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Iron in PDB 3voo: Cytochrome P450SP Alpha (CYP152B1) Mutant A245E

Enzymatic activity of Cytochrome P450SP Alpha (CYP152B1) Mutant A245E

All present enzymatic activity of Cytochrome P450SP Alpha (CYP152B1) Mutant A245E:
1.11.2.4;

Protein crystallography data

The structure of Cytochrome P450SP Alpha (CYP152B1) Mutant A245E, PDB code: 3voo was solved by T.Fujishiro, O.Shoji, H.Sugimoto, Y.Shiro, Y.Watanabe, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 19.64 / 2.34
Space group P 31 2 1
Cell size a, b, c (Å), α, β, γ (°) 94.426, 94.426, 113.260, 90.00, 90.00, 120.00
R / Rfree (%) 19.6 / 23.4

Iron Binding Sites:

The binding sites of Iron atom in the Cytochrome P450SP Alpha (CYP152B1) Mutant A245E (pdb code 3voo). 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 Cytochrome P450SP Alpha (CYP152B1) Mutant A245E, PDB code: 3voo:

Iron binding site 1 out of 1 in 3voo

Go back to Iron Binding Sites List in 3voo
Iron binding site 1 out of 1 in the Cytochrome P450SP Alpha (CYP152B1) Mutant A245E


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Cytochrome P450SP Alpha (CYP152B1) Mutant A245E within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe501

b:2.2
occ:1.00
FE A:HEM501 0.0 2.2 1.0
NC A:HEM501 2.1 2.0 1.0
NB A:HEM501 2.1 2.0 1.0
NA A:HEM501 2.1 2.0 1.0
ND A:HEM501 2.1 2.0 1.0
SG A:CYS361 2.2 14.8 1.0
O A:HOH649 2.6 20.7 1.0
C1B A:HEM501 3.1 2.0 1.0
C1C A:HEM501 3.1 2.0 1.0
C4C A:HEM501 3.1 2.0 1.0
C4A A:HEM501 3.1 2.0 1.0
C4B A:HEM501 3.1 2.0 1.0
C4D A:HEM501 3.1 2.0 1.0
C1A A:HEM501 3.1 2.0 1.0
C1D A:HEM501 3.1 2.0 1.0
CB A:CYS361 3.4 12.0 1.0
CHB A:HEM501 3.4 2.0 1.0
CHD A:HEM501 3.4 2.0 1.0
CHA A:HEM501 3.4 2.0 1.0
CHC A:HEM501 3.5 2.0 1.0
CA A:CYS361 4.2 11.9 1.0
C2B A:HEM501 4.3 2.1 1.0
C3C A:HEM501 4.3 2.0 1.0
C3B A:HEM501 4.3 2.0 1.0
C2C A:HEM501 4.3 2.0 1.0
C3A A:HEM501 4.3 2.0 1.0
O A:HOH650 4.3 30.0 1.0
C2A A:HEM501 4.3 2.0 1.0
C3D A:HEM501 4.3 2.0 1.0
C2D A:HEM501 4.4 2.0 1.0
NE2 A:GLN350 4.4 15.6 1.0
CB A:PRO242 4.6 13.8 1.0
CD A:PRO362 4.9 11.2 1.0
N A:GLY363 4.9 11.0 1.0
O A:HOH651 4.9 33.8 1.0
C A:CYS361 5.0 11.6 1.0

Reference:

O.Shoji, T.Fujishiro, K.Nishio, Y.Kano, H.Kimoto, S.-C.Chien, H.Onoda, A.Muramatsu, S.Tanaka, A.Hori, H.Sugimoto, Y.Shiro, Y.Watanabe. A Substrate-Binding-State Mimic of H2O2-Dependent Cytochrome P450 Produced By One-Point Mutagenesis and Peroxygenation of Non-Native Substrates Catalysis Science and V. 6 5806 2016TECHNOLOGY.
ISSN: ISSN 2044-4753
DOI: 10.1039/C6CY00630B
Page generated: Sun Aug 4 22:07:17 2024

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