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Iron in PDB 3cv9: Crystal Structure of Vitamin D Hydroxylase Cytochrome P450 105A1 (R73A/R84A Mutant) in Complex with 1ALPHA,25- Dihydroxyvitamin D3

Enzymatic activity of Crystal Structure of Vitamin D Hydroxylase Cytochrome P450 105A1 (R73A/R84A Mutant) in Complex with 1ALPHA,25- Dihydroxyvitamin D3

All present enzymatic activity of Crystal Structure of Vitamin D Hydroxylase Cytochrome P450 105A1 (R73A/R84A Mutant) in Complex with 1ALPHA,25- Dihydroxyvitamin D3:
1.14.14.1;

Protein crystallography data

The structure of Crystal Structure of Vitamin D Hydroxylase Cytochrome P450 105A1 (R73A/R84A Mutant) in Complex with 1ALPHA,25- Dihydroxyvitamin D3, PDB code: 3cv9 was solved by K.Hayashi, H.Sugimoto, R.Shinkyo, M.Yamada, S.Ikeda, S.Ikushiro, M.Kamakura, Y.Shiro, T.Sakaki, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 1.70
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 53.315, 53.659, 140.605, 90.00, 90.00, 90.00
R / Rfree (%) 19.9 / 25.3

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure of Vitamin D Hydroxylase Cytochrome P450 105A1 (R73A/R84A Mutant) in Complex with 1ALPHA,25- Dihydroxyvitamin D3 (pdb code 3cv9). 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 Vitamin D Hydroxylase Cytochrome P450 105A1 (R73A/R84A Mutant) in Complex with 1ALPHA,25- Dihydroxyvitamin D3, PDB code: 3cv9:

Iron binding site 1 out of 1 in 3cv9

Go back to Iron Binding Sites List in 3cv9
Iron binding site 1 out of 1 in the Crystal Structure of Vitamin D Hydroxylase Cytochrome P450 105A1 (R73A/R84A Mutant) in Complex with 1ALPHA,25- Dihydroxyvitamin D3


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 Vitamin D Hydroxylase Cytochrome P450 105A1 (R73A/R84A Mutant) in Complex with 1ALPHA,25- Dihydroxyvitamin D3 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe413

b:13.8
occ:1.00
 FE A:HEM413 0.0 13.8 1.0
NB A:HEM413 2.0 12.4 1.0
NC A:HEM413 2.1 12.3 1.0
NA A:HEM413 2.1 11.5 1.0
ND A:HEM413 2.1 13.1 1.0
SG A:CYS355 2.4 13.5 1.0
C1B A:HEM413 3.0 12.0 1.0
C1C A:HEM413 3.0 15.1 1.0
C4B A:HEM413 3.0 13.5 1.0
C1D A:HEM413 3.1 11.7 1.0
C4C A:HEM413 3.1 13.8 1.0
C1A A:HEM413 3.1 13.1 1.0
C4A A:HEM413 3.1 11.5 1.0
C4D A:HEM413 3.1 12.1 1.0
CB A:CYS355 3.3 12.9 1.0
CHC A:HEM413 3.4 12.9 1.0
CHD A:HEM413 3.4 13.9 1.0
CHB A:HEM413 3.4 11.7 1.0
CHA A:HEM413 3.5 12.7 1.0
CA A:CYS355 4.0 12.4 1.0
C2B A:HEM413 4.3 12.8 1.0
C2C A:HEM413 4.3 11.5 1.0
C3B A:HEM413 4.3 14.2 1.0
C3C A:HEM413 4.3 12.5 1.0
C2D A:HEM413 4.3 13.4 1.0
C2A A:HEM413 4.3 12.8 1.0
C3A A:HEM413 4.3 12.9 1.0
C3D A:HEM413 4.3 13.1 1.0
C A:CYS355 4.7 13.0 1.0
N A:GLY357 4.7 12.1 1.0
N A:LEU356 4.7 12.6 1.0
CD1 A:PHE348 4.8 14.2 1.0

Reference:

K.Hayashi, H.Sugimoto, R.Shinkyo, M.Yamada, S.Ikeda, S.Ikushiro, M.Kamakura, Y.Shiro, T.Sakaki. Structure-Based Design of A Highly Active Vitamin D Hydroxylase From Streptomyces Griseolus CYP105A1 Biochemistry V. 47 11964 2008.
ISSN: ISSN 0006-2960
PubMed: 18937506
DOI: 10.1021/BI801222D
Page generated: Sun Aug 4 08:33:46 2024

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