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Iron in PDB 3awq: Cytochrome P450SP Alpha (CYP152B1) Mutant L78F

Enzymatic activity of Cytochrome P450SP Alpha (CYP152B1) Mutant L78F

All present enzymatic activity of Cytochrome P450SP Alpha (CYP152B1) Mutant L78F:
1.11.2.4;

Protein crystallography data

The structure of Cytochrome P450SP Alpha (CYP152B1) Mutant L78F, PDB code: 3awq was solved by T.Fujishiro, O.Shoji, S.Nagano, 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) 19.98 / 1.90
Space group P 31 2 1
Cell size a, b, c (Å), α, β, γ (°) 94.137, 94.137, 113.402, 90.00, 90.00, 120.00
R / Rfree (%) 15.9 / 18.8

Iron Binding Sites:

The binding sites of Iron atom in the Cytochrome P450SP Alpha (CYP152B1) Mutant L78F (pdb code 3awq). 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 L78F, PDB code: 3awq:

Iron binding site 1 out of 1 in 3awq

Go back to Iron Binding Sites List in 3awq
Iron binding site 1 out of 1 in the Cytochrome P450SP Alpha (CYP152B1) Mutant L78F


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 L78F within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe501

b:3.2
occ:1.00
FE A:HEM501 0.0 3.2 1.0
NB A:HEM501 2.0 3.2 1.0
ND A:HEM501 2.1 2.9 1.0
NA A:HEM501 2.1 2.9 1.0
NC A:HEM501 2.1 2.6 1.0
O A:HOH482 2.2 13.9 1.0
SG A:CYS361 2.3 7.9 1.0
C4B A:HEM501 3.0 4.3 1.0
C4D A:HEM501 3.1 3.1 1.0
C1D A:HEM501 3.1 2.4 1.0
C1B A:HEM501 3.1 3.8 1.0
C1C A:HEM501 3.1 3.6 1.0
C1A A:HEM501 3.1 2.4 1.0
C4A A:HEM501 3.1 3.4 1.0
C4C A:HEM501 3.1 3.1 1.0
CB A:CYS361 3.3 4.5 1.0
CHC A:HEM501 3.4 3.2 1.0
CHA A:HEM501 3.4 2.7 1.0
CHB A:HEM501 3.4 3.1 1.0
CHD A:HEM501 3.4 2.8 1.0
CA A:CYS361 4.2 5.7 1.0
C3B A:HEM501 4.3 4.2 1.0
C3D A:HEM501 4.3 2.3 1.0
C2B A:HEM501 4.3 4.6 1.0
C2D A:HEM501 4.3 2.4 1.0
C2C A:HEM501 4.3 4.5 1.0
C2A A:HEM501 4.3 3.2 1.0
C3C A:HEM501 4.3 3.8 1.0
C3A A:HEM501 4.3 3.8 1.0
NE2 A:GLN350 4.4 7.4 1.0
O A:HOH628 4.4 26.8 1.0
C2 A:PLM601 4.5 9.2 0.3
CB A:PRO242 4.6 7.5 1.0
CD A:PRO362 4.8 4.4 1.0
N A:GLY363 4.9 5.4 1.0
O A:HOH578 4.9 21.3 1.0
C A:CYS361 4.9 5.2 1.0

Reference:

T.Fujishiro, O.Shoji, S.Nagano, H.Sugimoto, Y.Shiro, Y.Watanabe. Crystal Structure of H2O2-Dependent Cytochrome P450SPALPHA with Its Bound Fatty Acid Substrate: Insight Into the Regioselective Hydroxylation of Fatty Acids at the Alpha Position. J.Biol.Chem. V. 286 29941 2011.
ISSN: ISSN 0021-9258
PubMed: 21719702
DOI: 10.1074/JBC.M111.245225
Page generated: Sun Dec 13 15:01:17 2020

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