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Iron in PDB 2ylj: Horse Radish Peroxidase, Mutant S167Y

Enzymatic activity of Horse Radish Peroxidase, Mutant S167Y

All present enzymatic activity of Horse Radish Peroxidase, Mutant S167Y:
1.11.1.7;

Protein crystallography data

The structure of Horse Radish Peroxidase, Mutant S167Y, PDB code: 2ylj was solved by S.M.Roe, F.S.Al-Fartusie, A.T.Smith, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 44.336 / 1.69
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 40.400, 67.370, 117.770, 90.00, 90.00, 90.00
R / Rfree (%) 15.24 / 18.88

Other elements in 2ylj:

The structure of Horse Radish Peroxidase, Mutant S167Y also contains other interesting chemical elements:

Calcium (Ca) 2 atoms

Iron Binding Sites:

The binding sites of Iron atom in the Horse Radish Peroxidase, Mutant S167Y (pdb code 2ylj). 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 Horse Radish Peroxidase, Mutant S167Y, PDB code: 2ylj:

Iron binding site 1 out of 1 in 2ylj

Go back to Iron Binding Sites List in 2ylj
Iron binding site 1 out of 1 in the Horse Radish Peroxidase, Mutant S167Y


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Horse Radish Peroxidase, Mutant S167Y within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe350

b:9.8
occ:1.00
FE A:HEM350 0.0 9.8 1.0
NB A:HEM350 2.1 8.8 0.3
ND A:HEM350 2.1 9.3 0.7
NA A:HEM350 2.1 10.7 0.7
NC A:HEM350 2.1 8.6 0.3
NC A:HEM350 2.1 8.5 0.7
NB A:HEM350 2.1 8.6 0.7
NE2 A:HIS170 2.1 10.0 1.0
NA A:HEM350 2.1 10.6 0.3
ND A:HEM350 2.2 9.3 0.3
O A:HOH2090 2.8 21.1 1.0
C4A A:HEM350 3.0 10.7 0.7
C1D A:HEM350 3.0 9.3 0.7
C4B A:HEM350 3.1 11.7 0.3
C1B A:HEM350 3.1 9.8 0.3
C4C A:HEM350 3.1 8.3 0.7
C1B A:HEM350 3.1 9.6 0.7
CE1 A:HIS170 3.1 12.0 1.0
C4C A:HEM350 3.1 8.3 0.3
C1D A:HEM350 3.1 9.3 0.3
C1C A:HEM350 3.1 9.9 0.3
C4A A:HEM350 3.1 10.8 0.3
CD2 A:HIS170 3.1 9.2 1.0
C4D A:HEM350 3.1 9.8 0.7
C1A A:HEM350 3.1 10.1 0.7
C1C A:HEM350 3.1 9.9 0.7
C4B A:HEM350 3.1 11.8 0.7
C4D A:HEM350 3.2 9.7 0.3
C1A A:HEM350 3.2 10.1 0.3
CHB A:HEM350 3.4 12.3 0.7
CHD A:HEM350 3.4 8.1 0.7
CHC A:HEM350 3.4 9.9 0.3
CHB A:HEM350 3.4 12.3 0.3
CHD A:HEM350 3.4 8.1 0.3
CHA A:HEM350 3.5 10.1 0.7
CHC A:HEM350 3.5 9.9 0.7
CHA A:HEM350 3.6 9.9 0.3
O A:ACT1309 4.0 20.6 1.0
ND1 A:HIS170 4.2 8.6 1.0
CG A:HIS170 4.2 9.0 1.0
C2D A:HEM350 4.2 8.8 0.7
C3B A:HEM350 4.3 10.6 0.3
C2B A:HEM350 4.3 11.4 0.3
C3A A:HEM350 4.3 10.1 0.7
C3D A:HEM350 4.3 8.9 0.7
C2A A:HEM350 4.3 8.9 0.7
C2C A:HEM350 4.3 8.6 0.3
C3C A:HEM350 4.3 8.8 0.3
C2D A:HEM350 4.3 8.8 0.3
C2B A:HEM350 4.3 11.4 0.7
C2C A:HEM350 4.3 8.8 0.7
C3C A:HEM350 4.3 8.8 0.7
C3A A:HEM350 4.3 10.2 0.3
C3B A:HEM350 4.3 10.6 0.7
C3D A:HEM350 4.3 9.1 0.3
C2A A:HEM350 4.4 9.2 0.3
CE2 A:PHE41 4.5 10.8 1.0
NE A:ARG38 4.5 9.3 1.0
CZ A:PHE221 4.6 9.5 1.0
H1 A:ACT1309 4.7 22.8 1.0
C A:ACT1309 4.8 25.4 1.0
CD2 A:PHE41 4.9 9.6 1.0
CD A:ARG38 4.9 9.2 1.0

Reference:

U.Sussex, S.M.Roe, F.S.Al-Fartusie, A.T.Smith. N/A N/A.
Page generated: Thu Jul 17 06:14:21 2025

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