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Iron in PDB 8vf3: The Crystal Structure of Galqe CYP199A4 Bound to 4-Methoxybenzoic Acid

Protein crystallography data

The structure of The Crystal Structure of Galqe CYP199A4 Bound to 4-Methoxybenzoic Acid, PDB code: 8vf3 was solved by M.N.Podgorski, S.G.Bell, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 45.00 / 1.47
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 45.085, 51.53, 78.52, 90, 93.53, 90
R / Rfree (%) 15.3 / 17.3

Other elements in 8vf3:

The structure of The Crystal Structure of Galqe CYP199A4 Bound to 4-Methoxybenzoic Acid also contains other interesting chemical elements:

Chlorine (Cl) 1 atom
Magnesium (Mg) 1 atom

Iron Binding Sites:

The binding sites of Iron atom in the The Crystal Structure of Galqe CYP199A4 Bound to 4-Methoxybenzoic Acid (pdb code 8vf3). 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 The Crystal Structure of Galqe CYP199A4 Bound to 4-Methoxybenzoic Acid, PDB code: 8vf3:

Iron binding site 1 out of 1 in 8vf3

Go back to Iron Binding Sites List in 8vf3
Iron binding site 1 out of 1 in the The Crystal Structure of Galqe CYP199A4 Bound to 4-Methoxybenzoic Acid


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of The Crystal Structure of Galqe CYP199A4 Bound to 4-Methoxybenzoic Acid within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe502

b:7.9
occ:1.00
FE A:HEM502 0.0 7.9 1.0
ND A:HEM502 2.0 7.2 1.0
NC A:HEM502 2.0 7.8 1.0
NA A:HEM502 2.0 8.7 1.0
NB A:HEM502 2.0 7.5 1.0
O A:HOH621 2.2 7.0 0.7
SG A:CYS358 2.3 8.9 1.0
C1C A:HEM502 3.0 6.0 1.0
C4C A:HEM502 3.0 8.1 1.0
C1D A:HEM502 3.1 8.2 1.0
C4D A:HEM502 3.1 6.9 1.0
C4A A:HEM502 3.1 7.7 1.0
C4B A:HEM502 3.1 8.5 1.0
C1B A:HEM502 3.1 7.3 1.0
C1A A:HEM502 3.1 7.3 1.0
CB A:CYS358 3.4 7.4 1.0
CHC A:HEM502 3.4 6.6 1.0
CHD A:HEM502 3.4 8.5 1.0
CHB A:HEM502 3.4 7.4 1.0
CHA A:HEM502 3.4 8.1 1.0
CA A:CYS358 4.1 8.5 1.0
O A:GLY248 4.1 17.9 1.0
C2C A:HEM502 4.2 7.0 1.0
C3C A:HEM502 4.3 7.8 1.0
C3D A:HEM502 4.3 8.2 1.0
C2D A:HEM502 4.3 8.1 1.0
C3A A:HEM502 4.3 7.8 1.0
C3B A:HEM502 4.3 7.5 1.0
C8 A:ANN501 4.3 9.8 1.0
C2A A:HEM502 4.3 6.3 1.0
C2B A:HEM502 4.3 7.0 1.0
OE2 A:GLU252 4.4 15.1 1.0
C A:CYS358 4.8 7.5 1.0
N A:GLY360 4.9 8.4 1.0

Reference:

M.N.Podgorski, J.Akter, L.R.Churchman, J.B.Bruning, J.J.De Voss, S.G.Bell. Engineering Peroxygenase Activity Into Cytochrome P450 Monooxygenases Through Modification of the Oxygen Binding Region Acs Catalysis 7426 2024.
ISSN: ESSN 2155-5435
DOI: 10.1021/ACSCATAL.4C01326
Page generated: Fri Aug 8 00:05:29 2025

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