Iron in PDB 2lzz: Solution Structure of A Mutant of the Triheme Cytochrome Ppca From Geobacter Sulfurreducens Sheds Light on the Role of the Conserved Aromatic Residue F15

The binding sites of Iron atom in the Solution Structure of A Mutant of the Triheme Cytochrome Ppca From Geobacter Sulfurreducens Sheds Light on the Role of the Conserved Aromatic Residue F15 (pdb code 2lzz). 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 of A Mutant of the Triheme Cytochrome Ppca From Geobacter Sulfurreducens Sheds Light on the Role of the Conserved Aromatic Residue F15, PDB code: 2lzz:
Jump to Iron binding site number: 1; 2; 3;

Iron binding site 1 out of 3 in the Solution Structure of A Mutant of the Triheme Cytochrome Ppca From Geobacter Sulfurreducens Sheds Light on the Role of the Conserved Aromatic Residue F15


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Solution Structure of A Mutant of the Triheme Cytochrome Ppca From Geobacter Sulfurreducens Sheds Light on the Role of the Conserved Aromatic Residue F15 within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe101 b:1.0 occ:1.00 FE A:HEM101 0.0 1.0 1.0 NC A:HEM101 1.9 1.0 1.0 NE2 A:HIS31 1.9 1.0 1.0 NE2 A:HIS17 2.0 1.0 1.0 NB A:HEM101 2.0 1.0 1.0 ND A:HEM101 2.1 1.0 1.0 NA A:HEM101 2.2 1.0 1.0 CD2 A:HIS31 2.9 1.0 1.0 CE1 A:HIS31 2.9 1.0 1.0 C1C A:HEM101 2.9 1.0 1.0 C4C A:HEM101 2.9 1.0 1.0 CD2 A:HIS17 3.0 1.0 1.0 C4B A:HEM101 3.0 1.0 1.0 CE1 A:HIS17 3.0 1.0 1.0 C1D A:HEM101 3.0 1.0 1.0 C1B A:HEM101 3.1 1.0 1.0 HD2 A:HIS31 3.1 1.0 1.0 C4D A:HEM101 3.1 1.0 1.0 HE1 A:HIS31 3.2 1.0 1.0 C4A A:HEM101 3.2 1.0 1.0 HD2 A:HIS17 3.2 1.0 1.0 C1A A:HEM101 3.2 1.0 1.0 HE1 A:HIS17 3.2 1.0 1.0 CHC A:HEM101 3.3 1.0 1.0 CHD A:HEM101 3.4 1.0 1.0 CHB A:HEM101 3.5 1.0 1.0 CHA A:HEM101 3.6 1.0 1.0 ND1 A:HIS31 4.0 1.0 1.0 CG A:HIS31 4.0 1.0 1.0 ND1 A:HIS17 4.1 1.0 1.0 CG A:HIS17 4.1 1.0 1.0 C2C A:HEM101 4.1 1.0 1.0 C3C A:HEM101 4.2 1.0 1.0 C3B A:HEM101 4.2 1.0 1.0 C2B A:HEM101 4.3 1.0 1.0 C2D A:HEM101 4.3 1.0 1.0 C3D A:HEM101 4.3 1.0 1.0 C3A A:HEM101 4.4 1.0 1.0 C2A A:HEM101 4.4 1.0 1.0 HG2 A:GLN21 4.5 1.0 1.0 HB3 A:CYS30 4.5 1.0 1.0 HE21 A:GLN21 4.6 1.0 1.0 HG3 A:GLN21 4.6 1.0 1.0 H A:GLY36 4.6 1.0 1.0 HB3 A:CYS27 4.8 1.0 1.0 HA A:PRO35 4.9 1.0 1.0 NE2 A:GLN21 4.9 1.0 1.0 HD1 A:HIS31 4.9 1.0 1.0 CG A:GLN21 5.0 1.0 1.0

Iron binding site 2 out of 3 in the Solution Structure of A Mutant of the Triheme Cytochrome Ppca From Geobacter Sulfurreducens Sheds Light on the Role of the Conserved Aromatic Residue F15


