Iron in PDB 6sv3: Structure of Coproheme-Lmcpfc

All present enzymatic activity of Structure of Coproheme-Lmcpfc:
4.99.1.1;

The structure of Structure of Coproheme-Lmcpfc, PDB code: 6sv3 was solved by S.Hofbauer, J.Helm, K.Djinovic-Carugo, P.G.Furtmueller, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	36.50 / 1.64
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	37.470, 68.140, 62.910, 90.00, 103.06, 90.00
R / Rfree (%)	17.1 / 20.1

The binding sites of Iron atom in the Structure of Coproheme-Lmcpfc (pdb code 6sv3). 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 Structure of Coproheme-Lmcpfc, PDB code: 6sv3:

Iron binding site 1 out of 1 in the Structure of Coproheme-Lmcpfc


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Structure of Coproheme-Lmcpfc within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe401 b:26.1 occ:1.00 FE A:FEC401 0.0 26.1 1.0 ND A:FEC401 2.0 19.8 1.0 NC A:FEC401 2.0 24.9 1.0 NA A:FEC401 2.0 20.5 1.0 NB A:FEC401 2.0 24.7 1.0 OH A:TYR12 2.7 36.0 1.0 CZ A:TYR12 3.0 31.9 1.0 C1A A:FEC401 3.0 21.5 1.0 C4D A:FEC401 3.0 20.1 1.0 C1C A:FEC401 3.0 27.6 1.0 C4B A:FEC401 3.0 29.7 1.0 C1D A:FEC401 3.1 18.4 1.0 C4C A:FEC401 3.1 27.3 1.0 C1B A:FEC401 3.1 18.4 1.0 C4A A:FEC401 3.1 28.6 1.0 NE2 A:HIS182 3.2 17.8 1.0 CHC A:FEC401 3.4 31.3 1.0 CHA A:FEC401 3.4 22.7 1.0 CHB A:FEC401 3.4 24.8 1.0 CE1 A:TYR12 3.4 26.3 1.0 CHD A:FEC401 3.4 27.2 1.0 CD2 A:HIS182 3.7 18.4 1.0 CE2 A:TYR12 3.7 23.2 1.0 OE1 A:GLU263 3.7 25.4 0.4 OE1 A:GLU263 3.9 22.5 0.6 CE1 A:HIS182 4.1 18.0 1.0 C2A A:FEC401 4.3 22.9 1.0 C3D A:FEC401 4.3 19.3 1.0 C2C A:FEC401 4.3 33.5 1.0 C2D A:FEC401 4.3 21.9 1.0 C3A A:FEC401 4.3 27.6 1.0 C3C A:FEC401 4.3 30.4 1.0 C3B A:FEC401 4.3 26.5 1.0 C2B A:FEC401 4.3 21.7 1.0 O A:HOH554 4.3 27.5 1.0 CD1 A:TYR12 4.4 26.2 1.0 O A:HOH548 4.6 36.0 1.0 CD2 A:TYR12 4.6 23.6 1.0 CD A:GLU263 4.7 25.3 0.6 CG A:HIS182 4.7 18.3 1.0 CD A:GLU263 4.8 23.5 0.4 CG A:TYR12 4.9 23.8 1.0 ND1 A:HIS182 4.9 19.1 1.0

S.Hofbauer, J.Helm, C.Obinger, K.Djinovic-Carugo, P.G.Furtmuller. Crystal Structures and Calorimetry Reveal Catalytically Relevant Binding Mode of Coproporphyrin and Coproheme in Coproporphyrin Ferrochelatase. Febs J. 2019.
ISSN: ISSN 1742-464X
PubMed: 31794133
DOI: 10.1111/FEBS.15164