Iron in PDB 8q1v: TTX183A - A C-Type Cytochrome Domain From the Teredinibacter Turnerae Protein TERTU_2913

The structure of TTX183A - A C-Type Cytochrome Domain From the Teredinibacter Turnerae Protein TERTU_2913, PDB code: 8q1v was solved by B.S.Rajagopal, G.R.Hemsworth, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	65.53 / 1.40
Space group	P 41 3 2
Cell size a, b, c (Å), α, β, γ (°)	92.669, 92.669, 92.669, 90, 90, 90
R / Rfree (%)	16.5 / 19.3

The structure of TTX183A - A C-Type Cytochrome Domain From the Teredinibacter Turnerae Protein TERTU_2913 also contains other interesting chemical elements:

Chlorine

(Cl)

3 atoms

The binding sites of Iron atom in the TTX183A - A C-Type Cytochrome Domain From the Teredinibacter Turnerae Protein TERTU_2913 (pdb code 8q1v). 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 TTX183A - A C-Type Cytochrome Domain From the Teredinibacter Turnerae Protein TERTU_2913, PDB code: 8q1v:

Iron binding site 1 out of 1 in the TTX183A - A C-Type Cytochrome Domain From the Teredinibacter Turnerae Protein TERTU_2913


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of TTX183A - A C-Type Cytochrome Domain From the Teredinibacter Turnerae Protein TERTU_2913 within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe101 b:12.7 occ:1.00 FE A:HEC101 0.0 12.7 1.0 HE2 A:HIS22 1.2 13.4 0.0 ND A:HEC101 2.0 12.5 1.0 NA A:HEC101 2.0 11.6 1.0 NB A:HEC101 2.0 11.6 1.0 NE2 A:HIS22 2.0 13.9 1.0 NC A:HEC101 2.0 12.6 1.0 SD A:MET55 2.3 12.0 1.0 C1D A:HEC101 3.0 13.2 1.0 CE1 A:HIS22 3.0 15.9 1.0 C4D A:HEC101 3.0 13.4 1.0 C4C A:HEC101 3.0 12.8 1.0 C4B A:HEC101 3.0 12.3 1.0 C1A A:HEC101 3.0 12.6 1.0 C1B A:HEC101 3.0 11.5 1.0 C4A A:HEC101 3.0 11.5 1.0 C1C A:HEC101 3.0 12.8 1.0 CD2 A:HIS22 3.1 15.3 1.0 HE1 A:HIS22 3.2 15.5 1.0 HG3 A:MET55 3.2 11.7 1.0 HD2 A:HIS22 3.3 15.0 1.0 CHD A:HEC101 3.4 12.8 1.0 CHB A:HEC101 3.4 11.4 1.0 CG A:MET55 3.4 11.7 1.0 CHA A:HEC101 3.4 13.4 1.0 CE A:MET55 3.4 12.6 1.0 CHC A:HEC101 3.4 12.6 1.0 HE2 A:MET55 3.5 12.5 1.0 HE3 A:MET55 3.5 12.4 1.0 HB3 A:MET55 4.0 11.7 1.0 HG2 A:MET55 4.1 11.7 1.0 ND1 A:HIS22 4.1 15.6 1.0 CG A:HIS22 4.2 15.5 1.0 C3C A:HEC101 4.2 12.7 1.0 C2D A:HEC101 4.3 14.4 1.0 HE1 A:MET55 4.3 12.5 1.0 C3B A:HEC101 4.3 12.1 1.0 C2B A:HEC101 4.3 12.1 1.0 C3A A:HEC101 4.3 12.7 1.0 C3D A:HEC101 4.3 14.6 1.0 CB A:MET55 4.3 11.7 1.0 C2C A:HEC101 4.3 13.5 1.0 C2A A:HEC101 4.3 13.0 1.0 HHD A:HEC101 4.3 12.8 1.0 HHB A:HEC101 4.4 11.5 1.0 HHC A:HEC101 4.4 12.6 1.0 HHA A:HEC101 4.4 13.3 1.0 HB2 A:LEU57 4.5 14.6 1.0 HD23 A:LEU35 4.5 21.2 1.0 H A:LEU57 4.6 13.4 1.0 HA A:PRO56 4.7 13.6 1.0 HB2 A:MET55 4.9 11.7 1.0 HD1 A:HIS22 4.9 15.5 0.0

B.S.Rajagopal, N.Yates, J.Smith, A.Paradisi, C.Tetard-Jones, W.G.T.Willats, S.Marcus, P.J.Knox, M.Firdaus-Raih, B.Henrissat, G.J.Davies, P.H.Walton, A.Parkin, G.R.Hemsworth. Structural Dissection of Two Redox Proteins From the Shipworm Symbiont Teredinibacter Turnerae Iucrj 2024.
ISSN: ESSN 2052-2525
DOI: 10.1107/S2052252524001386