Iron in PDB 1iph: Structure of Catalase Hpii From Escherichia Coli

All present enzymatic activity of Structure of Catalase Hpii From Escherichia Coli:
1.11.1.6;

The structure of Structure of Catalase Hpii From Escherichia Coli, PDB code: 1iph was solved by J.Bravo, P.C.Loewen, I.Fita, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	N/A / 2.80
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	95.200, 134.700, 124.400, 90.00, 109.40, 90.00
R / Rfree (%)	20 / n/a

The binding sites of Iron atom in the Structure of Catalase Hpii From Escherichia Coli (pdb code 1iph). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 4 binding sites of Iron where determined in the Structure of Catalase Hpii From Escherichia Coli, PDB code: 1iph:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in the Structure of Catalase Hpii From Escherichia Coli


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Structure of Catalase Hpii From Escherichia Coli within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe754 b:2.0 occ:1.00 FE A:HEM754 0.0 2.0 1.0 NB A:HEM754 2.0 3.1 1.0 ND A:HEM754 2.0 4.0 1.0 NC A:HEM754 2.0 3.0 1.0 NA A:HEM754 2.0 2.7 1.0 OH A:TYR415 2.0 2.0 1.0 C4B A:HEM754 3.0 2.0 1.0 C1B A:HEM754 3.0 2.8 1.0 C1D A:HEM754 3.0 3.2 1.0 C4C A:HEM754 3.0 2.0 1.0 C4A A:HEM754 3.1 2.0 1.0 C4D A:HEM754 3.1 4.0 1.0 C1C A:HEM754 3.1 2.0 1.0 C1A A:HEM754 3.1 2.2 1.0 CZ A:TYR415 3.2 2.0 1.0 CHB A:HEM754 3.4 2.0 1.0 CHC A:HEM754 3.4 2.0 1.0 CHD A:HEM754 3.4 2.0 1.0 CHA A:HEM754 3.5 2.0 1.0 CE2 A:TYR415 3.9 2.0 1.0 CE1 A:TYR415 4.1 2.0 1.0 C3D A:HEM754 4.2 5.7 1.0 C3C A:HEM754 4.3 2.0 1.0 C3B A:HEM754 4.3 3.2 1.0 C2D A:HEM754 4.3 4.5 1.0 NE A:ARG411 4.3 2.0 1.0 C2B A:HEM754 4.3 2.0 1.0 C2C A:HEM754 4.3 2.0 1.0 C3A A:HEM754 4.3 2.0 1.0 NH2 A:ARG411 4.3 2.0 1.0 C2A A:HEM754 4.3 2.0 1.0 CZ A:ARG411 4.6 2.0 1.0 CD2 A:HIS128 4.7 2.0 1.0 CG2 A:VAL127 4.7 2.6 1.0 CZ A:PHE214 4.7 2.0 1.0 NE2 A:HIS128 4.7 2.9 1.0

Iron binding site 2 out of 4 in the Structure of Catalase Hpii From Escherichia Coli


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Structure of Catalase Hpii From Escherichia Coli within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe754 b:2.0 occ:1.00 FE B:HEM754 0.0 2.0 1.0 NB B:HEM754 2.0 3.1 1.0 ND B:HEM754 2.0 4.0 1.0 NC B:HEM754 2.0 3.0 1.0 NA B:HEM754 2.0 2.7 1.0 OH B:TYR415 2.0 2.0 1.0 C4B B:HEM754 3.0 2.0 1.0 C1B B:HEM754 3.0 2.8 1.0 C1D B:HEM754 3.0 3.2 1.0 C4C B:HEM754 3.0 2.0 1.0 C4A B:HEM754 3.1 2.0 1.0 C4D B:HEM754 3.1 4.0 1.0 C1C B:HEM754 3.1 2.0 1.0 C1A B:HEM754 3.1 2.2 1.0 CZ B:TYR415 3.2 2.0 1.0 CHB B:HEM754 3.4 2.0 1.0 CHC B:HEM754 3.4 2.0 1.0 CHD B:HEM754 3.4 2.0 1.0 CHA B:HEM754 3.5 2.0 1.0 CE2 B:TYR415 3.9 2.0 1.0 CE1 B:TYR415 4.1 2.0 1.0 C3D B:HEM754 4.2 5.7 1.0 C3C B:HEM754 4.3 2.0 1.0 C3B B:HEM754 4.3 3.2 1.0 C2D B:HEM754 4.3 4.5 1.0 NE B:ARG411 4.3 2.0 1.0 C2B B:HEM754 4.3 2.0 1.0 C2C B:HEM754 4.3 2.0 1.0 C3A B:HEM754 4.3 2.0 1.0 NH2 B:ARG411 4.3 2.0 1.0 C2A B:HEM754 4.3 2.0 1.0 CZ B:ARG411 4.6 2.0 1.0 CD2 B:HIS128 4.7 2.0 1.0 CG2 B:VAL127 4.7 2.6 1.0 CZ B:PHE214 4.7 2.0 1.0 NE2 B:HIS128 4.7 2.9 1.0

