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Iron in PDB 5al9: Structure of Leishmania Major Peroxidase D211R Mutant (High Res)

Enzymatic activity of Structure of Leishmania Major Peroxidase D211R Mutant (High Res)

All present enzymatic activity of Structure of Leishmania Major Peroxidase D211R Mutant (High Res):
1.11.1.5;

Protein crystallography data

The structure of Structure of Leishmania Major Peroxidase D211R Mutant (High Res), PDB code: 5al9 was solved by G.Chreifi, S.A.Hollingsworth, H.Li, S.Tripathi, A.P.Arce, H.I.Magana-Garcia, T.L.Poulos, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 36.511 / 1.37
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 142.439, 57.860, 36.620, 90.00, 97.59, 90.00
R / Rfree (%) 18.48 / 20.37

Other elements in 5al9:

The structure of Structure of Leishmania Major Peroxidase D211R Mutant (High Res) also contains other interesting chemical elements:

Potassium (K) 1 atom
Calcium (Ca) 1 atom

Iron Binding Sites:

The binding sites of Iron atom in the Structure of Leishmania Major Peroxidase D211R Mutant (High Res) (pdb code 5al9). 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 Leishmania Major Peroxidase D211R Mutant (High Res), PDB code: 5al9:

Iron binding site 1 out of 1 in 5al9

Go back to Iron Binding Sites List in 5al9
Iron binding site 1 out of 1 in the Structure of Leishmania Major Peroxidase D211R Mutant (High Res)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Structure of Leishmania Major Peroxidase D211R Mutant (High Res) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe305

b:8.1
occ:1.00
FE A:HEM305 0.0 8.1 1.0
NA A:HEM305 2.0 6.4 1.0
NC A:HEM305 2.0 6.6 1.0
NB A:HEM305 2.1 8.2 1.0
ND A:HEM305 2.1 6.4 1.0
NE2 A:HIS192 2.1 8.9 1.0
O A:HOH2054 2.2 22.9 1.0
C1A A:HEM305 3.0 8.6 1.0
C4A A:HEM305 3.0 7.4 1.0
C4D A:HEM305 3.1 7.2 1.0
C4B A:HEM305 3.1 8.9 1.0
C1D A:HEM305 3.1 6.7 1.0
C1B A:HEM305 3.1 8.7 1.0
C4C A:HEM305 3.1 5.0 1.0
C1C A:HEM305 3.1 7.5 1.0
CE1 A:HIS192 3.1 11.2 1.0
CD2 A:HIS192 3.1 10.3 1.0
CHB A:HEM305 3.4 8.1 1.0
CHA A:HEM305 3.4 8.0 1.0
CHD A:HEM305 3.4 5.9 1.0
CHC A:HEM305 3.4 9.3 1.0
O A:HOH2055 4.2 24.2 1.0
ND1 A:HIS192 4.2 11.3 1.0
NE1 A:TRP67 4.2 12.9 1.0
CG A:HIS192 4.2 7.8 1.0
C2D A:HEM305 4.2 8.6 1.0
C2B A:HEM305 4.3 8.4 1.0
C2A A:HEM305 4.3 10.3 1.0
C3D A:HEM305 4.3 9.4 1.0
C3B A:HEM305 4.3 9.1 1.0
C3A A:HEM305 4.3 11.1 1.0
C3C A:HEM305 4.3 6.9 1.0
C2C A:HEM305 4.3 8.5 1.0
O A:HOH2049 4.5 36.1 1.0
CD1 A:TRP67 4.7 11.5 1.0
CH2 A:TRP208 5.0 12.2 1.0

Reference:

G.Chreifi, S.A.Hollingsworth, H.Li, S.Tripathi, A.P.Arce, H.I.Magana-Garcia, T.L.Poulos. Enzymatic Mechanism of Leishmania Major Peroxidase and the Critical Role of Specific Ionic Interactions. Biochemistry 2015.
ISSN: ESSN 1520-4995
PubMed: 25941976
DOI: 10.1021/ACS.BIOCHEM.5B00338
Page generated: Sun Dec 13 15:56:16 2020

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