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Iron in PDB 5ala: Structure of Leishmania Major Peroxidase D211R Mutant (Low Res)

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

All present enzymatic activity of Structure of Leishmania Major Peroxidase D211R Mutant (Low Res):
1.11.1.11; 1.11.1.5;

Protein crystallography data

The structure of Structure of Leishmania Major Peroxidase D211R Mutant (Low Res), PDB code: 5ala 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) 40.837 / 2.73
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 45.880, 79.170, 179.190, 90.00, 90.00, 90.00
R / Rfree (%) 20.92 / 28.23

Other elements in 5ala:

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

Potassium (K) 2 atoms
Calcium (Ca) 1 atom

Iron Binding Sites:

The binding sites of Iron atom in the Structure of Leishmania Major Peroxidase D211R Mutant (Low Res) (pdb code 5ala). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Structure of Leishmania Major Peroxidase D211R Mutant (Low Res), PDB code: 5ala:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in 5ala

Go back to Iron Binding Sites List in 5ala
Iron binding site 1 out of 2 in the Structure of Leishmania Major Peroxidase D211R Mutant (Low 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 (Low Res) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe305

b:28.6
occ:1.00
FE A:HEM305 0.0 28.6 1.0
NE2 A:HIS192 2.0 24.1 1.0
NB A:HEM305 2.0 28.6 1.0
NA A:HEM305 2.1 28.6 1.0
NC A:HEM305 2.1 28.6 1.0
O A:HOH2004 2.1 0.9 1.0
ND A:HEM305 2.2 28.6 1.0
CE1 A:HIS192 3.0 23.4 1.0
CD2 A:HIS192 3.0 24.9 1.0
C1B A:HEM305 3.0 28.6 1.0
C4A A:HEM305 3.0 28.6 1.0
C4B A:HEM305 3.1 28.6 1.0
C4C A:HEM305 3.1 28.6 1.0
C1D A:HEM305 3.1 28.6 1.0
C1A A:HEM305 3.1 28.6 1.0
C1C A:HEM305 3.1 28.6 1.0
C4D A:HEM305 3.2 28.6 1.0
CHB A:HEM305 3.4 28.6 1.0
CHD A:HEM305 3.4 28.6 1.0
CHC A:HEM305 3.5 28.6 1.0
CHA A:HEM305 3.5 28.6 1.0
ND1 A:HIS192 4.1 23.7 1.0
NE1 A:TRP67 4.1 35.9 1.0
CG A:HIS192 4.1 24.7 1.0
C2B A:HEM305 4.3 28.6 1.0
C3B A:HEM305 4.3 28.6 1.0
C3A A:HEM305 4.3 28.6 1.0
C2A A:HEM305 4.3 28.6 1.0
O A:HOH2005 4.3 20.7 1.0
C3C A:HEM305 4.3 28.6 1.0
C2D A:HEM305 4.3 28.6 1.0
C2C A:HEM305 4.3 28.6 1.0
C3D A:HEM305 4.4 28.6 1.0
CD1 A:TRP67 4.8 38.7 1.0
CH2 A:TRP208 5.0 26.0 1.0

Iron binding site 2 out of 2 in 5ala

Go back to Iron Binding Sites List in 5ala
Iron binding site 2 out of 2 in the Structure of Leishmania Major Peroxidase D211R Mutant (Low Res)


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Structure of Leishmania Major Peroxidase D211R Mutant (Low Res) within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe305

b:24.7
occ:1.00
FE B:HEM305 0.0 24.7 1.0
NE2 B:HIS192 2.0 30.2 1.0
NC B:HEM305 2.0 24.7 1.0
ND B:HEM305 2.0 24.7 1.0
NA B:HEM305 2.0 24.7 1.0
NB B:HEM305 2.1 24.7 1.0
O B:HOH2011 2.2 23.7 1.0
CE1 B:HIS192 2.9 30.0 1.0
C4D B:HEM305 3.0 24.7 1.0
C4C B:HEM305 3.0 24.7 1.0
C1A B:HEM305 3.0 24.7 1.0
C1D B:HEM305 3.0 24.7 1.0
CD2 B:HIS192 3.0 30.2 1.0
C1C B:HEM305 3.0 24.7 1.0
C4A B:HEM305 3.1 24.7 1.0
C4B B:HEM305 3.1 24.7 1.0
C1B B:HEM305 3.2 24.7 1.0
CHA B:HEM305 3.3 24.7 1.0
CHD B:HEM305 3.4 24.7 1.0
CHC B:HEM305 3.5 24.7 1.0
CHB B:HEM305 3.6 24.7 1.0
ND1 B:HIS192 4.0 29.9 1.0
CG B:HIS192 4.1 29.9 1.0
C3D B:HEM305 4.2 24.7 1.0
C2D B:HEM305 4.2 24.7 1.0
C3C B:HEM305 4.2 24.7 1.0
C2A B:HEM305 4.2 24.7 1.0
C2C B:HEM305 4.2 24.7 1.0
NE1 B:TRP67 4.3 31.6 1.0
C3A B:HEM305 4.3 24.7 1.0
C3B B:HEM305 4.4 24.7 1.0
C2B B:HEM305 4.4 24.7 1.0
CD1 B:TRP67 4.9 31.9 1.0
CH2 B:TRP208 4.9 32.5 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: Mon Aug 5 19:38:34 2024

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