Iron binding site 3 out of 4 in the Structure of Catalase Hpii From Escherichia Coli


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Structure of Catalase Hpii From Escherichia Coli within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe754 b:2.0 occ:1.00 FE C:HEM754 0.0 2.0 1.0 NB C:HEM754 2.0 3.1 1.0 ND C:HEM754 2.0 4.0 1.0 NC C:HEM754 2.0 3.0 1.0 NA C:HEM754 2.0 2.7 1.0 OH C:TYR415 2.0 2.0 1.0 C4B C:HEM754 3.0 2.0 1.0 C1B C:HEM754 3.0 2.8 1.0 C1D C:HEM754 3.0 3.2 1.0 C4C C:HEM754 3.0 2.0 1.0 C4A C:HEM754 3.1 2.0 1.0 C4D C:HEM754 3.1 4.0 1.0 C1C C:HEM754 3.1 2.0 1.0 C1A C:HEM754 3.1 2.2 1.0 CZ C:TYR415 3.2 2.0 1.0 CHB C:HEM754 3.4 2.0 1.0 CHC C:HEM754 3.4 2.0 1.0 CHD C:HEM754 3.4 2.0 1.0 CHA C:HEM754 3.5 2.0 1.0 CE2 C:TYR415 3.9 2.0 1.0 CE1 C:TYR415 4.1 2.0 1.0 C3D C:HEM754 4.2 5.7 1.0 C3C C:HEM754 4.3 2.0 1.0 C3B C:HEM754 4.3 3.2 1.0 C2D C:HEM754 4.3 4.5 1.0 NE C:ARG411 4.3 2.0 1.0 C2B C:HEM754 4.3 2.0 1.0 C2C C:HEM754 4.3 2.0 1.0 C3A C:HEM754 4.3 2.0 1.0 NH2 C:ARG411 4.3 2.0 1.0 C2A C:HEM754 4.3 2.0 1.0 CZ C:ARG411 4.6 2.0 1.0 CD2 C:HIS128 4.7 2.0 1.0 CG2 C:VAL127 4.7 2.6 1.0 CZ C:PHE214 4.7 2.0 1.0 NE2 C:HIS128 4.7 2.9 1.0

Iron binding site 4 out of 4 in the Structure of Catalase Hpii From Escherichia Coli


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Structure of Catalase Hpii From Escherichia Coli within 5.0Å range: probe atom residue distance (Å) B Occ D:Fe754 b:2.0 occ:1.00 FE D:HEM754 0.0 2.0 1.0 NB D:HEM754 2.0 3.1 1.0 ND D:HEM754 2.0 4.0 1.0 NC D:HEM754 2.0 3.0 1.0 NA D:HEM754 2.0 2.7 1.0 OH D:TYR415 2.0 2.0 1.0 C4B D:HEM754 3.0 2.0 1.0 C1B D:HEM754 3.0 2.8 1.0 C1D D:HEM754 3.0 3.2 1.0 C4C D:HEM754 3.0 2.0 1.0 C4A D:HEM754 3.1 2.0 1.0 C4D D:HEM754 3.1 4.0 1.0 C1C D:HEM754 3.1 2.0 1.0 C1A D:HEM754 3.1 2.2 1.0 CZ D:TYR415 3.2 2.0 1.0 CHB D:HEM754 3.4 2.0 1.0 CHC D:HEM754 3.4 2.0 1.0 CHD D:HEM754 3.4 2.0 1.0 CHA D:HEM754 3.5 2.0 1.0 CE2 D:TYR415 3.9 2.0 1.0 CE1 D:TYR415 4.1 2.0 1.0 C3D D:HEM754 4.2 5.7 1.0 C3C D:HEM754 4.3 2.0 1.0 C3B D:HEM754 4.3 3.2 1.0 C2D D:HEM754 4.3 4.5 1.0 NE D:ARG411 4.3 2.0 1.0 C2B D:HEM754 4.3 2.0 1.0 C2C D:HEM754 4.3 2.0 1.0 C3A D:HEM754 4.3 2.0 1.0 NH2 D:ARG411 4.3 2.0 1.0 C2A D:HEM754 4.3 2.0 1.0 CZ D:ARG411 4.6 2.0 1.0 CD2 D:HIS128 4.7 2.0 1.0 CG2 D:VAL127 4.7 2.6 1.0 CZ D:PHE214 4.7 2.0 1.0 NE2 D:HIS128 4.7 2.9 1.0

J.Bravo, N.Verdaguer, J.Tormo, C.Betzel, J.Switala, P.C.Loewen, I.Fita. Crystal Structure of Catalase Hpii From Escherichia Coli. Structure V. 3 491 1995.
ISSN: ISSN 0969-2126
PubMed: 7663946
DOI: 10.1016/S0969-2126(01)00182-4