Iron in PDB 9hqt: Sfx Structure of Cytochrome C Prime Beta From Methylococcus Capsulatus (Bath)

The structure of Sfx Structure of Cytochrome C Prime Beta From Methylococcus Capsulatus (Bath), PDB code: 9hqt 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)	33.89 / 1.80
Space group	P 21 3
Cell size a, b, c (Å), α, β, γ (°)	107.1, 107.1, 107.1, 90, 90, 90
R / Rfree (%)	19 / 21.9

The structure of Sfx Structure of Cytochrome C Prime Beta From Methylococcus Capsulatus (Bath) also contains other interesting chemical elements:

Zinc

(Zn)

2 atoms

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

Iron binding site 1 out of 2 in the Sfx Structure of Cytochrome C Prime Beta From Methylococcus Capsulatus (Bath)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Sfx Structure of Cytochrome C Prime Beta From Methylococcus Capsulatus (Bath) within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe201 b:22.4 occ:1.00 FE B:HEC201 0.0 22.4 1.0 NA B:HEC201 2.0 19.2 1.0 NE2 B:HIS123 2.0 23.7 1.0 NC B:HEC201 2.1 24.2 1.0 ND B:HEC201 2.1 20.9 1.0 NB B:HEC201 2.1 22.3 1.0 CE1 B:HIS123 3.0 22.6 1.0 C1A B:HEC201 3.0 19.5 1.0 C1C B:HEC201 3.0 23.4 1.0 C4A B:HEC201 3.0 20.9 1.0 C4B B:HEC201 3.0 22.6 1.0 C4D B:HEC201 3.1 20.5 1.0 C4C B:HEC201 3.1 24.6 1.0 C1B B:HEC201 3.1 20.6 1.0 C1D B:HEC201 3.1 22.5 1.0 CD2 B:HIS123 3.1 23.1 1.0 HE1 B:HIS123 3.2 21.9 1.0 HD2 B:HIS123 3.3 24.1 1.0 CHC B:HEC201 3.4 22.9 1.0 CHA B:HEC201 3.4 18.7 1.0 CHB B:HEC201 3.4 20.7 1.0 CHD B:HEC201 3.5 22.8 1.0 ND1 B:HIS123 4.2 22.4 1.0 CG B:HIS123 4.2 23.7 1.0 HE2 B:PHE32 4.2 47.3 1.0 C2A B:HEC201 4.3 18.9 1.0 C3A B:HEC201 4.3 18.6 1.0 HHC B:HEC201 4.3 24.1 1.0 C3B B:HEC201 4.3 23.2 1.0 C3D B:HEC201 4.3 21.2 1.0 C3C B:HEC201 4.3 26.4 1.0 C2C B:HEC201 4.4 25.6 1.0 HHA B:HEC201 4.4 18.9 1.0 C2D B:HEC201 4.4 21.8 1.0 HD2 B:PHE133 4.4 23.7 1.0 HE2 B:PHE133 4.4 26.5 1.0 HHB B:HEC201 4.4 20.6 1.0 C2B B:HEC201 4.4 21.9 1.0 HHD B:HEC201 4.4 24.1 1.0 HZ B:PHE32 4.6 45.8 1.0 CE2 B:PHE32 4.6 47.9 1.0 CZ B:PHE32 4.8 47.1 1.0 HE2 B:TYR99 4.9 25.2 1.0 CD2 B:PHE133 4.9 24.1 1.0 HD1 B:HIS123 4.9 30.0 1.0 CE2 B:PHE133 5.0 26.7 1.0

Iron binding site 2 out of 2 in the Sfx Structure of Cytochrome C Prime Beta From Methylococcus Capsulatus (Bath)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Sfx Structure of Cytochrome C Prime Beta From Methylococcus Capsulatus (Bath) within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe203 b:21.4 occ:1.00 FE A:HEC203 0.0 21.4 1.0 NC A:HEC203 2.0 22.2 1.0 NA A:HEC203 2.0 19.5 1.0 NE2 A:HIS123 2.0 20.6 1.0 NB A:HEC203 2.0 18.7 1.0 ND A:HEC203 2.1 21.2 1.0 CE1 A:HIS123 3.0 21.3 1.0 C4B A:HEC203 3.0 20.6 1.0 C1B A:HEC203 3.0 19.7 1.0 C1A A:HEC203 3.0 18.2 1.0 C4C A:HEC203 3.0 24.6 1.0 C4A A:HEC203 3.0 17.9 1.0 C1C A:HEC203 3.1 23.1 1.0 C4D A:HEC203 3.1 19.7 1.0 C1D A:HEC203 3.1 21.9 1.0 CD2 A:HIS123 3.1 21.8 1.0 HE1 A:HIS123 3.1 20.4 1.0 HD2 A:HIS123 3.3 22.5 1.0 CHC A:HEC203 3.4 22.3 1.0 CHB A:HEC203 3.4 18.2 1.0 CHA A:HEC203 3.4 17.3 1.0 CHD A:HEC203 3.4 22.7 1.0 ND1 A:HIS123 4.1 22.0 1.0 CG A:HIS123 4.2 23.3 1.0 C3C A:HEC203 4.3 25.9 1.0 C2A A:HEC203 4.3 16.8 1.0 C3A A:HEC203 4.3 18.1 1.0 HE1 A:PHE133 4.3 26.9 1.0 C3B A:HEC203 4.3 20.9 1.0 C2B A:HEC203 4.3 20.0 1.0 HHC A:HEC203 4.3 23.0 1.0 HHB A:HEC203 4.4 18.3 1.0 HHA A:HEC203 4.4 17.8 1.0 C3D A:HEC203 4.4 19.8 1.0 C2C A:HEC203 4.4 25.8 1.0 HHD A:HEC203 4.4 24.0 1.0 C2D A:HEC203 4.4 21.2 1.0 HD1 A:PHE133 4.5 24.8 1.0 HZ A:PHE32 4.6 45.4 1.0 CZ A:PHE32 4.8 45.1 1.0 HE2 A:PHE32 4.8 47.0 1.0 HE2 A:TYR99 4.9 25.2 1.0 CE1 A:PHE133 4.9 26.7 1.0 HD1 A:HIS123 4.9 30.0 1.0 CD1 A:PHE133 5.0 25.6 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