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Iron in PDB 1ggh: Crystal Structure of Catalase Hpii From Escherichia Coli, HIS128ALA Variant.

Enzymatic activity of Crystal Structure of Catalase Hpii From Escherichia Coli, HIS128ALA Variant.

All present enzymatic activity of Crystal Structure of Catalase Hpii From Escherichia Coli, HIS128ALA Variant.:
1.11.1.6;

Protein crystallography data

The structure of Crystal Structure of Catalase Hpii From Escherichia Coli, HIS128ALA Variant., PDB code: 1ggh 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) 87.65 / 2.15
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 (%) 15 / 20.6

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure of Catalase Hpii From Escherichia Coli, HIS128ALA Variant. (pdb code 1ggh). 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, HIS128ALA Variant., PDB code: 1ggh:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in 1ggh

Go back to Iron Binding Sites List in 1ggh
Iron binding site 1 out of 4 in the Crystal Structure of Catalase Hpii From Escherichia Coli, HIS128ALA 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, HIS128ALA Variant. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe760

b:5.8
occ:1.00
FE A:HEM760 0.0 5.8 1.0
NA A:HEM760 2.0 5.6 1.0
OH A:TYR415 2.0 4.0 1.0
ND A:HEM760 2.0 5.7 1.0
NB A:HEM760 2.0 5.4 1.0
NC A:HEM760 2.0 5.3 1.0
CZ A:TYR415 3.0 4.7 1.0
C4D A:HEM760 3.0 5.8 1.0
C4C A:HEM760 3.0 4.4 1.0
C1B A:HEM760 3.0 5.4 1.0
C4A A:HEM760 3.0 5.2 1.0
C1A A:HEM760 3.0 6.0 1.0
C1C A:HEM760 3.0 2.8 1.0
C1D A:HEM760 3.0 6.6 1.0
C4B A:HEM760 3.1 5.5 1.0
CHA A:HEM760 3.4 6.0 1.0
CHB A:HEM760 3.4 5.0 1.0
CHD A:HEM760 3.5 4.5 1.0
CHC A:HEM760 3.5 4.7 1.0
CE1 A:TYR415 3.6 4.2 1.0
CE2 A:TYR415 3.8 3.2 1.0
O A:HOH1039 4.0 6.9 1.0
NE A:ARG411 4.1 5.8 1.0
NH2 A:ARG411 4.1 5.9 1.0
C3D A:HEM760 4.2 6.0 1.0
C3C A:HEM760 4.2 4.1 1.0
C2C A:HEM760 4.3 4.7 1.0
C2D A:HEM760 4.3 6.9 1.0
C2A A:HEM760 4.3 5.8 1.0
C2B A:HEM760 4.3 6.0 1.0
C3A A:HEM760 4.3 5.4 1.0
C3B A:HEM760 4.3 5.4 1.0
O A:HOH1041 4.3 20.7 1.0
CZ A:ARG411 4.5 6.1 1.0
CG2 A:VAL127 4.6 2.1 1.0
CZ A:PHE214 4.8 3.3 1.0
CD1 A:TYR415 4.9 5.0 1.0

Iron binding site 2 out of 4 in 1ggh

Go back to Iron Binding Sites List in 1ggh
Iron binding site 2 out of 4 in the Crystal Structure of Catalase Hpii From Escherichia Coli, HIS128ALA 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, HIS128ALA Variant. within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe760

b:5.5
occ:1.00
FE B:HEM760 0.0 5.5 1.0
OH B:TYR415 2.0 6.5 1.0
ND B:HEM760 2.0 5.6 1.0
NB B:HEM760 2.0 6.6 1.0
NC B:HEM760 2.0 5.6 1.0
NA B:HEM760 2.0 6.0 1.0
CZ B:TYR415 3.0 5.9 1.0
C1D B:HEM760 3.0 5.3 1.0
C4C B:HEM760 3.0 5.1 1.0
C4B B:HEM760 3.0 5.6 1.0
C1B B:HEM760 3.0 5.7 1.0
C1C B:HEM760 3.0 6.0 1.0
C4D B:HEM760 3.1 6.0 1.0
C4A B:HEM760 3.1 4.9 1.0
C1A B:HEM760 3.1 5.4 1.0
CHD B:HEM760 3.4 4.7 1.0
CHB B:HEM760 3.4 5.3 1.0
CHC B:HEM760 3.4 4.9 1.0
CHA B:HEM760 3.5 5.2 1.0
CE1 B:TYR415 3.6 5.5 1.0
CE2 B:TYR415 3.8 5.8 1.0
NE B:ARG411 4.0 4.3 1.0
O B:HOH1097 4.1 14.0 1.0
NH2 B:ARG411 4.1 4.9 1.0
C2D B:HEM760 4.2 4.8 1.0
C3B B:HEM760 4.2 5.3 1.0
C2C B:HEM760 4.2 6.3 1.0
C3C B:HEM760 4.2 5.1 1.0
C2B B:HEM760 4.2 4.9 1.0
C3D B:HEM760 4.2 5.6 1.0
C3A B:HEM760 4.3 5.2 1.0
C2A B:HEM760 4.3 5.0 1.0
O B:HOH1099 4.4 20.5 1.0
CZ B:ARG411 4.5 4.8 1.0
CG2 B:VAL127 4.7 3.0 1.0
CZ B:PHE214 4.7 3.5 1.0
CD1 B:TYR415 4.9 5.2 1.0
CD B:ARG411 5.0 4.4 1.0

