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Iron in PDB 1e93: High Resolution Structure and Biochemical Properties of A Recombinant Catalase Depleted in Iron

Enzymatic activity of High Resolution Structure and Biochemical Properties of A Recombinant Catalase Depleted in Iron

All present enzymatic activity of High Resolution Structure and Biochemical Properties of A Recombinant Catalase Depleted in Iron:
1.11.1.6;

Protein crystallography data

The structure of High Resolution Structure and Biochemical Properties of A Recombinant Catalase Depleted in Iron, PDB code: 1e93 was solved by P.Andreoletti, G.Sainz, M.Jaquinod, J.Gagnon, H.M.Jouve, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 14.95 / 2.00
Space group P 62 2 2
Cell size a, b, c (Å), α, β, γ (°) 108.572, 108.572, 248.760, 90.00, 90.00, 120.00
R / Rfree (%) 19.9 / 21.5

Iron Binding Sites:

The binding sites of Iron atom in the High Resolution Structure and Biochemical Properties of A Recombinant Catalase Depleted in Iron (pdb code 1e93). 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 High Resolution Structure and Biochemical Properties of A Recombinant Catalase Depleted in Iron, PDB code: 1e93:

Iron binding site 1 out of 1 in 1e93

Go back to Iron Binding Sites List in 1e93
Iron binding site 1 out of 1 in the High Resolution Structure and Biochemical Properties of A Recombinant Catalase Depleted in Iron


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of High Resolution Structure and Biochemical Properties of A Recombinant Catalase Depleted in Iron within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe600

b:20.1
occ:0.60
 FE A:HEM600 0.0 20.1 0.6
ND A:HEM600 2.0 18.9 1.0
NB A:HEM600 2.0 19.4 1.0
OH A:TYR337 2.0 19.2 1.0
NC A:HEM600 2.0 19.1 1.0
NA A:HEM600 2.0 19.1 1.0
O A:HOH2609 2.6 43.8 1.0
CZ A:TYR337 3.0 19.2 1.0
C4D A:HEM600 3.0 19.0 1.0
C1D A:HEM600 3.0 18.8 1.0
C1B A:HEM600 3.0 19.4 1.0
C1A A:HEM600 3.0 18.9 1.0
C1C A:HEM600 3.0 19.4 1.0
C4B A:HEM600 3.1 19.9 1.0
C4A A:HEM600 3.1 19.2 1.0
C4C A:HEM600 3.1 19.2 1.0
CHA A:HEM600 3.4 18.7 1.0
CHD A:HEM600 3.4 18.9 1.0
CHB A:HEM600 3.4 19.6 1.0
CHC A:HEM600 3.4 20.0 1.0
CE2 A:TYR337 3.7 18.6 1.0
CE1 A:TYR337 3.8 19.0 1.0
NE A:ARG333 4.2 18.4 1.0
NH2 A:ARG333 4.2 18.2 1.0
C3D A:HEM600 4.2 18.6 1.0
C2D A:HEM600 4.2 18.6 1.0
C2B A:HEM600 4.2 19.5 1.0
C3C A:HEM600 4.3 18.9 1.0
C3B A:HEM600 4.3 19.9 1.0
C2A A:HEM600 4.3 19.2 1.0
C3A A:HEM600 4.3 19.5 1.0
C2C A:HEM600 4.3 19.5 1.0
CZ A:PHE140 4.3 21.2 1.0
CZ A:ARG333 4.6 19.1 1.0
NE2 A:HIS54 4.6 19.0 1.0
CD2 A:HIS54 4.7 19.4 1.0
O A:HOH2194 4.8 52.7 1.0
CE1 A:PHE140 4.9 20.7 1.0
CD2 A:TYR337 5.0 19.0 1.0
CE2 A:PHE140 5.0 20.4 1.0

Reference:

P.Andreoletti, G.Sainz, M.Jaquinod, J.Gagnon, H.M.Jouve. High-Resolution Structure and Biochemical Properties of A Recombinant Proteus Mirabilis Catalase Depleted in Iron. Proteins: Struct.,Funct., V. 50 261 2003GENET..
ISSN: ISSN 0887-3585
PubMed: 12486720
DOI: 10.1002/PROT.10283
Page generated: Wed Jul 16 13:40:14 2025

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