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Solution Structure of A Mutant of the Triheme Cytochrome Ppca From Geobacter Sulfurreducens Sheds Light on the Role of the Conserved Aromatic Residue F15 within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe102 b:1.0 occ:1.00 FE A:HEM102 0.0 1.0 1.0 NE2 A:HIS55 1.9 1.0 1.0 ND A:HEM102 1.9 1.0 1.0 NC A:HEM102 2.0 1.0 1.0 NE2 A:HIS20 2.0 1.0 1.0 NA A:HEM102 2.1 1.0 1.0 NB A:HEM102 2.1 1.0 1.0 CD2 A:HIS55 2.8 1.0 1.0 CE1 A:HIS55 2.9 1.0 1.0 CD2 A:HIS20 3.0 1.0 1.0 C1D A:HEM102 3.0 1.0 1.0 C4C A:HEM102 3.0 1.0 1.0 CE1 A:HIS20 3.0 1.0 1.0 C4D A:HEM102 3.0 1.0 1.0 C1C A:HEM102 3.0 1.0 1.0 C1A A:HEM102 3.1 1.0 1.0 HD2 A:HIS55 3.1 1.0 1.0 C4B A:HEM102 3.1 1.0 1.0 C4A A:HEM102 3.2 1.0 1.0 HE1 A:HIS55 3.2 1.0 1.0 C1B A:HEM102 3.2 1.0 1.0 HD2 A:HIS20 3.2 1.0 1.0 HE1 A:HIS20 3.2 1.0 1.0 CHD A:HEM102 3.4 1.0 1.0 HD2 A:PRO62 3.4 1.0 1.0 CHA A:HEM102 3.4 1.0 1.0 CHC A:HEM102 3.5 1.0 1.0 CHB A:HEM102 3.6 1.0 1.0 HA3 A:GLY61 3.6 1.0 1.0 ND1 A:HIS55 4.0 1.0 1.0 CG A:HIS55 4.0 1.0 1.0 ND1 A:HIS20 4.1 1.0 1.0 CG A:HIS20 4.1 1.0 1.0 C2D A:HEM102 4.2 1.0 1.0 C3D A:HEM102 4.2 1.0 1.0 C3C A:HEM102 4.2 1.0 1.0 C2C A:HEM102 4.3 1.0 1.0 C2A A:HEM102 4.3 1.0 1.0 C3B A:HEM102 4.4 1.0 1.0 C3A A:HEM102 4.4 1.0 1.0 C2B A:HEM102 4.4 1.0 1.0 CD A:PRO62 4.4 1.0 1.0 HD13 A:LEU15 4.5 1.0 1.0 HD12 A:LEU15 4.5 1.0 1.0 HA2 A:GLY61 4.6 1.0 1.0 CA A:GLY61 4.6 1.0 1.0 HD3 A:PRO62 4.6 1.0 1.0 O A:CYS51 4.7 1.0 1.0 HG2 A:PRO62 4.8 1.0 1.0 HB3 A:CYS51 4.8 1.0 1.0 HD1 A:HIS55 4.9 1.0 1.0 CD1 A:LEU15 4.9 1.0 1.0 HA A:CYS51 4.9 1.0 1.0

Iron binding site 3 out of 3 in the Solution Structure of A Mutant of the Triheme Cytochrome Ppca From Geobacter Sulfurreducens Sheds Light on the Role of the Conserved Aromatic Residue F15


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Solution Structure of A Mutant of the Triheme Cytochrome Ppca From Geobacter Sulfurreducens Sheds Light on the Role of the Conserved Aromatic Residue F15 within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe103 b:1.0 occ:1.00 FE A:HEM103 0.0 1.0 1.0 NE2 A:HIS69 1.8 1.0 1.0 NE2 A:HIS47 2.0 1.0 1.0 NC A:HEM103 2.0 1.0 1.0 NB A:HEM103 2.0 1.0 1.0 ND A:HEM103 2.1 1.0 1.0 NA A:HEM103 2.1 1.0 1.0 CD2 A:HIS69 2.8 1.0 1.0 CE1 A:HIS69 2.8 1.0 1.0 CD2 A:HIS47 3.0 1.0 1.0 CE1 A:HIS47 3.0 1.0 1.0 C1C A:HEM103 3.0 1.0 1.0 C4B A:HEM103 3.0 1.0 1.0 C4C A:HEM103 3.0 1.0 1.0 C1B A:HEM103 3.0 1.0 1.0 C1D A:HEM103 3.1 1.0 1.0 C4A A:HEM103 3.1 1.0 1.0 HD2 A:HIS69 3.1 1.0 1.0 HE1 A:HIS69 3.1 1.0 1.0 C4D A:HEM103 3.1 1.0 1.0 C1A A:HEM103 3.1 1.0 1.0 HD2 A:HIS47 3.2 1.0 1.0 HE1 A:HIS47 3.2 1.0 1.0 CHC A:HEM103 3.4 1.0 1.0 CHD A:HEM103 3.4 1.0 1.0 CHB A:HEM103 3.5 1.0 1.0 CHA A:HEM103 3.5 1.0 1.0 ND1 A:HIS69 4.0 1.0 1.0 CG A:HIS69 4.0 1.0 1.0 ND1 A:HIS47 4.1 1.0 1.0 CG A:HIS47 4.1 1.0 1.0 C2C A:HEM103 4.2 1.0 1.0 C3C A:HEM103 4.2 1.0 1.0 C3B A:HEM103 4.3 1.0 1.0 C2B A:HEM103 4.3 1.0 1.0 C2D A:HEM103 4.3 1.0 1.0 C3A A:HEM103 4.3 1.0 1.0 C3D A:HEM103 4.3 1.0 1.0 C2A A:HEM103 4.4 1.0 1.0 HG2 A:LYS43 4.6 1.0 1.0 HG23 A:VAL13 4.8 1.0 1.0 HD1 A:HIS69 4.9 1.0 1.0 HB3 A:CYS68 4.9 1.0 1.0

J.M.Dantas, L.Morgado, P.R.Pokkuluri, D.L.Turner, C.A.Salgueiro. Solution Structure of A Mutant of the Triheme Cytochrome Ppca From Geobacter Sulfurreducens Sheds Light on the Role of the Conserved Aromatic Residue F15. Biochim.Biophys.Acta V.1827 484 2013.
ISSN: ISSN 0006-3002
PubMed: 23313804
DOI: 10.1016/J.BBABIO.2012.12.008