Iron in PDB 6to2: Crystal Structure of CYP154C5 From Nocardia Farcinica in Complex with 5ALPHA-Androstan-3-One

The structure of Crystal Structure of CYP154C5 From Nocardia Farcinica in Complex with 5ALPHA-Androstan-3-One, PDB code: 6to2 was solved by A.Rodriguez, T.Kluenemann, W.Blankenfeldt, A.Schallmey, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	82.85 / 2.00
Space group	H 3
Cell size a, b, c (Å), α, β, γ (°)	103.411, 103.411, 218.210, 90.00, 90.00, 120.00
R / Rfree (%)	20.7 / 24.9

The structure of Crystal Structure of CYP154C5 From Nocardia Farcinica in Complex with 5ALPHA-Androstan-3-One also contains other interesting chemical elements:

Chlorine

(Cl)

2 atoms

The binding sites of Iron atom in the Crystal Structure of CYP154C5 From Nocardia Farcinica in Complex with 5ALPHA-Androstan-3-One (pdb code 6to2). 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 CYP154C5 From Nocardia Farcinica in Complex with 5ALPHA-Androstan-3-One, PDB code: 6to2:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Crystal Structure of CYP154C5 From Nocardia Farcinica in Complex with 5ALPHA-Androstan-3-One


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 CYP154C5 From Nocardia Farcinica in Complex with 5ALPHA-Androstan-3-One within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe501 b:25.4 occ:1.00 FE A:HEM501 0.0 25.4 1.0 ND A:HEM501 2.0 28.3 1.0 NA A:HEM501 2.0 28.2 1.0 NC A:HEM501 2.1 27.6 1.0 NB A:HEM501 2.2 28.8 1.0 SG A:CYS357 2.3 26.5 1.0 C4D A:HEM501 2.9 29.2 1.0 C1A A:HEM501 3.0 27.7 1.0 HB2 A:CYS357 3.0 34.1 1.0 C1D A:HEM501 3.0 28.2 1.0 C4C A:HEM501 3.1 28.2 1.0 C4A A:HEM501 3.1 28.5 1.0 C1C A:HEM501 3.2 28.2 1.0 C1B A:HEM501 3.2 26.4 1.0 CB A:CYS357 3.2 28.4 1.0 C4B A:HEM501 3.3 27.9 1.0 CHA A:HEM501 3.3 27.6 1.0 H9 A:NQ8502 3.4 30.8 1.0 CHD A:HEM501 3.4 28.2 1.0 CHB A:HEM501 3.5 27.8 1.0 CHC A:HEM501 3.6 25.6 1.0 HB1 A:ALA244 3.6 30.8 1.0 HD2 A:PRO358 3.6 31.6 1.0 HA A:CYS357 3.6 33.5 1.0 CA A:CYS357 4.0 27.9 1.0 HB3 A:CYS357 4.0 34.1 1.0 H A:GLY359 4.1 34.0 1.0 H7 A:NQ8502 4.1 32.6 1.0 C3D A:HEM501 4.2 34.1 1.0 C2D A:HEM501 4.2 33.7 1.0 C2A A:HEM501 4.2 28.7 1.0 HD1 A:PHE350 4.3 37.6 1.0 C3A A:HEM501 4.3 29.4 1.0 HHA A:HEM501 4.3 33.1 1.0 C3C A:HEM501 4.3 27.6 1.0 C6 A:NQ8502 4.3 25.6 1.0 C2C A:HEM501 4.3 28.8 1.0 HHD A:HEM501 4.4 33.8 1.0 HG21 A:THR248 4.4 33.4 1.0 C2B A:HEM501 4.4 26.2 1.0 H10 A:NQ8502 4.5 30.8 1.0 C3B A:HEM501 4.5 26.9 1.0 HHB A:HEM501 4.5 33.4 1.0 CB A:ALA244 4.5 25.6 1.0 CD A:PRO358 4.5 26.3 1.0 HHC A:HEM501 4.6 30.7 1.0 HB3 A:ALA244 4.7 30.8 1.0 C5 A:NQ8502 4.8 27.1 1.0 C A:CYS357 4.8 27.9 1.0 HD3 A:PRO358 4.8 31.6 1.0 HB2 A:ALA244 4.9 30.8 1.0 N A:PRO358 4.9 26.6 1.0 N A:GLY359 4.9 28.3 1.0

