Iron in PDB 1gg9: Crystal Structure of Catalase Hpii From Escherichia Coli, HIS128ASN Variant.

All present enzymatic activity of Crystal Structure of Catalase Hpii From Escherichia Coli, HIS128ASN Variant.:
1.11.1.6;

The structure of Crystal Structure of Catalase Hpii From Escherichia Coli, HIS128ASN Variant., PDB code: 1gg9 was solved by W.R.Melik-Adamyan, J.Bravo, X.Carpena, J.Switala, M.J.Mate, I.Fita, P.C.Loewen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	87.63 / 1.89
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	93.040, 132.340, 121.200, 90.00, 109.63, 90.00
R / Rfree (%)	14.4 / 18.8

The binding sites of Iron atom in the Crystal Structure of Catalase Hpii From Escherichia Coli, HIS128ASN Variant. (pdb code 1gg9). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 4 binding sites of Iron where determined in the Crystal Structure of Catalase Hpii From Escherichia Coli, HIS128ASN Variant., PDB code: 1gg9:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in the Crystal Structure of Catalase Hpii From Escherichia Coli, HIS128ASN Variant.


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 Hpii From Escherichia Coli, HIS128ASN Variant. within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe760 b:6.3 occ:1.00 FE A:HEM760 0.0 6.3 1.0 OH A:TYR415 2.0 5.2 1.0 NA A:HEM760 2.0 5.8 1.0 ND A:HEM760 2.0 5.4 1.0 NC A:HEM760 2.0 5.5 1.0 NB A:HEM760 2.0 4.7 1.0 CZ A:TYR415 3.0 4.8 1.0 C1D A:HEM760 3.0 5.9 1.0 C4C A:HEM760 3.0 5.4 1.0 C1B A:HEM760 3.0 4.3 1.0 C4A A:HEM760 3.0 5.9 1.0 C4B A:HEM760 3.1 4.6 1.0 C1C A:HEM760 3.1 5.2 1.0 C4D A:HEM760 3.1 5.3 1.0 C1A A:HEM760 3.1 5.9 1.0 CHD A:HEM760 3.4 6.1 1.0 CHB A:HEM760 3.4 5.0 1.0 CHC A:HEM760 3.5 4.8 1.0 CHA A:HEM760 3.5 5.7 1.0 O A:HOH1143 3.5 8.7 1.0 CE1 A:TYR415 3.6 5.3 1.0 CE2 A:TYR415 3.9 4.5 1.0 NE A:ARG411 3.9 4.4 1.0 NH2 A:ARG411 4.1 4.7 1.0 C3C A:HEM760 4.2 5.5 1.0 C2D A:HEM760 4.2 5.8 1.0 C2C A:HEM760 4.2 4.8 1.0 C3D A:HEM760 4.3 4.8 1.0 C2B A:HEM760 4.3 4.8 1.0 C3B A:HEM760 4.3 3.9 1.0 C3A A:HEM760 4.3 5.9 1.0 C2A A:HEM760 4.3 6.0 1.0 CZ A:ARG411 4.4 5.7 1.0 O A:HOH1257 4.5 11.0 1.0 CG2 A:VAL127 4.8 3.7 1.0 CZ A:PHE214 4.8 5.0 1.0 CD1 A:TYR415 4.9 6.3 1.0 CD A:ARG411 4.9 5.2 1.0

Iron binding site 2 out of 4 in the Crystal Structure of Catalase Hpii From Escherichia Coli, HIS128ASN Variant.


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 Hpii From Escherichia Coli, HIS128ASN Variant. within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe760 b:5.9 occ:1.00 FE B:HEM760 0.0 5.9 1.0 OH B:TYR415 2.0 6.5 1.0 ND B:HEM760 2.0 5.6 1.0 NC B:HEM760 2.0 5.1 1.0 NA B:HEM760 2.0 5.0 1.0 NB B:HEM760 2.0 5.9 1.0 CZ B:TYR415 3.0 6.4 1.0 C4C B:HEM760 3.0 5.4 1.0 C1D B:HEM760 3.0 5.7 1.0 C1B B:HEM760 3.0 5.5 1.0 C4B B:HEM760 3.0 5.8 1.0 C4A B:HEM760 3.1 4.7 1.0 C1A B:HEM760 3.1 5.9 1.0 C1C B:HEM760 3.1 5.1 1.0 C4D B:HEM760 3.1 5.9 1.0 CHD B:HEM760 3.4 5.9 1.0 CHB B:HEM760 3.4 5.2 1.0 CHC B:HEM760 3.5 5.5 1.0 CHA B:HEM760 3.5 6.1 1.0 O B:HOH836 3.5 12.6 1.0 CE1 B:TYR415 3.6 6.0 1.0 CE2 B:TYR415 3.9 6.9 1.0 NE B:ARG411 4.0 4.2 1.0 NH2 B:ARG411 4.2 3.2 1.0 C3C B:HEM760 4.2 5.6 1.0 C2B B:HEM760 4.2 6.3 1.0 C2D B:HEM760 4.3 5.8 1.0 C2C B:HEM760 4.3 5.6 1.0 C3B B:HEM760 4.3 5.7 1.0 C3D B:HEM760 4.3 5.6 1.0 C2A B:HEM760 4.3 5.4 1.0 C3A B:HEM760 4.3 5.1 1.0 CZ B:ARG411 4.5 4.0 1.0 O B:HOH1205 4.5 15.5 1.0 CG2 B:VAL127 4.7 5.7 1.0 CZ B:PHE214 4.8 5.5 1.0 CD1 B:TYR415 4.9 5.2 1.0

Iron binding site 3 out of 4 in the Crystal Structure of Catalase Hpii From Escherichia Coli, HIS128ASN Variant.


