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Iron in PDB 7s10: Crystal Structure of Ascorbate Peroxidase Triple Mutant: S160M, L203M, Q204M

Enzymatic activity of Crystal Structure of Ascorbate Peroxidase Triple Mutant: S160M, L203M, Q204M

All present enzymatic activity of Crystal Structure of Ascorbate Peroxidase Triple Mutant: S160M, L203M, Q204M:
1.11.1.11;

Protein crystallography data

The structure of Crystal Structure of Ascorbate Peroxidase Triple Mutant: S160M, L203M, Q204M, PDB code: 7s10 was solved by T.L.Poulos, J.Kim, V.Murarka, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 36.23 / 1.40
Space group P 42 21 2
Cell size a, b, c (Å), α, β, γ (°) 82.644, 82.644, 75.322, 90, 90, 90
R / Rfree (%) 17.1 / 20.8

Other elements in 7s10:

The structure of Crystal Structure of Ascorbate Peroxidase Triple Mutant: S160M, L203M, Q204M also contains other interesting chemical elements:

Potassium (K) 1 atom

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure of Ascorbate Peroxidase Triple Mutant: S160M, L203M, Q204M (pdb code 7s10). 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 Ascorbate Peroxidase Triple Mutant: S160M, L203M, Q204M, PDB code: 7s10:

Iron binding site 1 out of 1 in 7s10

Go back to Iron Binding Sites List in 7s10
Iron binding site 1 out of 1 in the Crystal Structure of Ascorbate Peroxidase Triple Mutant: S160M, L203M, Q204M


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 Ascorbate Peroxidase Triple Mutant: S160M, L203M, Q204M within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe301

b:16.9
occ:1.00
 FE A:HEM301 0.0 16.9 1.0
NA A:HEM301 2.0 17.8 1.0
NC A:HEM301 2.0 17.9 1.0
NB A:HEM301 2.0 17.4 1.0
ND A:HEM301 2.0 15.4 1.0
O A:HOH437 2.1 28.3 1.0
NE2 A:HIS163 2.2 16.3 1.0
C1C A:HEM301 3.0 18.7 1.0
C1B A:HEM301 3.1 18.2 1.0
C1D A:HEM301 3.1 16.2 1.0
C4A A:HEM301 3.1 19.2 1.0
C1A A:HEM301 3.1 18.5 1.0
C4C A:HEM301 3.1 14.6 1.0
C4D A:HEM301 3.1 16.4 1.0
CD2 A:HIS163 3.1 15.4 1.0
C4B A:HEM301 3.1 17.1 1.0
CE1 A:HIS163 3.2 17.8 1.0
CHD A:HEM301 3.4 14.6 1.0
CHC A:HEM301 3.4 16.5 1.0
CHB A:HEM301 3.4 19.5 1.0
CHA A:HEM301 3.4 17.2 1.0
NE1 A:TRP41 4.0 29.5 0.4
NE1 A:TRP41 4.1 14.5 0.6
CG A:HIS163 4.2 17.7 1.0
O A:HOH585 4.2 25.9 1.0
C2D A:HEM301 4.2 14.9 1.0
C2B A:HEM301 4.3 18.5 1.0
ND1 A:HIS163 4.3 18.8 1.0
C3A A:HEM301 4.3 15.2 1.0
C2C A:HEM301 4.3 15.0 1.0
C2A A:HEM301 4.3 17.7 1.0
C3D A:HEM301 4.3 15.2 1.0
C3C A:HEM301 4.3 14.2 1.0
C3B A:HEM301 4.3 20.0 1.0
O A:HOH582 4.3 25.3 1.0
CD1 A:TRP41 4.6 14.9 0.6
CD1 A:TRP41 4.6 25.9 0.4
CH2 A:TRP179 4.9 19.0 1.0
CE2 A:TRP41 5.0 21.3 0.4

Reference:

T.L.Poulos, J.S.Kim, V.C.Murarka. Computational Analysis of the Tryptophan Cation Radical Energetics in Peroxidase Compound I. J.Biol.Inorg.Chem. V. 27 229 2022.
ISSN: ESSN 1432-1327
PubMed: 35064363
DOI: 10.1007/S00775-022-01925-8
Page generated: Fri Aug 9 00:17:03 2024

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