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Iron in PDB 2d09: A Role For Active Site Water Molecules and Hydroxyl Groups of Substrate For Oxygen Activation in Cytochrome P450 158A2

Protein crystallography data

The structure of A Role For Active Site Water Molecules and Hydroxyl Groups of Substrate For Oxygen Activation in Cytochrome P450 158A2, PDB code: 2d09 was solved by B.Zhao, M.R.Waterman, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 15.00 / 1.80
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 55.000, 70.935, 102.950, 90.00, 90.00, 90.00
R / Rfree (%) 23.2 / 23.9

Iron Binding Sites:

The binding sites of Iron atom in the A Role For Active Site Water Molecules and Hydroxyl Groups of Substrate For Oxygen Activation in Cytochrome P450 158A2 (pdb code 2d09). 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 A Role For Active Site Water Molecules and Hydroxyl Groups of Substrate For Oxygen Activation in Cytochrome P450 158A2, PDB code: 2d09:

Iron binding site 1 out of 1 in 2d09

Go back to Iron Binding Sites List in 2d09
Iron binding site 1 out of 1 in the A Role For Active Site Water Molecules and Hydroxyl Groups of Substrate For Oxygen Activation in Cytochrome P450 158A2


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of A Role For Active Site Water Molecules and Hydroxyl Groups of Substrate For Oxygen Activation in Cytochrome P450 158A2 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe430

b:12.8
occ:1.00
FE A:HEM430 0.0 12.8 1.0
O2 A:OXY433 1.9 48.4 1.0
ND A:HEM430 2.0 12.9 1.0
NC A:HEM430 2.0 12.8 1.0
NB A:HEM430 2.0 11.3 1.0
NA A:HEM430 2.0 12.3 1.0
SG A:CYS353 2.3 18.4 1.0
O1 A:OXY433 2.7 48.2 1.0
C1C A:HEM430 3.0 13.3 1.0
C1B A:HEM430 3.0 11.8 1.0
C4D A:HEM430 3.1 9.9 1.0
C4B A:HEM430 3.1 10.8 1.0
C1A A:HEM430 3.1 10.1 1.0
C1D A:HEM430 3.1 12.5 1.0
C4C A:HEM430 3.1 12.7 1.0
C4A A:HEM430 3.1 11.0 1.0
CB A:CYS353 3.3 17.3 1.0
CHB A:HEM430 3.4 11.9 1.0
CHD A:HEM430 3.4 12.3 1.0
CHC A:HEM430 3.4 10.7 1.0
CHA A:HEM430 3.4 11.7 1.0
CA A:CYS353 4.2 14.5 1.0
C2C A:HEM430 4.3 13.2 1.0
C3B A:HEM430 4.3 12.5 1.0
C3D A:HEM430 4.3 11.6 1.0
C2D A:HEM430 4.3 11.9 1.0
C2B A:HEM430 4.3 13.1 1.0
C3C A:HEM430 4.3 13.2 1.0
C3A A:HEM430 4.3 13.0 1.0
C2A A:HEM430 4.3 12.7 1.0
O A:HOH529 4.6 18.2 1.0
CAF A:FLV431 4.6 18.6 1.0
O A:HOH664 4.9 27.0 1.0
C A:CYS353 4.9 12.6 1.0
N A:GLY355 5.0 10.2 1.0

Reference:

B.Zhao, F.P.Guengerich, M.Voehler, M.R.Waterman. Role of Active Site Water Molecules and Substrate Hydroxyl Groups in Oxygen Activation By Cytochrome P450 158A2: A New Mechanism of Proton Transfer J.Biol.Chem. V. 280 42188 2005.
ISSN: ISSN 0021-9258
PubMed: 16239228
DOI: 10.1074/JBC.M509220200
Page generated: Sat Aug 3 20:35:32 2024

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