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Iron in PDB 3p3z: Crystal Structure of the Cytochrome P450 Monooxygenase Aurh From Streptomyces Thioluteus in Complex with Ancymidol

Protein crystallography data

The structure of Crystal Structure of the Cytochrome P450 Monooxygenase Aurh From Streptomyces Thioluteus in Complex with Ancymidol, PDB code: 3p3z was solved by G.Zocher, M.E.A.Richter, U.Mueller, C.Hertweck, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 2.30
Space group H 3
Cell size a, b, c (Å), α, β, γ (°) 129.370, 129.370, 71.070, 90.00, 90.00, 120.00
R / Rfree (%) 18.3 / 23.1

Other elements in 3p3z:

The structure of Crystal Structure of the Cytochrome P450 Monooxygenase Aurh From Streptomyces Thioluteus in Complex with Ancymidol also contains other interesting chemical elements:

Chlorine (Cl) 3 atoms

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure of the Cytochrome P450 Monooxygenase Aurh From Streptomyces Thioluteus in Complex with Ancymidol (pdb code 3p3z). 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 Cytochrome P450 Monooxygenase Aurh From Streptomyces Thioluteus in Complex with Ancymidol, PDB code: 3p3z:

Iron binding site 1 out of 1 in 3p3z

Go back to Iron Binding Sites List in 3p3z
Iron binding site 1 out of 1 in the Crystal Structure of the Cytochrome P450 Monooxygenase Aurh From Streptomyces Thioluteus in Complex with Ancymidol


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 Cytochrome P450 Monooxygenase Aurh From Streptomyces Thioluteus in Complex with Ancymidol within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe501

b:13.0
occ:1.00
FE A:HEM501 0.0 13.0 1.0
NA A:HEM501 2.0 11.7 1.0
NB A:HEM501 2.1 11.4 1.0
NC A:HEM501 2.1 14.0 1.0
ND A:HEM501 2.1 14.6 1.0
NAM A:P3Z502 2.4 22.9 0.8
SG A:CYS355 2.4 12.4 1.0
C4A A:HEM501 3.1 10.8 1.0
C1A A:HEM501 3.1 12.0 1.0
C4C A:HEM501 3.1 15.8 1.0
C1C A:HEM501 3.1 13.7 1.0
C1B A:HEM501 3.1 10.4 1.0
C4B A:HEM501 3.1 11.4 1.0
C4D A:HEM501 3.1 14.5 1.0
C1D A:HEM501 3.1 15.8 1.0
CAG A:P3Z502 3.1 23.0 0.8
CB A:CYS355 3.4 12.1 1.0
CAI A:P3Z502 3.4 24.1 0.8
CHA A:HEM501 3.4 13.2 1.0
CHB A:HEM501 3.4 10.2 1.0
CHC A:HEM501 3.4 12.8 1.0
CHD A:HEM501 3.4 16.4 1.0
CA A:CYS355 4.0 13.2 1.0
C3A A:HEM501 4.3 10.6 1.0
C2A A:HEM501 4.3 11.4 1.0
C3C A:HEM501 4.3 16.8 1.0
C2C A:HEM501 4.3 15.4 1.0
C2B A:HEM501 4.3 9.8 1.0
C3B A:HEM501 4.3 10.3 1.0
C3D A:HEM501 4.3 16.0 1.0
C2D A:HEM501 4.3 17.0 1.0
NAL A:P3Z502 4.4 23.8 0.8
CAQ A:P3Z502 4.6 25.4 0.8
O A:ALA243 4.7 22.7 1.0
CB A:ALA243 4.7 24.5 1.0
C A:CYS355 4.7 14.5 1.0
N A:LEU356 4.8 16.0 1.0
N A:GLY357 4.9 16.3 1.0

Reference:

G.Zocher, M.E.Richter, U.Mueller, C.Hertweck. Structural Fine-Tuning of A Multifunctional Cytochrome P450 Monooxygenase. J.Am.Chem.Soc. V. 133 2292 2011.
ISSN: ISSN 0002-7863
PubMed: 21280577
DOI: 10.1021/JA110146Z
Page generated: Sun Dec 13 15:16:25 2020

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