Iron in PDB 7txe: Plasmodium Falciparum Cyt C2 Dsd

The structure of Plasmodium Falciparum Cyt C2 Dsd, PDB code: 7txe was solved by C.P.Hill, H.J.Wienkers, F.G.Whitby, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	31.80 / 2.30
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	54.44, 71.994, 78.409, 90, 90, 90
R / Rfree (%)	23.1 / 28

The binding sites of Iron atom in the Plasmodium Falciparum Cyt C2 Dsd (pdb code 7txe). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Plasmodium Falciparum Cyt C2 Dsd, PDB code: 7txe:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Plasmodium Falciparum Cyt C2 Dsd


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Plasmodium Falciparum Cyt C2 Dsd within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe201 b:24.3 occ:1.00 FE A:HEC201 0.0 24.3 1.0 NE2 A:HIS42 1.9 25.3 1.0 NC A:HEC201 2.0 29.7 1.0 NB A:HEC201 2.0 28.7 1.0 O A:HOH311 2.0 25.3 1.0 ND A:HEC201 2.1 31.6 1.0 NA A:HEC201 2.1 26.3 1.0 CD2 A:HIS42 2.8 25.8 1.0 CE1 A:HIS42 2.9 30.0 1.0 C1C A:HEC201 3.0 33.6 1.0 C4C A:HEC201 3.0 26.8 1.0 HD2 A:HIS42 3.0 30.9 1.0 C1D A:HEC201 3.0 27.5 1.0 C4B A:HEC201 3.0 29.8 1.0 C1B A:HEC201 3.1 27.9 1.0 C4D A:HEC201 3.1 28.6 1.0 HE1 A:HIS42 3.1 36.0 1.0 C4A A:HEC201 3.1 29.4 1.0 C1A A:HEC201 3.1 30.2 1.0 CHC A:HEC201 3.4 31.6 1.0 CHD A:HEC201 3.4 28.6 1.0 CHB A:HEC201 3.5 24.5 1.0 CHA A:HEC201 3.5 28.1 1.0 ND1 A:HIS42 4.0 27.5 1.0 CG A:HIS42 4.0 26.9 1.0 HE1 A:TYR100 4.1 40.9 1.0 C2C A:HEC201 4.2 32.8 1.0 C3C A:HEC201 4.2 31.5 1.0 C2D A:HEC201 4.2 33.7 1.0 C3D A:HEC201 4.3 26.9 1.0 C3B A:HEC201 4.3 31.1 1.0 C2B A:HEC201 4.3 31.9 1.0 C3A A:HEC201 4.3 24.2 1.0 C2A A:HEC201 4.3 25.8 1.0 OH A:TYR100 4.3 31.4 1.0 HHC A:HEC201 4.4 37.9 1.0 HHD A:HEC201 4.4 34.3 1.0 HHB A:HEC201 4.4 29.4 1.0 HHA A:HEC201 4.4 33.7 1.0 HD12 A:LEU62 4.4 35.1 1.0 HD22 A:LEU62 4.6 38.1 1.0 HB2 A:CYS41 4.7 39.6 1.0 HD1 A:HIS42 4.7 33.0 0.0 HA3 A:GLY59 4.9 39.9 1.0 CE1 A:TYR100 4.9 34.0 1.0 HD2 A:PRO60 4.9 48.2 1.0 HH A:TYR100 4.9 37.7 0.0 HD2 B:PHE116 4.9 48.4 1.0 O A:HOH321 4.9 46.6 1.0

Iron binding site 2 out of 2 in the Plasmodium Falciparum Cyt C2 Dsd


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Plasmodium Falciparum Cyt C2 Dsd within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe201 b:26.5 occ:1.00 FE B:HEC201 0.0 26.5 1.0 NE2 B:HIS42 1.9 25.0 1.0 O B:HOH309 2.0 24.8 1.0 NC B:HEC201 2.0 29.0 1.0 NA B:HEC201 2.1 25.1 1.0 NB B:HEC201 2.1 28.9 1.0 ND B:HEC201 2.1 24.4 1.0 CD2 B:HIS42 2.8 25.2 1.0 HD2 B:HIS42 3.0 30.2 1.0 CE1 B:HIS42 3.0 30.2 1.0 C4C B:HEC201 3.0 29.1 1.0 C1C B:HEC201 3.0 30.5 1.0 C1D B:HEC201 3.1 30.4 1.0 C4A B:HEC201 3.1 31.3 1.0 C4B B:HEC201 3.1 33.6 1.0 C4D B:HEC201 3.1 28.4 1.0 C1B B:HEC201 3.1 26.5 1.0 C1A B:HEC201 3.1 27.0 1.0 HE1 B:HIS42 3.2 36.2 1.0 CHD B:HEC201 3.4 27.1 1.0 CHC B:HEC201 3.4 31.4 1.0 CHB B:HEC201 3.4 27.1 1.0 CHA B:HEC201 3.4 25.1 1.0 HH B:TYR100 3.6 36.5 0.0 CG B:HIS42 4.0 25.7 1.0 HE2 B:TYR100 4.0 39.2 1.0 ND1 B:HIS42 4.0 25.4 1.0 C3C B:HEC201 4.3 27.9 1.0 C2C B:HEC201 4.3 32.8 1.0 C2D B:HEC201 4.3 32.9 1.0 C3D B:HEC201 4.3 30.4 1.0 C3A B:HEC201 4.3 27.9 1.0 C2B B:HEC201 4.3 33.5 1.0 C2A B:HEC201 4.3 27.0 1.0 C3B B:HEC201 4.3 34.2 1.0 HHD B:HEC201 4.4 32.5 1.0 HHC B:HEC201 4.4 37.7 1.0 HHB B:HEC201 4.4 32.5 1.0 HHA B:HEC201 4.4 30.1 1.0 OH B:TYR100 4.4 30.4 1.0 HD12 B:LEU62 4.5 33.0 1.0 HD22 B:LEU62 4.7 44.5 1.0 HB2 B:CYS41 4.7 33.1 1.0 HD1 B:HIS42 4.8 30.5 0.0 CE2 B:TYR100 4.9 32.7 1.0 HA3 B:GLY59 4.9 37.5 1.0 HD2 A:PHE116 4.9 45.6 1.0 HD2 B:PRO60 5.0 45.8 1.0

T.J.Espino-Sanchez, H.Wienkers, R.G.Marvin, S.A.Nalder, A.E.Garcia-Guerrero, P.E.Vannatta, Y.Jami-Alahmadi, A.Mixon Blackwell, F.G.Whitby, J.A.Wohlschlegel, M.T.Kieber-Emmons, C.P.Hill, P.A.Sigala. Direct Tests of Cytochrome C and C1 Functions in the Electron Transport Chain of Malaria Parasites Proc Natl Acad Sci U S A V. 120 47120 2023.
ISSN: ESSN 1091-6490
PubMed: 37126705
DOI: 10.1073/PNAS.2301047120