Iron binding site 3 out of 4 in 1ggh

Go back to Iron Binding Sites List in 1ggh
Iron binding site 3 out of 4 in the Crystal Structure of Catalase Hpii From Escherichia Coli, HIS128ALA 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, HIS128ALA Variant. within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Fe760

b:5.4
occ:1.00
FE C:HEM760 0.0 5.4 1.0
OH C:TYR415 2.0 3.0 1.0
NA C:HEM760 2.0 4.9 1.0
ND C:HEM760 2.0 5.2 1.0
NC C:HEM760 2.0 6.2 1.0
NB C:HEM760 2.0 6.7 1.0
CZ C:TYR415 3.0 2.3 1.0
C1A C:HEM760 3.0 5.1 1.0
C1D C:HEM760 3.0 5.0 1.0
C4C C:HEM760 3.0 7.0 1.0
C4A C:HEM760 3.0 5.3 1.0
C1B C:HEM760 3.0 6.1 1.0
C4D C:HEM760 3.1 4.7 1.0
C1C C:HEM760 3.1 7.7 1.0
C4B C:HEM760 3.1 6.3 1.0
CHD C:HEM760 3.4 5.9 1.0
CHB C:HEM760 3.4 5.9 1.0
CHA C:HEM760 3.4 4.6 1.0
CHC C:HEM760 3.5 6.9 1.0
CE1 C:TYR415 3.6 3.1 1.0
NE C:ARG411 3.9 2.6 1.0
CE2 C:TYR415 3.9 3.3 1.0
O C:HOH1130 4.0 12.8 1.0
O C:HOH1132 4.1 28.4 1.0
NH2 C:ARG411 4.2 2.0 1.0
C2A C:HEM760 4.3 5.7 1.0
C3C C:HEM760 4.3 7.5 1.0
C2D C:HEM760 4.3 4.8 1.0
C2C C:HEM760 4.3 8.7 1.0
C3A C:HEM760 4.3 4.8 1.0
C3D C:HEM760 4.3 4.2 1.0
C2B C:HEM760 4.3 6.5 1.0
C3B C:HEM760 4.3 6.5 1.0
CZ C:ARG411 4.5 2.1 1.0
CG2 C:VAL127 4.7 2.7 1.0
CZ C:PHE214 4.8 6.8 1.0
CD1 C:TYR415 4.9 3.3 1.0
CD C:ARG411 4.9 2.8 1.0

Iron binding site 4 out of 4 in 1ggh

Go back to Iron Binding Sites List in 1ggh
Iron binding site 4 out of 4 in the Crystal Structure of Catalase Hpii From Escherichia Coli, HIS128ALA 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, HIS128ALA Variant. within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Fe760

b:4.8
occ:1.00
FE D:HEM760 0.0 4.8 1.0
OH D:TYR415 2.0 5.6 1.0
NB D:HEM760 2.0 5.5 1.0
NA D:HEM760 2.0 6.3 1.0
ND D:HEM760 2.0 5.0 1.0
NC D:HEM760 2.0 5.2 1.0
C4B D:HEM760 3.0 5.7 1.0
C1B D:HEM760 3.0 5.9 1.0
C1A D:HEM760 3.0 5.6 1.0
C4C D:HEM760 3.0 4.8 1.0
C1D D:HEM760 3.1 4.4 1.0
CZ D:TYR415 3.1 6.3 1.0
C4D D:HEM760 3.1 4.7 1.0
C1C D:HEM760 3.1 2.7 1.0
C4A D:HEM760 3.1 5.5 1.0
CHC D:HEM760 3.4 4.2 1.0
CHD D:HEM760 3.4 5.7 1.0
CHA D:HEM760 3.4 5.4 1.0
CHB D:HEM760 3.4 6.0 1.0
CE1 D:TYR415 3.8 5.0 1.0
NE D:ARG411 3.9 5.7 1.0
CE2 D:TYR415 3.9 5.4 1.0
O D:HOH1183 4.0 12.0 1.0
O D:HOH1185 4.0 11.8 1.0
NH2 D:ARG411 4.1 4.3 1.0
C2B D:HEM760 4.2 6.2 1.0
C3B D:HEM760 4.2 5.8 1.0
C2A D:HEM760 4.3 5.6 1.0
C3C D:HEM760 4.3 5.2 1.0
C3D D:HEM760 4.3 5.6 1.0
C2C D:HEM760 4.3 4.3 1.0
C2D D:HEM760 4.3 4.9 1.0
C3A D:HEM760 4.3 4.9 1.0
CZ D:ARG411 4.4 5.3 1.0
CG2 D:VAL127 4.7 4.0 1.0
CZ D:PHE214 4.7 4.6 1.0
CD D:ARG411 4.9 4.2 1.0

Reference:

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
Page generated: Wed Jul 16 14:57:53 2025

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