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Iron in PDB 5l05: Crystal Structure of Catalase-Peroxidase Katg of Burkholderia Pseudomallei Treated with Inh

Enzymatic activity of Crystal Structure of Catalase-Peroxidase Katg of Burkholderia Pseudomallei Treated with Inh

All present enzymatic activity of Crystal Structure of Catalase-Peroxidase Katg of Burkholderia Pseudomallei Treated with Inh:
1.11.1.21;

Protein crystallography data

The structure of Crystal Structure of Catalase-Peroxidase Katg of Burkholderia Pseudomallei Treated with Inh, PDB code: 5l05 was solved by P.C.Loewen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 18.00 / 1.70
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 100.940, 115.620, 175.200, 90.00, 90.00, 90.00
R / Rfree (%) 14.5 / 17.6

Other elements in 5l05:

The structure of Crystal Structure of Catalase-Peroxidase Katg of Burkholderia Pseudomallei Treated with Inh also contains other interesting chemical elements:

Sodium (Na) 2 atoms

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure of Catalase-Peroxidase Katg of Burkholderia Pseudomallei Treated with Inh (pdb code 5l05). 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 Catalase-Peroxidase Katg of Burkholderia Pseudomallei Treated with Inh, PDB code: 5l05:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in 5l05

Go back to Iron Binding Sites List in 5l05
Iron binding site 1 out of 2 in the Crystal Structure of Catalase-Peroxidase Katg of Burkholderia Pseudomallei Treated with Inh


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 Catalase-Peroxidase Katg of Burkholderia Pseudomallei Treated with Inh within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe801

b:15.1
occ:1.00
FE A:HP5801 0.0 15.1 1.0
NE2 A:HIS279 2.0 14.6 1.0
NC A:HP5801 2.1 14.0 1.0
ND A:HP5801 2.1 14.3 1.0
NB A:HP5801 2.1 16.4 1.0
NA A:HP5801 2.1 15.1 1.0
O A:HOH1241 2.4 33.9 1.0
CHA A:HP5801 2.9 17.3 1.0
CHB A:HP5801 3.0 21.8 1.0
CHC A:HP5801 3.1 17.3 1.0
CE1 A:HIS279 3.1 14.6 1.0
C4C A:HP5801 3.1 14.2 1.0
C1D A:HP5801 3.1 13.6 1.0
CD2 A:HIS279 3.1 13.9 1.0
C1C A:HP5801 3.2 15.0 1.0
C4D A:HP5801 3.2 14.4 1.0
C1A A:HP5801 3.2 16.1 1.0
C4A A:HP5801 3.2 18.6 1.0
C4B A:HP5801 3.2 17.4 1.0
C1B A:HP5801 3.2 17.6 1.0
CHD A:HP5801 3.5 13.7 1.0
ND1 A:HIS279 4.2 16.3 1.0
CG A:HIS279 4.2 15.1 1.0
C2D A:HP5801 4.3 13.8 1.0
C3C A:HP5801 4.3 14.7 1.0
C3D A:HP5801 4.3 13.6 1.0
C2C A:HP5801 4.4 15.4 1.0
C3A A:HP5801 4.4 17.9 1.0
O A:HOH1506 4.4 35.4 1.0
C2A A:HP5801 4.4 16.5 1.0
NE1 A:TRP111 4.4 18.2 1.0
C3B A:HP5801 4.4 18.9 1.0
C2B A:HP5801 4.4 20.1 1.0
O1 A:OXY803 4.5 33.8 1.0
CD1 A:TRP111 4.6 19.1 1.0

Iron binding site 2 out of 2 in 5l05

Go back to Iron Binding Sites List in 5l05
Iron binding site 2 out of 2 in the Crystal Structure of Catalase-Peroxidase Katg of Burkholderia Pseudomallei Treated with Inh


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 Catalase-Peroxidase Katg of Burkholderia Pseudomallei Treated with Inh within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe801

b:14.6
occ:1.00
FE B:HP5801 0.0 14.6 1.0
NC B:HP5801 2.0 13.7 1.0
NA B:HP5801 2.1 13.2 1.0
NE2 B:HIS279 2.1 14.8 1.0
ND B:HP5801 2.1 13.3 1.0
NB B:HP5801 2.1 13.7 1.0
O B:HOH1358 2.5 30.4 1.0
CHC B:HP5801 2.9 15.6 1.0
CHB B:HP5801 3.0 16.9 1.0
CHA B:HP5801 3.0 14.7 1.0
C4C B:HP5801 3.0 13.6 1.0
C1D B:HP5801 3.1 13.2 1.0
CE1 B:HIS279 3.1 14.3 1.0
CD2 B:HIS279 3.1 14.8 1.0
C1C B:HP5801 3.2 13.2 1.0
C1A B:HP5801 3.2 14.3 1.0
C4B B:HP5801 3.2 16.9 1.0
C4A B:HP5801 3.2 15.1 1.0
C1B B:HP5801 3.2 16.9 1.0
C4D B:HP5801 3.3 13.8 1.0
CHD B:HP5801 3.4 12.8 1.0
ND1 B:HIS279 4.2 15.5 1.0
CG B:HIS279 4.2 14.0 1.0
C2D B:HP5801 4.3 13.0 1.0
O B:HOH1472 4.3 33.2 1.0
C3C B:HP5801 4.3 13.1 1.0
C3A B:HP5801 4.3 14.3 1.0
C2A B:HP5801 4.4 13.5 1.0
C3D B:HP5801 4.4 13.5 1.0
NE1 B:TRP111 4.4 15.1 1.0
C3B B:HP5801 4.4 18.5 1.0
C2B B:HP5801 4.4 17.1 1.0
C2C B:HP5801 4.4 13.5 1.0
CD1 B:TRP111 4.6 16.0 1.0
O1 B:OXY803 4.6 31.8 1.0

Reference:

X.Carpena, S.Loprasert, S.Mongkolsuk, J.Switala, P.C.Loewen, I.Fita. Catalase-Peroxidase Katg of Burkholderia Pseudomallei at 1.7A Resolution. J. Mol. Biol. V. 327 475 2003.
ISSN: ISSN 0022-2836
PubMed: 12628252
Page generated: Tue Aug 6 04:01:16 2024

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