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Iron in PDB 5x23: Crystal Structure of CYP2C9 Genetic Variant A477T (*30) in Complex with Multiple Losartan Molecules

Enzymatic activity of Crystal Structure of CYP2C9 Genetic Variant A477T (*30) in Complex with Multiple Losartan Molecules

All present enzymatic activity of Crystal Structure of CYP2C9 Genetic Variant A477T (*30) in Complex with Multiple Losartan Molecules:
1.14.13.48; 1.14.13.49; 1.14.13.80; 1.14.99.38;

Protein crystallography data

The structure of Crystal Structure of CYP2C9 Genetic Variant A477T (*30) in Complex with Multiple Losartan Molecules, PDB code: 5x23 was solved by K.Maekawa, M.Adachi, M.B.Shah, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 45.51 / 2.00
Space group I 2 2 2
Cell size a, b, c (Å), α, β, γ (°) 74.952, 142.273, 161.831, 90.00, 90.00, 90.00
R / Rfree (%) 21.7 / 25.3

Other elements in 5x23:

The structure of Crystal Structure of CYP2C9 Genetic Variant A477T (*30) in Complex with Multiple Losartan Molecules also contains other interesting chemical elements:

Potassium (K) 1 atom
Chlorine (Cl) 4 atoms

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure of CYP2C9 Genetic Variant A477T (*30) in Complex with Multiple Losartan Molecules (pdb code 5x23). 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 Crystal Structure of CYP2C9 Genetic Variant A477T (*30) in Complex with Multiple Losartan Molecules, PDB code: 5x23:

Iron binding site 1 out of 1 in 5x23

Go back to Iron Binding Sites List in 5x23
Iron binding site 1 out of 1 in the Crystal Structure of CYP2C9 Genetic Variant A477T (*30) in Complex with Multiple Losartan Molecules


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 CYP2C9 Genetic Variant A477T (*30) in Complex with Multiple Losartan Molecules within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe501

b:30.0
occ:1.00
 FE A:HEM501 0.0 30.0 1.0
ND A:HEM501 1.9 29.0 1.0
NA A:HEM501 2.0 32.3 1.0
O A:HOH662 2.0 51.1 1.0
NB A:HEM501 2.1 27.9 1.0
NC A:HEM501 2.1 31.6 1.0
SG A:CYS435 2.5 28.2 1.0
C4D A:HEM501 2.8 27.7 1.0
C1D A:HEM501 2.9 27.2 1.0
C1A A:HEM501 3.0 31.6 1.0
C4B A:HEM501 3.0 23.7 1.0
C4A A:HEM501 3.0 30.0 1.0
C1B A:HEM501 3.0 26.6 1.0
C4C A:HEM501 3.0 31.8 1.0
C1C A:HEM501 3.1 29.2 1.0
CHA A:HEM501 3.3 27.0 1.0
CHD A:HEM501 3.3 28.4 1.0
CHB A:HEM501 3.4 28.8 1.0
CHC A:HEM501 3.4 25.2 1.0
CB A:CYS435 3.5 26.3 1.0
C3D A:HEM501 4.1 28.4 1.0
C2D A:HEM501 4.1 28.7 1.0
C2A A:HEM501 4.2 28.0 1.0
C3A A:HEM501 4.2 26.8 1.0
O A:ALA297 4.2 37.1 1.0
C2B A:HEM501 4.2 21.9 1.0
C3C A:HEM501 4.2 31.9 1.0
C2C A:HEM501 4.2 28.6 1.0
C3B A:HEM501 4.2 27.1 1.0
CA A:CYS435 4.3 27.5 1.0
CB A:ALA297 4.6 36.9 1.0
C5 A:LSN502 4.7 53.7 1.0
N A:GLY437 4.8 31.6 1.0
C A:ALA297 4.9 37.4 1.0
C A:CYS435 4.9 28.3 1.0
N A:VAL436 5.0 27.9 1.0

Reference:

K.Maekawa, M.Adachi, Y.Matsuzawa, Q.Zhang, R.Kuroki, Y.Saito, M.B.Shah. Structural Basis of Single-Nucleotide Polymorphisms in Cytochrome P450 2C9 Biochemistry V. 56 5476 2017.
ISSN: ISSN 1520-4995
PubMed: 28972767
DOI: 10.1021/ACS.BIOCHEM.7B00795
Page generated: Tue Aug 6 11:29:49 2024

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