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Iron in PDB 3wnu: The Crystal Structure of Catalase-Peroxidase, Katg, From Synechococcus PCC7942

Enzymatic activity of The Crystal Structure of Catalase-Peroxidase, Katg, From Synechococcus PCC7942

All present enzymatic activity of The Crystal Structure of Catalase-Peroxidase, Katg, From Synechococcus PCC7942:
1.11.1.21;

Protein crystallography data

The structure of The Crystal Structure of Catalase-Peroxidase, Katg, From Synechococcus PCC7942, PDB code: 3wnu was solved by T.Tada, K.Wada, S.Kamachi, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 34.39 / 2.20
Space group P 41 21 2
Cell size a, b, c (Å), α, β, γ (°) 108.744, 108.744, 202.888, 90.00, 90.00, 90.00
R / Rfree (%) 16.8 / 20.6

Other elements in 3wnu:

The structure of The Crystal Structure of Catalase-Peroxidase, Katg, From Synechococcus PCC7942 also contains other interesting chemical elements:

Sodium (Na) 2 atoms

Iron Binding Sites:

The binding sites of Iron atom in the The Crystal Structure of Catalase-Peroxidase, Katg, From Synechococcus PCC7942 (pdb code 3wnu). 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 The Crystal Structure of Catalase-Peroxidase, Katg, From Synechococcus PCC7942, PDB code: 3wnu:

Iron binding site 1 out of 1 in 3wnu

Go back to Iron Binding Sites List in 3wnu
Iron binding site 1 out of 1 in the The Crystal Structure of Catalase-Peroxidase, Katg, From Synechococcus PCC7942


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of The Crystal Structure of Catalase-Peroxidase, Katg, From Synechococcus PCC7942 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe801

b:28.5
occ:1.00
 FE A:HEB801 0.0 28.5 1.0
ND A:HEB801 1.9 24.9 1.0
NA A:HEB801 2.0 26.4 1.0
NB A:HEB801 2.0 25.4 1.0
NC A:HEB801 2.0 25.3 1.0
NE2 A:HIS263 2.2 32.3 1.0
C1D A:HEB801 2.9 26.5 1.0
C1B A:HEB801 2.9 29.8 1.0
C4C A:HEB801 3.0 23.3 1.0
C4A A:HEB801 3.0 28.4 1.0
C4D A:HEB801 3.0 26.3 1.0
C4B A:HEB801 3.0 28.5 1.0
C1A A:HEB801 3.1 27.4 1.0
C1C A:HEB801 3.1 27.5 1.0
CE1 A:HIS263 3.1 29.7 1.0
CD2 A:HIS263 3.2 28.1 1.0
CHD A:HEB801 3.3 24.5 1.0
CHB A:HEB801 3.3 30.0 1.0
CHA A:HEB801 3.5 29.0 1.0
CHC A:HEB801 3.5 26.3 1.0
C2B A:HEB801 4.2 31.9 1.0
C3A A:HEB801 4.2 26.4 1.0
C2D A:HEB801 4.2 25.6 1.0
C3B A:HEB801 4.2 24.8 1.0
C3C A:HEB801 4.2 22.9 1.0
C2A A:HEB801 4.3 29.7 1.0
C3D A:HEB801 4.3 23.4 1.0
NE1 A:TRP94 4.3 26.4 1.0
C2C A:HEB801 4.3 23.1 1.0
ND1 A:HIS263 4.3 27.6 1.0
CG A:HIS263 4.3 28.0 1.0
CD1 A:TRP94 4.6 26.7 1.0
CH2 A:TRP314 4.8 31.6 1.0
CZ2 A:TRP314 4.8 31.5 1.0

Reference:

S.Kamachi, K.Wada, M.Tamoi, S.Shigeoka, T.Tada. The 2.2 Aa Resolution Structure of the Catalase-Peroxidase Katg From Synechococcus Elongatus PCC7942. Acta Crystallogr.,Sect.F V. 70 288 2014.
ISSN: ESSN 1744-3091
DOI: 10.1107/S2053230X14002052
Page generated: Sun Aug 4 22:43:01 2024

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