Iron in PDB 9hs8: Cytochrome C Prime Beta From Methylococcus Capsulatus (Bath) in Complex with Nitric Oxide From Proli Nonoate

The structure of Cytochrome C Prime Beta From Methylococcus Capsulatus (Bath) in Complex with Nitric Oxide From Proli Nonoate, PDB code: 9hs8 was solved by P.Smyth, L.J.Williams, M.A.Hough, J.A.R.Worrall, R.L.Owen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	76.09 / 1.85
Space group	P 21 3
Cell size a, b, c (Å), α, β, γ (°)	107.441, 107.441, 107.441, 90, 90, 90
R / Rfree (%)	15.5 / 18

The structure of Cytochrome C Prime Beta From Methylococcus Capsulatus (Bath) in Complex with Nitric Oxide From Proli Nonoate also contains other interesting chemical elements:

Zinc

(Zn)

2 atoms

The binding sites of Iron atom in the Cytochrome C Prime Beta From Methylococcus Capsulatus (Bath) in Complex with Nitric Oxide From Proli Nonoate (pdb code 9hs8). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Cytochrome C Prime Beta From Methylococcus Capsulatus (Bath) in Complex with Nitric Oxide From Proli Nonoate, PDB code: 9hs8:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Cytochrome C Prime Beta From Methylococcus Capsulatus (Bath) in Complex with Nitric Oxide From Proli Nonoate


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Cytochrome C Prime Beta From Methylococcus Capsulatus (Bath) in Complex with Nitric Oxide From Proli Nonoate within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe201 b:25.9 occ:1.00 FE B:HEC201 0.0 25.9 1.0 N B:NO204 1.9 27.2 1.0 NE2 B:HIS123 2.0 26.8 1.0 NC B:HEC201 2.0 28.7 1.0 NA B:HEC201 2.1 24.3 1.0 ND B:HEC201 2.1 27.3 1.0 NB B:HEC201 2.1 26.3 1.0 CE1 B:HIS123 2.9 30.9 1.0 O B:NO204 3.0 34.7 1.0 C1C B:HEC201 3.0 27.8 1.0 C4D B:HEC201 3.0 25.6 1.0 C1A B:HEC201 3.0 22.8 1.0 C4B B:HEC201 3.1 25.6 1.0 C4C B:HEC201 3.1 30.7 1.0 C1D B:HEC201 3.1 26.7 1.0 CD2 B:HIS123 3.1 28.1 1.0 C4A B:HEC201 3.1 23.2 1.0 C1B B:HEC201 3.1 24.3 1.0 CHC B:HEC201 3.4 23.2 1.0 CHA B:HEC201 3.4 22.6 1.0 CHD B:HEC201 3.5 26.5 1.0 CHB B:HEC201 3.5 23.1 1.0 ND1 B:HIS123 4.1 29.1 1.0 CG B:HIS123 4.2 31.3 1.0 C3C B:HEC201 4.3 29.6 1.0 C2A B:HEC201 4.3 21.0 1.0 C3D B:HEC201 4.3 25.3 1.0 C2C B:HEC201 4.3 29.5 1.0 C3B B:HEC201 4.4 25.0 1.0 C2D B:HEC201 4.4 24.5 1.0 C3A B:HEC201 4.4 22.4 1.0 C2B B:HEC201 4.5 24.1 1.0 CE2 B:PHE32 4.9 33.4 1.0 CZ B:PHE32 5.0 34.1 1.0

Iron binding site 2 out of 2 in the Cytochrome C Prime Beta From Methylococcus Capsulatus (Bath) in Complex with Nitric Oxide From Proli Nonoate


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Cytochrome C Prime Beta From Methylococcus Capsulatus (Bath) in Complex with Nitric Oxide From Proli Nonoate within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe203 b:25.1 occ:1.00 FE A:HEC203 0.0 25.1 1.0 N A:NO204 1.9 25.3 1.0 NE2 A:HIS123 2.0 25.3 1.0 NA A:HEC203 2.0 24.1 1.0 NC A:HEC203 2.0 26.9 1.0 NB A:HEC203 2.0 25.1 1.0 ND A:HEC203 2.1 27.6 1.0 CE1 A:HIS123 2.9 25.4 1.0 O A:NO204 3.0 40.4 1.0 C4B A:HEC203 3.0 24.6 1.0 C1A A:HEC203 3.0 23.4 1.0 C1C A:HEC203 3.0 28.2 1.0 C4A A:HEC203 3.1 23.2 1.0 C1B A:HEC203 3.1 24.4 1.0 C4D A:HEC203 3.1 25.5 1.0 C4C A:HEC203 3.1 28.6 1.0 C1D A:HEC203 3.1 28.6 1.0 CD2 A:HIS123 3.1 24.7 1.0 CHC A:HEC203 3.4 24.5 1.0 CHA A:HEC203 3.4 19.2 1.0 CHD A:HEC203 3.5 25.1 1.0 CHB A:HEC203 3.5 23.5 1.0 ND1 A:HIS123 4.1 22.9 1.0 CG A:HIS123 4.2 28.0 1.0 C2A A:HEC203 4.3 21.6 1.0 C3A A:HEC203 4.3 21.4 1.0 C3B A:HEC203 4.3 26.1 1.0 C3C A:HEC203 4.4 28.2 1.0 C2C A:HEC203 4.4 29.6 1.0 C2B A:HEC203 4.4 23.4 1.0 C3D A:HEC203 4.4 25.8 1.0 C2D A:HEC203 4.4 27.3 1.0 CZ A:PHE32 4.9 34.0 1.0 CE1 A:PHE133 5.0 32.5 1.0

P.Smyth, S.Jaho, L.J.Williams, G.Karras, A.Fitzpatrick, A.J.Thompson, S.Battah, D.Axford, S.Horrell, M.Lucic, K.Ishihara, M.Kataoka, H.Matsuura, K.Shimba, K.Tono, T.Tosha, H.Sugimoto, S.Owada, M.A.Hough, J.A.R.Worrall, R.L.Owen. Time-Resolved Serial Synchrotron and Serial Femtosecond Crystallography of Heme Proteins Using Photocaged Nitric Oxide. Iucrj 2025.
ISSN: ESSN 2052-2525
PubMed: 40843530
DOI: 10.1107/S2052252525006645