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Iron in PDB 1qf7: Structure of the Mutant HIS392GLN of Catalase Hpii From E. Coli

Enzymatic activity of Structure of the Mutant HIS392GLN of Catalase Hpii From E. Coli

All present enzymatic activity of Structure of the Mutant HIS392GLN of Catalase Hpii From E. Coli:
1.11.1.6;

Protein crystallography data

The structure of Structure of the Mutant HIS392GLN of Catalase Hpii From E. Coli, PDB code: 1qf7 was solved by M.J.Mate, P.C.Loewen, I.Fita, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 2.20
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 93.400, 132.920, 121.670, 90.00, 109.47, 90.00
R / Rfree (%) 14.4 / 21

Iron Binding Sites:

The binding sites of Iron atom in the Structure of the Mutant HIS392GLN of Catalase Hpii From E. Coli (pdb code 1qf7). 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 the Mutant HIS392GLN of Catalase Hpii From E. Coli, PDB code: 1qf7:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in 1qf7

Go back to Iron Binding Sites List in 1qf7
Iron binding site 1 out of 4 in the Structure of the Mutant HIS392GLN of Catalase Hpii From E. 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 the Mutant HIS392GLN of Catalase Hpii From E. Coli within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe754

b:16.5
occ:1.00
FE A:HEM754 0.0 16.5 1.0
OH A:TYR415 2.0 16.4 1.0
ND A:HEM754 2.0 13.1 1.0
NA A:HEM754 2.0 13.5 1.0
NB A:HEM754 2.0 15.4 1.0
NC A:HEM754 2.0 14.8 1.0
CZ A:TYR415 2.9 14.7 1.0
C4D A:HEM754 3.0 13.1 1.0
C1B A:HEM754 3.0 16.9 1.0
C1A A:HEM754 3.0 14.5 1.0
C1D A:HEM754 3.0 17.2 1.0
C4C A:HEM754 3.0 15.7 1.0
C4A A:HEM754 3.1 16.3 1.0
C4B A:HEM754 3.1 17.2 1.0
C1C A:HEM754 3.1 14.4 1.0
CHA A:HEM754 3.4 13.1 1.0
CHB A:HEM754 3.4 11.0 1.0
CHD A:HEM754 3.4 12.4 1.0
CHC A:HEM754 3.5 13.7 1.0
CE2 A:TYR415 3.6 16.4 1.0
CE1 A:TYR415 3.7 12.3 1.0
NE A:ARG411 4.0 15.2 1.0
NH2 A:ARG411 4.2 11.0 1.0
C3D A:HEM754 4.2 13.5 1.0
C2B A:HEM754 4.2 19.1 1.0
C2D A:HEM754 4.2 16.9 1.0
C3B A:HEM754 4.3 19.0 1.0
C3C A:HEM754 4.3 17.7 1.0
C2A A:HEM754 4.3 16.2 1.0
C2C A:HEM754 4.3 19.0 1.0
C3A A:HEM754 4.3 16.5 1.0
CZ A:ARG411 4.5 14.0 1.0
O A:HOH1469 4.5 25.5 1.0
CZ A:PHE214 4.7 14.6 1.0
CD2 A:HIS128 4.7 5.2 1.0
CG2 A:VAL127 4.7 9.7 1.0
NE2 A:HIS128 4.8 7.3 1.0
CD2 A:TYR415 4.9 17.9 1.0
CD1 A:TYR415 5.0 16.1 1.0

Iron binding site 2 out of 4 in 1qf7

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Iron binding site 2 out of 4 in the Structure of the Mutant HIS392GLN of Catalase Hpii From E. 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 the Mutant HIS392GLN of Catalase Hpii From E. Coli within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe754

