 CHC A:HEC70 3.4 0.0 1.0 CHD A:HEC70 3.5 0.0 1.0 ND1 A:HIS53 4.1 0.0 1.0 ND1 A:HIS20 4.1 0.0 1.0 CG A:HIS20 4.2 0.0 1.0 CG A:HIS53 4.2 0.0 1.0 C2B A:HEC70 4.2 0.0 1.0 C3B A:HEC70 4.2 0.0 1.0 C2A A:HEC70 4.2 0.0 1.0 C3A A:HEC70 4.2 0.0 1.0 C3D A:HEC70 4.3 0.0 1.0 C2D A:HEC70 4.3 0.0 1.0 C2C A:HEC70 4.3 0.0 1.0 C3C A:HEC70 4.3 0.0 1.0 HHB A:HEC70 4.5 0.0 1.0 HHA A:HEC70 4.5 0.0 1.0 HHC A:HEC70 4.5 0.0 1.0 HHD A:HEC70 4.5 0.0 1.0 HD12 A:LEU24 4.7 0.0 1.0 HB2 A:ASP16 4.8 0.0 1.0 HD21 A:ASN56 4.9 0.0 1.0

Iron binding site 3 out of 3 in the A Proton-uc(Nmr) Investigation of the Fully Reduced Cytochrome C7 From Desulfuromonas Acetoxidans. Comparison Between the Reduced and the Oxidized Forms.


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of A Proton-uc(Nmr) Investigation of the Fully Reduced Cytochrome C7 From Desulfuromonas Acetoxidans. Comparison Between the Reduced and the Oxidized Forms. within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe71 b:0.0 occ:1.00 FE A:HEC71 0.0 0.0 1.0 NE2 A:HIS66 1.9 0.0 1.0 NE2 A:HIS45 2.0 0.0 1.0 NA A:HEC71 2.0 0.0 1.0 NB A:HEC71 2.0 0.0 1.0 ND A:HEC71 2.0 0.0 1.0 NC A:HEC71 2.1 0.0 1.0 CE1 A:HIS66 2.9 0.0 1.0 CE1 A:HIS45 2.9 0.0 1.0 CD2 A:HIS66 2.9 0.0 1.0 C4A A:HEC71 3.0 0.0 1.0 C1A A:HEC71 3.0 0.0 1.0 C1B A:HEC71 3.0 0.0 1.0 C4B A:HEC71 3.0 0.0 1.0 C4D A:HEC71 3.0 0.0 1.0 C1C A:HEC71 3.0 0.0 1.0 C1D A:HEC71 3.1 0.0 1.0 C4C A:HEC71 3.1 0.0 1.0 CD2 A:HIS45 3.1 0.0 1.0 HE1 A:HIS45 3.1 0.0 1.0 HE1 A:HIS66 3.1 0.0 1.0 HD2 A:HIS66 3.2 0.0 1.0 HD2 A:HIS45 3.4 0.0 1.0 CHB A:HEC71 3.4 0.0 1.0 CHA A:HEC71 3.4 0.0 1.0 CHC A:HEC71 3.5 0.0 1.0 CHD A:HEC71 3.5 0.0 1.0 ND1 A:HIS66 4.0 0.0 1.0 CG A:HIS66 4.1 0.0 1.0 ND1 A:HIS45 4.1 0.0 1.0 CG A:HIS45 4.2 0.0 1.0 HZ1 A:LYS10 4.2 0.0 1.0 C3A A:HEC71 4.2 0.0 1.0 C2A A:HEC71 4.2 0.0 1.0 C2B A:HEC71 4.2 0.0 1.0 C3B A:HEC71 4.3 0.0 1.0 C3D A:HEC71 4.3 0.0 1.0 C2D A:HEC71 4.3 0.0 1.0 C2C A:HEC71 4.3 0.0 1.0 C3C A:HEC71 4.3 0.0 1.0 HG2 A:LYS10 4.3 0.0 1.0 HHB A:HEC71 4.5 0.0 1.0 HHA A:HEC71 4.5 0.0 1.0 HG23 A:VAL13 4.5 0.0 1.0 HHC A:HEC71 4.5 0.0 1.0 HHD A:HEC71 4.5 0.0 1.0 HG21 A:VAL13 4.9 0.0 1.0 HD1 A:HIS66 5.0 0.0 1.0 HD1 A:HIS45 5.0 0.0 1.0

M.Assfalg, L.Banci, I.Bertini, M.Bruschi, M.T.Giudici-Orticoni. A Proton-uc(Nmr) Investigation of the Fully Reduced Cytochrome C7 From Desulfuromonas Acetoxidans. Comparison Between the Reduced and the Oxidized Forms. Eur.J.Biochem. V. 266 634 1999.
ISSN: ISSN 0014-2956
PubMed: 10561607
DOI: 10.1046/J.1432-1327.1999.00904.X