Iron in PDB 8zxq: Crystal Structure of SSR1698 in Complex with Heme B

The structure of Crystal Structure of SSR1698 in Complex with Heme B, PDB code: 8zxq was solved by X.Wang, L.Liu, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	27.28 / 1.51
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	58.898, 92.348, 34.464, 90, 90, 90
R / Rfree (%)	17.5 / 21.1

The binding sites of Iron atom in the Crystal Structure of SSR1698 in Complex with Heme B (pdb code 8zxq). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total only one binding site of Iron was determined in the Crystal Structure of SSR1698 in Complex with Heme B, PDB code: 8zxq:

Iron binding site 1 out of 1 in the Crystal Structure of SSR1698 in Complex with Heme B


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Crystal Structure of SSR1698 in Complex with Heme B within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe200 b:2.7 occ:0.50 FE A:HEM200 0.0 2.7 0.5 NB A:HEM200 1.9 1.2 0.5 NA A:HEM200 2.0 2.2 0.5 ND A:HEM200 2.1 4.1 0.5 NC A:HEM200 2.1 3.2 0.5 NE2 A:HIS79 2.2 5.5 1.0 C4B A:HEM200 3.0 5.1 0.5 C1B A:HEM200 3.0 4.0 0.5 C1A A:HEM200 3.0 2.1 0.5 C1C A:HEM200 3.0 6.8 0.5 CD2 A:HIS79 3.0 7.1 1.0 C4D A:HEM200 3.1 2.3 0.5 C4A A:HEM200 3.1 2.3 0.5 C1D A:HEM200 3.1 3.1 0.5 C4C A:HEM200 3.1 3.8 0.5 CE1 A:HIS79 3.2 8.0 1.0 CHC A:HEM200 3.3 8.4 0.5 CHA A:HEM200 3.4 2.4 0.5 CHB A:HEM200 3.4 3.7 0.5 CHD A:HEM200 3.5 2.4 0.5 C3B A:HEM200 4.2 6.8 0.5 C2B A:HEM200 4.2 5.2 0.5 CG A:HIS79 4.2 6.6 1.0 ND1 A:HIS79 4.2 6.9 1.0 C2A A:HEM200 4.2 2.3 0.5 C3A A:HEM200 4.3 2.0 0.5 C3D A:HEM200 4.3 2.0 0.5 C2C A:HEM200 4.3 8.5 0.5 C2D A:HEM200 4.3 4.3 0.5 C3C A:HEM200 4.3 6.0 0.5 CD1 A:ILE83 4.9 5.2 1.0

X.Y.Wang, J.Zhang, H.Y.Li, C.S.Dong, H.E.Dai, M.Wang, L.Liu. Structural Basis For Monomer-Dimer Transition of DRI1 Upon Heme Binding. Proteins 2024.
ISSN: ESSN 1097-0134
PubMed: 39670557
DOI: 10.1002/PROT.26778