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Iron in PDB 4jmv: Crystal Structure of Cytochrome C Peroxidase W191G-Gateless in Complex with Imidazo[1,2-A]Pyridin-6-Amine

Enzymatic activity of Crystal Structure of Cytochrome C Peroxidase W191G-Gateless in Complex with Imidazo[1,2-A]Pyridin-6-Amine

All present enzymatic activity of Crystal Structure of Cytochrome C Peroxidase W191G-Gateless in Complex with Imidazo[1,2-A]Pyridin-6-Amine:
1.11.1.5;

Protein crystallography data

The structure of Crystal Structure of Cytochrome C Peroxidase W191G-Gateless in Complex with Imidazo[1,2-A]Pyridin-6-Amine, PDB code: 4jmv was solved by S.Barelier, M.Fischer, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 29.19 / 1.82
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 106.560, 73.840, 51.230, 90.00, 90.00, 90.00
R / Rfree (%) 13.9 / 17.4

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure of Cytochrome C Peroxidase W191G-Gateless in Complex with Imidazo[1,2-A]Pyridin-6-Amine (pdb code 4jmv). 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 Cytochrome C Peroxidase W191G-Gateless in Complex with Imidazo[1,2-A]Pyridin-6-Amine, PDB code: 4jmv:

Iron binding site 1 out of 1 in 4jmv

Go back to Iron Binding Sites List in 4jmv
Iron binding site 1 out of 1 in the Crystal Structure of Cytochrome C Peroxidase W191G-Gateless in Complex with Imidazo[1,2-A]Pyridin-6-Amine


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 Cytochrome C Peroxidase W191G-Gateless in Complex with Imidazo[1,2-A]Pyridin-6-Amine within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe301

b:15.5
occ:1.00
 FE A:HEM301 0.0 15.5 1.0
NA A:HEM301 2.0 15.9 1.0
NC A:HEM301 2.0 14.8 1.0
NE2 A:HIS175 2.0 16.6 1.0
ND A:HEM301 2.0 15.5 1.0
NB A:HEM301 2.0 16.2 1.0
O A:HOH461 2.1 20.2 1.0
C1D A:HEM301 3.0 15.2 1.0
CD2 A:HIS175 3.0 16.7 1.0
C4B A:HEM301 3.0 16.2 1.0
CE1 A:HIS175 3.0 18.3 1.0
C1C A:HEM301 3.1 14.0 1.0
C4A A:HEM301 3.1 16.9 1.0
C1A A:HEM301 3.1 16.8 1.0
C4D A:HEM301 3.1 16.0 1.0
C1B A:HEM301 3.1 17.1 1.0
C4C A:HEM301 3.1 14.3 1.0
CHC A:HEM301 3.4 14.2 1.0
CHD A:HEM301 3.4 14.3 1.0
CHA A:HEM301 3.5 16.0 1.0
CHB A:HEM301 3.5 16.0 1.0
NE1 A:TRP51 4.0 16.0 1.0
NE A:ARG48 4.0 17.7 0.5
ND1 A:HIS175 4.2 17.2 1.0
CG A:HIS175 4.2 16.8 1.0
O A:HOH721 4.3 21.8 0.5
O A:HOH716 4.3 19.8 1.0
C3B A:HEM301 4.3 16.2 1.0
C2A A:HEM301 4.3 16.5 1.0
C2D A:HEM301 4.3 15.8 1.0
C3A A:HEM301 4.3 17.2 1.0
C2C A:HEM301 4.4 14.1 1.0
C3C A:HEM301 4.4 13.4 1.0
C3D A:HEM301 4.4 16.4 1.0
C2B A:HEM301 4.4 17.2 1.0
CD1 A:TRP51 4.5 15.4 1.0
NH1 A:ARG48 4.6 19.0 0.5
CZ A:ARG48 4.8 18.9 0.5
CD A:ARG48 4.8 17.0 0.5
CAC A:1LY302 4.9 15.9 0.5
CG A:ARG48 5.0 16.1 0.5

Reference:

S.Barelier, S.E.Boyce, I.Fish, M.Fischer, D.B.Goodin, B.K.Shoichet. Docking to A Water-Filled Model Binding Site in Cytochrome C Peroxidase To Be Published.
Page generated: Mon Aug 5 04:44:28 2024

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