Iron in PDB 28wn: Structure of Apo-Cdcpfc with 2FE2S Cluster

All present enzymatic activity of Structure of Apo-Cdcpfc with 2FE2S Cluster:
4.99.1.9;

The structure of Structure of Apo-Cdcpfc with 2FE2S Cluster, PDB code: 28wn was solved by T.Gabler, A.Cassiani, S.Hofbauer, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	46.98 / 1.87
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	66.233, 133.286, 45.17, 90, 90, 90
R / Rfree (%)	17.3 / 20.2

The structure of Structure of Apo-Cdcpfc with 2FE2S Cluster also contains other interesting chemical elements:

Potassium

(K)

1 atom

The binding sites of Iron atom in the Structure of Apo-Cdcpfc with 2FE2S Cluster (pdb code 28wn). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Structure of Apo-Cdcpfc with 2FE2S Cluster, PDB code: 28wn:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Structure of Apo-Cdcpfc with 2FE2S Cluster


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Structure of Apo-Cdcpfc with 2FE2S Cluster within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe401 b:22.3 occ:1.00 FE1 A:FES401 0.0 22.3 1.0 S1 A:FES401 2.2 22.3 1.0 S2 A:FES401 2.2 23.6 1.0 SG A:CYS358 2.3 22.6 1.0 SG A:CYS357 2.3 22.3 1.0 FE2 A:FES401 2.7 20.4 1.0 HB2 A:CYS358 3.1 24.6 1.0 HB3 A:CYS357 3.2 27.3 1.0 CB A:CYS358 3.3 20.5 1.0 CB A:CYS357 3.4 22.7 1.0 HA2 A:GLY208 3.6 32.3 1.0 H A:GLY208 3.7 23.0 1.0 C A:CYS357 3.7 22.7 1.0 HB2 A:CYS353 3.7 28.6 1.0 H A:GLY123 3.8 26.5 1.0 N A:CYS358 3.8 22.9 1.0 HD2 A:LYS344 3.9 30.0 1.0 O A:CYS357 3.9 25.3 1.0 HB3 A:CYS358 4.1 24.6 1.0 H A:CYS358 4.1 27.5 1.0 CA A:CYS357 4.1 23.9 1.0 CA A:CYS358 4.2 25.1 1.0 HB2 A:CYS357 4.2 27.3 1.0 H A:CYS353 4.3 32.1 1.0 HB3 A:CYS127 4.3 25.0 1.0 N A:GLY208 4.3 19.1 1.0 HA A:CYS357 4.3 28.7 1.0 CA A:GLY208 4.4 26.8 1.0 HZ2 A:LYS344 4.4 40.5 1.0 HB2 A:ARG128 4.4 28.6 1.0 SG A:CYS353 4.5 20.6 1.0 CB A:CYS353 4.5 23.8 1.0 N A:GLY123 4.6 22.0 1.0 HA A:CYS358 4.6 30.2 1.0 HD23 A:LEU215 4.6 28.9 1.0 SG A:CYS127 4.7 22.1 1.0 HE22 A:GLN156 4.8 25.2 1.0 HA2 A:GLY123 4.8 24.2 1.0 CD A:LYS344 4.8 25.0 1.0 HD2 A:ARG128 4.8 38.2 1.0 H A:GLU354 4.9 28.9 1.0 HD3 A:LYS344 5.0 30.0 1.0 CB A:CYS127 5.0 20.8 1.0 C A:GLY208 5.0 24.6 1.0

Iron binding site 2 out of 2 in the Structure of Apo-Cdcpfc with 2FE2S Cluster


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Structure of Apo-Cdcpfc with 2FE2S Cluster within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe401 b:20.4 occ:1.00 FE2 A:FES401 0.0 20.4 1.0 S2 A:FES401 2.2 23.6 1.0 S1 A:FES401 2.2 22.3 1.0 SG A:CYS353 2.3 20.6 1.0 SG A:CYS127 2.3 22.1 1.0 FE1 A:FES401 2.7 22.3 1.0 HB2 A:CYS353 3.1 28.6 1.0 HB3 A:CYS127 3.2 25.0 1.0 H A:CYS353 3.3 32.1 1.0 CB A:CYS353 3.3 23.8 1.0 CB A:CYS127 3.4 20.8 1.0 HE22 A:GLN156 3.5 25.2 1.0 HB2 A:CYS127 3.7 25.0 1.0 H A:GLY345 3.7 25.9 1.0 HE21 A:GLN156 3.8 25.2 1.0 HA2 A:GLY345 3.8 22.2 1.0 NE2 A:GLN156 4.0 20.9 1.0 HB2 A:LYS344 4.0 26.2 1.0 O A:HOH525 4.0 21.1 1.0 HB3 A:CYS353 4.0 28.6 1.0 N A:CYS353 4.1 26.7 1.0 HD2 A:LYS344 4.2 30.0 1.0 CA A:CYS353 4.3 26.2 1.0 HZ1 A:LYS153 4.3 28.7 1.0 HB3 A:LYS344 4.3 26.2 1.0 SG A:CYS357 4.4 22.3 1.0 N A:GLY345 4.4 21.6 1.0 SG A:CYS358 4.4 22.6 1.0 HA2 A:GLY122 4.4 25.6 1.0 HB2 A:ARG128 4.5 28.6 1.0 H A:ARG128 4.5 27.6 1.0 CA A:GLY345 4.6 18.4 1.0 H A:GLY123 4.6 26.5 1.0 N A:ARG128 4.6 22.9 1.0 CB A:LYS344 4.6 21.8 1.0 CA A:CYS127 4.7 18.5 1.0 HB3 A:CYS357 4.7 27.3 1.0 HA A:CYS353 4.8 31.6 1.0 HA A:ARG128 4.8 26.4 1.0 C A:CYS127 4.8 18.2 1.0 OD2 A:ASP131 4.8 24.0 1.0 HB2 A:CYS358 4.9 24.6 1.0 HA A:PRO352 4.9 34.5 1.0 O A:HOH690 5.0 35.0 1.0

A.Cassiani, T.Gabler, A.Dali, P.G.Furtmuller, F.Sebastiani, M.Becucci, G.Smulevich, S.Hofbauer. The [2FE2S] Cluster and Active-Site Architecture of Corynebacterium Diphtheriae Coproporphyrin Ferrochelatase: Structure, Stability, and Catalysis. Int.J.Biol.Macromol. 52684 2026.
ISSN: ISSN 0141-8130
PubMed: 42184855
DOI: 10.1016/J.IJBIOMAC.2026.152684