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Iron in PDB 2ycg: Structure of Unreduced Ferric Cytochrome C Peroxidase Obtained By Multicrystal Method

Enzymatic activity of Structure of Unreduced Ferric Cytochrome C Peroxidase Obtained By Multicrystal Method

All present enzymatic activity of Structure of Unreduced Ferric Cytochrome C Peroxidase Obtained By Multicrystal Method:
1.11.1.5;

Protein crystallography data

The structure of Structure of Unreduced Ferric Cytochrome C Peroxidase Obtained By Multicrystal Method, PDB code: 2ycg was solved by A.Gumiero, E.L.Raven, P.C.E.Moody, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 10.00 / 1.81
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 51.118, 75.600, 106.752, 90.00, 90.00, 90.00
R / Rfree (%) n/a / 19.6

Iron Binding Sites:

The binding sites of Iron atom in the Structure of Unreduced Ferric Cytochrome C Peroxidase Obtained By Multicrystal Method (pdb code 2ycg). 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 Structure of Unreduced Ferric Cytochrome C Peroxidase Obtained By Multicrystal Method, PDB code: 2ycg:

Iron binding site 1 out of 1 in 2ycg

Go back to Iron Binding Sites List in 2ycg
Iron binding site 1 out of 1 in the Structure of Unreduced Ferric Cytochrome C Peroxidase Obtained By Multicrystal Method


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Structure of Unreduced Ferric Cytochrome C Peroxidase Obtained By Multicrystal Method within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe301

b:6.8
occ:1.00
FE A:HEM301 0.0 6.8 1.0
O A:HOH495 2.0 10.1 1.0
NC A:HEM301 2.0 3.4 1.0
NA A:HEM301 2.0 6.4 1.0
NE2 A:HIS175 2.0 8.0 1.0
ND A:HEM301 2.1 5.0 1.0
NB A:HEM301 2.1 7.2 1.0
C4C A:HEM301 3.0 2.9 1.0
C1A A:HEM301 3.0 9.6 1.0
CE1 A:HIS175 3.0 5.5 1.0
C1D A:HEM301 3.0 4.2 1.0
C1C A:HEM301 3.0 4.0 1.0
C4A A:HEM301 3.0 5.7 1.0
C4B A:HEM301 3.0 5.2 1.0
C1B A:HEM301 3.0 4.1 1.0
CD2 A:HIS175 3.0 8.8 1.0
C4D A:HEM301 3.1 5.5 1.0
CHD A:HEM301 3.4 5.3 1.0
CHC A:HEM301 3.4 1.6 1.0
CHA A:HEM301 3.5 5.7 1.0
CHB A:HEM301 3.5 3.7 1.0
NE1 A:TRP51 4.0 4.1 1.0
NE A:ARG48 4.1 7.2 1.0
ND1 A:HIS175 4.1 3.9 1.0
CG A:HIS175 4.2 6.1 1.0
C2A A:HEM301 4.2 5.7 1.0
C2D A:HEM301 4.2 4.9 1.0
C2C A:HEM301 4.2 5.2 1.0
C3A A:HEM301 4.3 5.5 1.0
C2B A:HEM301 4.3 7.5 1.0
C3B A:HEM301 4.3 5.1 1.0
C3D A:HEM301 4.3 8.6 1.0
O A:HOH642 4.3 10.3 1.0
C3C A:HEM301 4.3 5.4 1.0
NH2 A:ARG48 4.6 11.3 1.0
CD1 A:TRP51 4.7 5.6 1.0
CZ A:ARG48 4.8 11.0 1.0
CD A:ARG48 4.9 7.9 1.0
CG A:ARG48 4.9 7.4 1.0

Reference:

A.Gumiero, M.P.Blakeley, C.L.Metcalfe, E.J.Murphy, E.L.Raven, P.C.E.Moody. Hydrogen Bonds in Ferric Cytochrome C Peroxidase: A Combined X-Ray and Neutron Study To Be Published.
Page generated: Sun Aug 4 05:13:05 2024

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