Iron binding site 2 out of 2 in the Crystal Structure of CYP154C5 From Nocardia Farcinica in Complex with 5ALPHA-Androstan-3-One


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 CYP154C5 From Nocardia Farcinica in Complex with 5ALPHA-Androstan-3-One within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe501 b:26.0 occ:1.00 FE B:HEM501 0.0 26.0 1.0 ND B:HEM501 2.0 27.7 1.0 NC B:HEM501 2.1 27.3 1.0 NA B:HEM501 2.1 28.7 1.0 NB B:HEM501 2.1 25.7 1.0 SG B:CYS357 2.2 22.7 1.0 C4D B:HEM501 3.0 26.1 1.0 C1D B:HEM501 3.0 27.8 1.0 C4C B:HEM501 3.0 23.2 1.0 C1A B:HEM501 3.0 23.9 1.0 HB2 B:CYS357 3.1 33.9 1.0 C1C B:HEM501 3.1 26.8 1.0 C4A B:HEM501 3.1 25.9 1.0 C1B B:HEM501 3.1 23.7 1.0 C4B B:HEM501 3.2 25.6 1.0 CB B:CYS357 3.2 28.2 1.0 CHA B:HEM501 3.4 25.3 1.0 H9 B:NQ8502 3.4 36.9 1.0 CHD B:HEM501 3.4 25.8 1.0 CHB B:HEM501 3.5 25.9 1.0 CHC B:HEM501 3.5 25.6 1.0 HB1 B:ALA244 3.5 35.3 1.0 HA B:CYS357 3.7 36.3 1.0 HD2 B:PRO358 3.8 32.9 1.0 HB3 B:CYS357 4.0 33.9 1.0 CA B:CYS357 4.0 30.2 1.0 H B:GLY359 4.1 29.2 1.0 H7 B:NQ8502 4.1 39.9 1.0 HD1 B:PHE350 4.2 36.3 1.0 C3D B:HEM501 4.2 29.0 1.0 C3C B:HEM501 4.2 22.9 1.0 C2D B:HEM501 4.2 30.9 1.0 C2C B:HEM501 4.3 25.2 1.0 C6 B:NQ8502 4.3 30.7 1.0 C2A B:HEM501 4.3 23.1 1.0 HHA B:HEM501 4.3 30.4 1.0 C3A B:HEM501 4.3 24.0 1.0 C2B B:HEM501 4.4 20.2 1.0 C3B B:HEM501 4.4 27.5 1.0 HHD B:HEM501 4.4 31.0 1.0 HG21 B:THR248 4.4 33.9 1.0 CB B:ALA244 4.4 29.4 1.0 H10 B:NQ8502 4.4 36.9 1.0 HHB B:HEM501 4.5 31.1 1.0 HHC B:HEM501 4.5 30.7 1.0 HB3 B:ALA244 4.7 35.3 1.0 HB2 B:ALA244 4.7 35.3 1.0 C5 B:NQ8502 4.7 33.2 1.0 CD B:PRO358 4.7 27.4 1.0 C B:CYS357 4.8 32.1 1.0 N B:GLY359 4.9 24.3 1.0 HA3 B:GLY359 4.9 30.6 1.0 N B:PRO358 4.9 29.7 1.0

P.Bracco, H.J.Wijma, B.Nicolai, J.A.Rodriguez Buitrago, T.Klunemann, A.Vila, P.Schrepfer, W.Blankenfeldt, D.B.Janssen, A.Schallmey. CYP154C5 Regioselectivity in Steroid Hydroxylation Explored By Substrate Modifications and Protein Engineering. Chembiochem 2020.
ISSN: ESSN 1439-7633
PubMed: 33145893
DOI: 10.1002/CBIC.202000735