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Iron in PDB 5vcg: Crystal Structure of the Cysteine Depleted CYP3A4 Bound to Bromoergocryptine

Enzymatic activity of Crystal Structure of the Cysteine Depleted CYP3A4 Bound to Bromoergocryptine

All present enzymatic activity of Crystal Structure of the Cysteine Depleted CYP3A4 Bound to Bromoergocryptine:
1.14.13.157; 1.14.13.32; 1.14.13.67; 1.14.13.9;

Protein crystallography data

The structure of Crystal Structure of the Cysteine Depleted CYP3A4 Bound to Bromoergocryptine, PDB code: 5vcg was solved by I.Sevrioukova, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 80.31 / 2.20
Space group I 2 2 2
Cell size a, b, c (Å), α, β, γ (°) 76.539, 100.459, 133.679, 90.00, 90.00, 90.00
R / Rfree (%) 23.5 / 27.2

Other elements in 5vcg:

The structure of Crystal Structure of the Cysteine Depleted CYP3A4 Bound to Bromoergocryptine also contains other interesting chemical elements:

Bromine (Br) 1 atom

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure of the Cysteine Depleted CYP3A4 Bound to Bromoergocryptine (pdb code 5vcg). 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 the Cysteine Depleted CYP3A4 Bound to Bromoergocryptine, PDB code: 5vcg:

Iron binding site 1 out of 1 in 5vcg

Go back to Iron Binding Sites List in 5vcg
Iron binding site 1 out of 1 in the Crystal Structure of the Cysteine Depleted CYP3A4 Bound to Bromoergocryptine


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 the Cysteine Depleted CYP3A4 Bound to Bromoergocryptine within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe601

b:51.7
occ:1.00
 FE A:HEM601 0.0 51.7 1.0
ND A:HEM601 1.9 52.5 1.0
NA A:HEM601 2.0 54.0 1.0
NB A:HEM601 2.1 59.3 1.0
NC A:HEM601 2.1 54.0 1.0
SG A:CYS442 2.3 48.7 1.0
C4D A:HEM601 2.9 53.7 1.0
C1D A:HEM601 3.0 55.3 1.0
C4A A:HEM601 3.0 52.9 1.0
C1A A:HEM601 3.0 51.7 1.0
C1B A:HEM601 3.0 57.0 1.0
C4B A:HEM601 3.1 58.4 1.0
C4C A:HEM601 3.1 54.5 1.0
C1C A:HEM601 3.1 58.7 1.0
CB A:CYS442 3.3 47.8 1.0
CHA A:HEM601 3.4 53.8 1.0
CHB A:HEM601 3.4 53.1 1.0
CHD A:HEM601 3.5 53.0 1.0
C7 A:08Y602 3.5 0.5 1.0
CHC A:HEM601 3.5 58.9 1.0
C6 A:08Y602 3.5 0.6 1.0
CA A:CYS442 4.1 48.9 1.0
C3D A:HEM601 4.2 57.5 1.0
C3A A:HEM601 4.2 52.0 1.0
C2D A:HEM601 4.2 56.7 1.0
C2A A:HEM601 4.2 52.8 1.0
C2B A:HEM601 4.3 59.2 1.0
C3C A:HEM601 4.3 57.2 1.0
C2C A:HEM601 4.3 58.1 1.0
C3B A:HEM601 4.3 59.9 1.0
C4 A:08Y602 4.8 0.4 1.0
N2 A:08Y602 4.9 0.6 1.0
C A:CYS442 4.9 52.5 1.0

Reference:

I.F.Sevrioukova, I.Sevrioukova. N/A N/A.
ISSN: ISSN 1520-4995
PubMed: 28590129
DOI: 10.1021/ACS.BIOCHEM.7B00334
Page generated: Tue Aug 6 10:17:55 2024

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