Iron in PDB 5e78: Crystal Structure of P450 BM3 Heme Domain Variant Complexed with Co(III)Sep

All present enzymatic activity of Crystal Structure of P450 BM3 Heme Domain Variant Complexed with Co(III)Sep:
1.14.14.1; 1.6.2.4;

The structure of Crystal Structure of P450 BM3 Heme Domain Variant Complexed with Co(III)Sep, PDB code: 5e78 was solved by S.Panneerselvm, A.Shehzad, M.Bocola, J.Mueller-Dieckmann, U.Schwaneberg, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 2.00
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	58.970, 128.540, 150.060, 90.00, 90.00, 90.00
R / Rfree (%)	17.5 / 21.2

The structure of Crystal Structure of P450 BM3 Heme Domain Variant Complexed with Co(III)Sep also contains other interesting chemical elements:

Cobalt	(Co)	1 atom
Chlorine	(Cl)	1 atom

The binding sites of Iron atom in the Crystal Structure of P450 BM3 Heme Domain Variant Complexed with Co(III)Sep (pdb code 5e78). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Crystal Structure of P450 BM3 Heme Domain Variant Complexed with Co(III)Sep, PDB code: 5e78:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Crystal Structure of P450 BM3 Heme Domain Variant Complexed with Co(III)Sep


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 P450 BM3 Heme Domain Variant Complexed with Co(III)Sep within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe501 b:15.4 occ:1.00 FE A:HEM501 0.0 15.4 1.0 ND A:HEM501 1.9 15.7 1.0 NA A:HEM501 2.0 12.4 1.0 NC A:HEM501 2.1 12.7 1.0 NB A:HEM501 2.1 13.4 1.0 SG A:CYS400 2.2 15.5 1.0 O A:HOH623 2.3 22.9 1.0 C1D A:HEM501 3.0 13.6 1.0 C4D A:HEM501 3.0 16.4 1.0 C1A A:HEM501 3.0 13.9 1.0 C4A A:HEM501 3.0 14.1 1.0 C4B A:HEM501 3.1 12.9 1.0 C1B A:HEM501 3.1 13.0 1.0 C4C A:HEM501 3.1 13.8 1.0 C1C A:HEM501 3.1 14.5 1.0 CB A:CYS400 3.3 15.2 1.0 CHA A:HEM501 3.4 15.1 1.0 CHD A:HEM501 3.4 13.5 1.0 CHB A:HEM501 3.4 12.5 1.0 CHC A:HEM501 3.5 13.2 1.0 CA A:CYS400 4.1 14.1 1.0 O A:ALA264 4.2 25.6 1.0 C2A A:HEM501 4.2 15.3 1.0 C2D A:HEM501 4.2 15.9 1.0 C3A A:HEM501 4.2 15.5 1.0 C3D A:HEM501 4.2 14.9 1.0 C2C A:HEM501 4.3 15.7 1.0 C3C A:HEM501 4.3 16.1 1.0 C2B A:HEM501 4.3 12.8 1.0 C3B A:HEM501 4.3 14.1 1.0 CB A:ALA264 4.8 21.1 1.0 C A:ALA264 4.9 24.2 1.0 C A:CYS400 4.9 14.3 1.0 O A:HOH1021 4.9 45.0 1.0 N A:GLY402 4.9 13.9 1.0

Iron binding site 2 out of 2 in the Crystal Structure of P450 BM3 Heme Domain Variant Complexed with Co(III)Sep


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Crystal Structure of P450 BM3 Heme Domain Variant Complexed with Co(III)Sep within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe501 b:13.9 occ:1.00 FE B:HEM501 0.0 13.9 1.0 ND B:HEM501 1.9 12.3 1.0 NA B:HEM501 2.0 14.3 1.0 NB B:HEM501 2.1 15.1 1.0 NC B:HEM501 2.1 11.5 1.0 O B:HOH714 2.1 22.8 1.0 SG B:CYS400 2.2 14.2 1.0 C1D B:HEM501 3.0 13.7 1.0 C4D B:HEM501 3.0 15.2 1.0 C1A B:HEM501 3.0 16.4 1.0 C4A B:HEM501 3.1 17.6 1.0 C4B B:HEM501 3.1 13.9 1.0 C1B B:HEM501 3.1 17.3 1.0 C4C B:HEM501 3.1 14.4 1.0 C1C B:HEM501 3.1 17.1 1.0 CB B:CYS400 3.3 13.7 1.0 CHA B:HEM501 3.4 16.4 1.0 CHD B:HEM501 3.4 12.3 1.0 CHB B:HEM501 3.4 13.1 1.0 CHC B:HEM501 3.4 12.8 1.0 CA B:CYS400 4.1 13.2 1.0 O B:ALA264 4.1 32.0 1.0 C2D B:HEM501 4.2 16.2 1.0 C3D B:HEM501 4.2 14.7 1.0 C3A B:HEM501 4.3 13.9 1.0 C2A B:HEM501 4.3 14.8 1.0 C2B B:HEM501 4.3 13.8 1.0 C2C B:HEM501 4.3 14.0 1.0 C3B B:HEM501 4.3 17.0 1.0 C3C B:HEM501 4.3 15.2 1.0 CB B:ALA264 4.8 34.0 1.0 C B:ALA264 4.8 33.1 1.0 C B:CYS400 4.9 13.7 1.0 N B:GLY402 4.9 14.9 1.0

S.Panneerselvam, A.Shehzad, J.Mueller-Dieckmann, M.Wilmanns, M.Bocola, M.D.Davari, U.Schwaneberg. Crystallographic Insights Into A Cobalt (III) Sepulchrate Based Alternative Cofactor System of P450 BM3 Monooxygenase. Biochim. Biophys. Acta V.1866 134 2018.
ISSN: ISSN 0006-3002
PubMed: 28739446
DOI: 10.1016/J.BBAPAP.2017.07.010