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Iron in PDB 2as4: Cytochrome C Peroxidase in Complex with 3-Fluorocatechol

Enzymatic activity of Cytochrome C Peroxidase in Complex with 3-Fluorocatechol

All present enzymatic activity of Cytochrome C Peroxidase in Complex with 3-Fluorocatechol:
1.11.1.5;

Protein crystallography data

The structure of Cytochrome C Peroxidase in Complex with 3-Fluorocatechol, PDB code: 2as4 was solved by R.Brenk, S.W.Vetter, S.E.Boyce, D.B.Goodin, B.K.Shoichet, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 10.00 / 1.30
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 51.240, 75.490, 107.040, 90.00, 90.00, 90.00
R / Rfree (%) n/a / 17.5

Other elements in 2as4:

The structure of Cytochrome C Peroxidase in Complex with 3-Fluorocatechol also contains other interesting chemical elements:

Fluorine (F) 2 atoms
Potassium (K) 1 atom

Iron Binding Sites:

The binding sites of Iron atom in the Cytochrome C Peroxidase in Complex with 3-Fluorocatechol (pdb code 2as4). 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 Cytochrome C Peroxidase in Complex with 3-Fluorocatechol, PDB code: 2as4:

Iron binding site 1 out of 1 in 2as4

Go back to Iron Binding Sites List in 2as4
Iron binding site 1 out of 1 in the Cytochrome C Peroxidase in Complex with 3-Fluorocatechol


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Cytochrome C Peroxidase in Complex with 3-Fluorocatechol within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe400

b:13.7
occ:1.00
FE A:HEM400 0.0 13.7 1.0
NC A:HEM400 2.0 13.2 1.0
NA A:HEM400 2.1 14.8 1.0
ND A:HEM400 2.1 14.6 1.0
NE2 A:HIS175 2.1 14.3 1.0
NB A:HEM400 2.1 15.3 1.0
O A:HOH1415 2.1 26.2 1.0
CE1 A:HIS175 3.0 15.5 1.0
C1C A:HEM400 3.0 13.9 1.0
C1A A:HEM400 3.0 15.0 1.0
C4B A:HEM400 3.0 13.7 1.0
C4D A:HEM400 3.1 14.8 1.0
C4C A:HEM400 3.1 13.5 1.0
C4A A:HEM400 3.1 14.9 1.0
C1D A:HEM400 3.1 13.9 1.0
C1B A:HEM400 3.1 13.8 1.0
CD2 A:HIS175 3.1 15.5 1.0
CHC A:HEM400 3.3 13.8 1.0
CHA A:HEM400 3.4 15.4 1.0
CHD A:HEM400 3.4 13.5 1.0
CHB A:HEM400 3.4 14.8 1.0
NE A:ARG48 4.0 16.9 0.6
NE1 A:TRP51 4.0 17.1 1.0
ND1 A:HIS175 4.2 14.7 1.0
C2A A:HEM400 4.2 15.2 1.0
CG A:HIS175 4.2 14.2 1.0
C2C A:HEM400 4.2 14.0 1.0
O A:HOH1200 4.2 23.7 1.0
C3C A:HEM400 4.2 13.2 1.0
C3A A:HEM400 4.3 15.5 1.0
C3B A:HEM400 4.3 13.4 1.0
C3D A:HEM400 4.3 14.0 1.0
C2D A:HEM400 4.3 13.6 1.0
C2B A:HEM400 4.3 14.3 1.0
O A:HOH1003 4.5 25.7 0.2
CD1 A:TRP51 4.6 16.2 1.0
NH2 A:ARG48 4.6 15.3 0.6
CD A:ARG48 4.8 15.6 0.6
CZ A:ARG48 4.8 16.6 0.6
CG A:ARG48 4.9 15.9 0.6
C6 A:3FA500 4.9 26.0 0.8

Reference:

R.Brenk, S.W.Vetter, S.E.Boyce, D.B.Goodin, B.K.Shoichet. Probing Molecular Docking in A Charged Model Binding Site. J.Mol.Biol. V. 357 1449 2006.
ISSN: ISSN 0022-2836
PubMed: 16490206
DOI: 10.1016/J.JMB.2006.01.034
Page generated: Sun Dec 13 14:39:58 2020

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