Iron in PDB 3zkp: Structure of A Mutant of P450 Eryk in Complex with Erythromycin B.

All present enzymatic activity of Structure of A Mutant of P450 Eryk in Complex with Erythromycin B.:
1.14.13.154;

The structure of Structure of A Mutant of P450 Eryk in Complex with Erythromycin B., PDB code: 3zkp was solved by L.C.Montemiglio, B.Vallone, C.Savino, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	29.12 / 2.00
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	57.753, 36.597, 96.273, 90.00, 92.93, 90.00
R / Rfree (%)	16.332 / 21.529

The binding sites of Iron atom in the Structure of A Mutant of P450 Eryk in Complex with Erythromycin B. (pdb code 3zkp). 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 A Mutant of P450 Eryk in Complex with Erythromycin B., PDB code: 3zkp:

Iron binding site 1 out of 1 in the Structure of A Mutant of P450 Eryk in Complex with Erythromycin B.


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Structure of A Mutant of P450 Eryk in Complex with Erythromycin B. within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe412 b:9.7 occ:1.00 FE A:HEM412 0.0 9.7 1.0 NA A:HEM412 2.1 7.9 1.0 NB A:HEM412 2.1 8.5 1.0 NC A:HEM412 2.1 8.1 1.0 ND A:HEM412 2.2 8.7 1.0 SG A:CYS353 2.3 10.3 1.0 O A:HOH2213 2.7 22.2 1.0 C4A A:HEM412 3.1 6.0 1.0 C1B A:HEM412 3.1 8.4 1.0 C1C A:HEM412 3.1 7.9 1.0 C4B A:HEM412 3.1 8.2 1.0 C1A A:HEM412 3.1 8.9 1.0 C4C A:HEM412 3.1 8.2 1.0 C4D A:HEM412 3.1 8.5 1.0 C1D A:HEM412 3.2 8.8 1.0 CB A:CYS353 3.3 8.2 1.0 CHB A:HEM412 3.4 7.5 1.0 CHC A:HEM412 3.5 8.0 1.0 CHA A:HEM412 3.5 7.8 1.0 CHD A:HEM412 3.5 8.5 1.0 CA A:CYS353 4.0 8.7 1.0 C3A A:HEM412 4.3 8.7 1.0 C2B A:HEM412 4.3 8.8 1.0 C2C A:HEM412 4.3 8.7 1.0 C2A A:HEM412 4.3 7.5 1.0 C3C A:HEM412 4.3 8.9 1.0 C3B A:HEM412 4.3 7.6 1.0 C3D A:HEM412 4.4 7.9 1.0 C2D A:HEM412 4.4 8.3 1.0 O A:ALA241 4.5 9.7 1.0 N A:GLY355 4.5 9.5 1.0 C A:CYS353 4.7 8.7 1.0 N A:LEU354 4.8 9.5 1.0 CB A:ALA241 4.9 8.2 1.0 CA A:GLY355 4.9 9.4 1.0

L.C.Montemiglio, A.Macone, C.Ardiccioni, G.Avella, B.Vallone, C.Savino. Redirecting P450 Eryk Specificity By Rational Site-Directed Mutagenesis. Biochemistry V. 52 3678 2013.
ISSN: ISSN 0006-2960
PubMed: 23597312
DOI: 10.1021/BI400223J