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Crystal Structure of Catalase Hpii From Escherichia Coli, HIS128ASN Variant. within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe760 b:6.8 occ:1.00 FE C:HEM760 0.0 6.8 1.0 NA C:HEM760 2.0 5.8 1.0 NC C:HEM760 2.0 7.0 1.0 OH C:TYR415 2.0 5.7 1.0 ND C:HEM760 2.0 6.2 1.0 NB C:HEM760 2.0 6.7 1.0 CZ C:TYR415 3.0 6.4 1.0 C4C C:HEM760 3.0 7.1 1.0 C4A C:HEM760 3.0 6.0 1.0 C1B C:HEM760 3.0 6.5 1.0 C1D C:HEM760 3.0 6.1 1.0 C4B C:HEM760 3.1 6.1 1.0 C1C C:HEM760 3.1 6.9 1.0 C1A C:HEM760 3.1 6.2 1.0 C4D C:HEM760 3.1 5.2 1.0 CHD C:HEM760 3.4 6.4 1.0 CHB C:HEM760 3.4 6.3 1.0 CHC C:HEM760 3.4 6.3 1.0 CHA C:HEM760 3.4 5.8 1.0 O C:HOH1246 3.5 11.2 1.0 CE1 C:TYR415 3.6 6.2 1.0 NE C:ARG411 3.9 5.3 1.0 CE2 C:TYR415 4.0 6.1 1.0 NH2 C:ARG411 4.0 4.5 1.0 C3C C:HEM760 4.2 7.2 1.0 C2C C:HEM760 4.2 7.4 1.0 C2B C:HEM760 4.3 6.4 1.0 C3B C:HEM760 4.3 5.8 1.0 C3A C:HEM760 4.3 5.7 1.0 C2D C:HEM760 4.3 6.0 1.0 C3D C:HEM760 4.3 5.8 1.0 C2A C:HEM760 4.3 6.5 1.0 CZ C:ARG411 4.4 5.3 1.0 O C:HOH866 4.4 17.6 1.0 CG2 C:VAL127 4.7 6.0 1.0 CZ C:PHE214 4.8 6.0 1.0 CD1 C:TYR415 4.9 6.2 1.0 CD C:ARG411 4.9 5.1 1.0

Iron binding site 4 out of 4 in the Crystal Structure of Catalase Hpii From Escherichia Coli, HIS128ASN Variant.


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Crystal Structure of Catalase Hpii From Escherichia Coli, HIS128ASN Variant. within 5.0Å range: probe atom residue distance (Å) B Occ D:Fe760 b:5.0 occ:1.00 FE D:HEM760 0.0 5.0 1.0 OH D:TYR415 2.0 4.4 1.0 NB D:HEM760 2.0 4.5 1.0 NA D:HEM760 2.0 4.0 1.0 ND D:HEM760 2.0 4.8 1.0 NC D:HEM760 2.0 4.7 1.0 CZ D:TYR415 3.0 4.6 1.0 C4C D:HEM760 3.0 3.6 1.0 C1B D:HEM760 3.0 4.0 1.0 C1A D:HEM760 3.0 5.1 1.0 C4B D:HEM760 3.0 5.3 1.0 C1D D:HEM760 3.0 4.8 1.0 C4A D:HEM760 3.1 3.5 1.0 C1C D:HEM760 3.1 3.8 1.0 C4D D:HEM760 3.1 4.3 1.0 CHD D:HEM760 3.4 4.4 1.0 CHC D:HEM760 3.4 4.6 1.0 CHB D:HEM760 3.4 2.5 1.0 CHA D:HEM760 3.4 4.0 1.0 O D:HOH960 3.6 8.5 1.0 CE1 D:TYR415 3.6 4.9 1.0 CE2 D:TYR415 3.9 4.5 1.0 NE D:ARG411 3.9 3.9 1.0 NH2 D:ARG411 4.0 3.9 1.0 C2B D:HEM760 4.2 4.0 1.0 C3C D:HEM760 4.2 3.8 1.0 C3B D:HEM760 4.3 4.7 1.0 C2C D:HEM760 4.3 3.7 1.0 C2A D:HEM760 4.3 4.3 1.0 C3D D:HEM760 4.3 4.5 1.0 C2D D:HEM760 4.3 5.1 1.0 C3A D:HEM760 4.3 3.8 1.0 O D:HOH820 4.3 13.8 1.0 CZ D:ARG411 4.4 4.5 1.0 CG2 D:VAL127 4.7 3.8 1.0 CZ D:PHE214 4.9 4.0 1.0 CD1 D:TYR415 4.9 4.7 1.0 CD D:ARG411 4.9 3.2 1.0

W.Melik-Adamyan, J.Bravo, X.Carpena, J.Switala, M.J.Mate, I.Fita, P.C.Loewen. Substrate Flow in Catalases Deduced From the Crystal Structures of Active Site Variants of Hpii From Escherichia Coli. Proteins V. 44 270 2001.
ISSN: ISSN 0887-3585
PubMed: 11455600
DOI: 10.1002/PROT.1092