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Iron in PDB 1sj2: Crystal Structure of Mycobacterium Tuberculosis Catalase-Peroxidase

Enzymatic activity of Crystal Structure of Mycobacterium Tuberculosis Catalase-Peroxidase

All present enzymatic activity of Crystal Structure of Mycobacterium Tuberculosis Catalase-Peroxidase:
1.11.1.6;

Protein crystallography data

The structure of Crystal Structure of Mycobacterium Tuberculosis Catalase-Peroxidase, PDB code: 1sj2 was solved by T.Bertrand, N.A.J.Eady, J.N.Jones, J.Bodiguel, Jesmin, J.M.Nagy, E.L.Raven, B.Jamart-Gregoire, K.A.Brown, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 23.71 / 2.41
Space group P 42 21 2
Cell size a, b, c (Å), α, β, γ (°) 150.330, 150.330, 154.281, 90.00, 90.00, 90.00
R / Rfree (%) 21.1 / 26.8

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure of Mycobacterium Tuberculosis Catalase-Peroxidase (pdb code 1sj2). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Crystal Structure of Mycobacterium Tuberculosis Catalase-Peroxidase, PDB code: 1sj2:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in 1sj2

Go back to Iron Binding Sites List in 1sj2
Iron binding site 1 out of 2 in the Crystal Structure of Mycobacterium Tuberculosis Catalase-Peroxidase


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 Mycobacterium Tuberculosis Catalase-Peroxidase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe1500

b:32.8
occ:1.00
FE A:HEM1500 0.0 32.8 1.0
ND A:HEM1500 2.0 28.9 1.0
NA A:HEM1500 2.0 29.0 1.0
NC A:HEM1500 2.1 28.1 1.0
NB A:HEM1500 2.1 28.4 1.0
NE2 A:HIS270 2.5 27.6 1.0
C1D A:HEM1500 3.0 28.6 1.0
C1A A:HEM1500 3.1 29.5 1.0
C4D A:HEM1500 3.1 29.4 1.0
C4C A:HEM1500 3.1 28.6 1.0
C4A A:HEM1500 3.1 30.6 1.0
C1C A:HEM1500 3.1 29.1 1.0
C4B A:HEM1500 3.1 27.0 1.0
C1B A:HEM1500 3.1 27.3 1.0
CD2 A:HIS270 3.3 27.6 1.0
CHD A:HEM1500 3.4 28.0 1.0
CHA A:HEM1500 3.4 27.8 1.0
CHC A:HEM1500 3.4 25.8 1.0
CHB A:HEM1500 3.5 29.7 1.0
CE1 A:HIS270 3.6 28.0 1.0
O A:HOH1733 4.2 52.1 1.0
C2D A:HEM1500 4.3 29.2 1.0
C3D A:HEM1500 4.3 29.7 1.0
C2A A:HEM1500 4.3 29.8 1.0
C3A A:HEM1500 4.3 29.4 1.0
C2C A:HEM1500 4.3 28.7 1.0
C3B A:HEM1500 4.3 25.7 1.0
C3C A:HEM1500 4.3 27.6 1.0
C2B A:HEM1500 4.4 26.7 1.0
NE1 A:TRP107 4.4 30.5 1.0
CG A:HIS270 4.5 28.8 1.0
CD1 A:TRP107 4.5 29.2 1.0
ND1 A:HIS270 4.6 26.3 1.0
CH2 A:TRP321 4.9 26.4 1.0

Iron binding site 2 out of 2 in 1sj2

Go back to Iron Binding Sites List in 1sj2
Iron binding site 2 out of 2 in the Crystal Structure of Mycobacterium Tuberculosis Catalase-Peroxidase


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Crystal Structure of Mycobacterium Tuberculosis Catalase-Peroxidase within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe1500

b:34.0
occ:1.00
FE B:HEM1500 0.0 34.0 1.0
ND B:HEM1500 2.0 31.6 1.0
NA B:HEM1500 2.1 32.2 1.0
NC B:HEM1500 2.1 32.1 1.0
NB B:HEM1500 2.1 32.4 1.0
NE2 B:HIS270 2.5 41.3 1.0
C1D B:HEM1500 3.0 30.6 1.0
C4C B:HEM1500 3.0 32.9 1.0
C4D B:HEM1500 3.1 31.6 1.0
C1C B:HEM1500 3.1 32.7 1.0
C1A B:HEM1500 3.1 34.1 1.0
C4B B:HEM1500 3.1 30.4 1.0
C4A B:HEM1500 3.1 33.1 1.0
C1B B:HEM1500 3.1 31.7 1.0
CD2 B:HIS270 3.2 39.2 1.0
CHD B:HEM1500 3.4 31.1 1.0
CHA B:HEM1500 3.4 31.4 1.0
CHC B:HEM1500 3.4 31.1 1.0
CHB B:HEM1500 3.5 31.1 1.0
CE1 B:HIS270 3.6 40.1 1.0
O B:HOH2234 4.1 34.5 1.0
C2D B:HEM1500 4.3 32.0 1.0
C3D B:HEM1500 4.3 32.6 1.0
C3C B:HEM1500 4.3 32.7 1.0
C2C B:HEM1500 4.3 33.6 1.0
C3B B:HEM1500 4.3 31.3 1.0
C2A B:HEM1500 4.3 33.1 1.0
C3A B:HEM1500 4.3 33.0 1.0
C2B B:HEM1500 4.4 31.1 1.0
NE1 B:TRP107 4.4 25.7 1.0
CG B:HIS270 4.5 38.8 1.0
ND1 B:HIS270 4.6 40.3 1.0
CD1 B:TRP107 4.7 24.2 1.0
CH2 B:TRP321 4.8 26.4 1.0

Reference:

T.Bertrand, N.A.J.Eady, J.N.Jones, Jesmin, J.M.Nagy, B.Jamart-Gregoire, E.L.Raven, K.A.Brown. Crystal Structure of Mycobacterium Tuberculosis Catalase-Peroxidase. J.Biol.Chem. V. 279 38991 2004.
ISSN: ISSN 0021-9258
PubMed: 15231843
DOI: 10.1074/JBC.M402382200
Page generated: Wed Jul 16 20:40:27 2025

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