b:16.8
occ:1.00
FE B:HEM754 0.0 16.8 1.0
OH B:TYR415 2.0 13.4 1.0
NB B:HEM754 2.0 16.1 1.0
NA B:HEM754 2.0 14.6 1.0
ND B:HEM754 2.0 13.5 1.0
NC B:HEM754 2.0 15.1 1.0
O B:HOH1377 2.9 31.3 0.5
CZ B:TYR415 2.9 16.3 1.0
C1B B:HEM754 3.0 17.7 1.0
C4B B:HEM754 3.0 17.3 1.0
C4C B:HEM754 3.0 15.4 1.0
C1C B:HEM754 3.1 15.4 1.0
C4A B:HEM754 3.1 16.8 1.0
C1D B:HEM754 3.1 17.2 1.0
C4D B:HEM754 3.1 13.3 1.0
C1A B:HEM754 3.1 15.0 1.0
CHB B:HEM754 3.4 10.8 1.0
CHD B:HEM754 3.4 12.2 1.0
CHC B:HEM754 3.4 14.0 1.0
CHA B:HEM754 3.5 13.0 1.0
CE2 B:TYR415 3.7 15.7 1.0
CE1 B:TYR415 3.8 15.5 1.0
NE B:ARG411 4.0 11.6 1.0
NH2 B:ARG411 4.1 13.5 1.0
C3B B:HEM754 4.2 18.8 1.0
C2B B:HEM754 4.2 18.6 1.0
C3C B:HEM754 4.2 17.5 1.0
C2C B:HEM754 4.2 19.1 1.0
C2D B:HEM754 4.3 16.6 1.0
C3A B:HEM754 4.3 16.5 1.0
C3D B:HEM754 4.3 13.8 1.0
C2A B:HEM754 4.3 16.3 1.0
CZ B:ARG411 4.4 14.2 1.0
O B:HOH1369 4.6 17.2 1.0
CZ B:PHE214 4.6 13.5 1.0
CG2 B:VAL127 4.7 11.6 1.0
NE2 B:HIS128 4.8 12.1 1.0
CD B:ARG411 4.9 11.1 1.0
CD2 B:HIS128 4.9 7.1 1.0
CD2 B:TYR415 4.9 15.2 1.0
CD1 B:TYR415 5.0 14.5 1.0

Iron binding site 3 out of 4 in 1qf7

Go back to Iron Binding Sites List in 1qf7
Iron binding site 3 out of 4 in the Structure of the Mutant HIS392GLN of Catalase Hpii From E. 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 the Mutant HIS392GLN of Catalase Hpii From E. Coli within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Fe754

b:16.9
occ:1.00
FE C:HEM754 0.0 16.9 1.0
OH C:TYR415 2.0 13.3 1.0
NA C:HEM754 2.0 13.4 1.0
NB C:HEM754 2.0 15.9 1.0
ND C:HEM754 2.0 13.8 1.0
NC C:HEM754 2.0 15.0 1.0
CZ C:TYR415 3.0 13.4 1.0
C1B C:HEM754 3.0 17.5 1.0
C1A C:HEM754 3.0 15.2 1.0
C4A C:HEM754 3.0 16.5 1.0
C4B C:HEM754 3.0 17.4 1.0
C4D C:HEM754 3.0 13.3 1.0
C1D C:HEM754 3.1 17.4 1.0
C4C C:HEM754 3.1 15.7 1.0
C1C C:HEM754 3.1 15.5 1.0
CHB C:HEM754 3.4 10.1 1.0
CHA C:HEM754 3.4 13.3 1.0
CHD C:HEM754 3.5 12.4 1.0
CHC C:HEM754 3.5 14.0 1.0
CE2 C:TYR415 3.7 16.3 1.0
CE1 C:TYR415 3.8 13.9 1.0
NE C:ARG411 3.9 13.7 1.0
NH2 C:ARG411 4.1 10.9 1.0
C2B C:HEM754 4.2 18.8 1.0
C3B C:HEM754 4.2 18.9 1.0
C2A C:HEM754 4.2 16.2 1.0
C3A C:HEM754 4.3 16.4 1.0
C3D C:HEM754 4.3 13.7 1.0
C3C C:HEM754 4.3 17.8 1.0
C2D C:HEM754 4.3 16.4 1.0
C2C C:HEM754 4.3 19.1 1.0
CZ C:ARG411 4.4 15.4 1.0
CZ C:PHE214 4.7 11.6 1.0
O C:HOH1382 4.7 26.9 1.0
CD2 C:HIS128 4.8 8.4 1.0
CG2 C:VAL127 4.8 10.6 1.0
NE2 C:HIS128 4.8 12.1 1.0
CD C:ARG411 4.9 13.6 1.0
CD2 C:TYR415 4.9 15.3 1.0
CD1 C:TYR415 5.0 12.9 1.0

Iron binding site 4 out of 4 in 1qf7

Go back to Iron Binding Sites List in 1qf7
Iron binding site 4 out of 4 in the Structure of the Mutant HIS392GLN of Catalase Hpii From E. 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 the Mutant HIS392GLN of Catalase Hpii From E. Coli within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Fe754

b:16.2
occ:1.00
FE D:HEM754 0.0 16.2 1.0
OH D:TYR415 2.0 15.1 1.0
NB D:HEM754 2.0 15.7 1.0
NA D:HEM754 2.0 13.9 1.0
ND D:HEM754 2.0 13.4 1.0
NC D:HEM754 2.0 15.1 1.0
CZ D:TYR415 3.0 17.4 1.0
C1B D:HEM754 3.0 17.0 1.0
C4D D:HEM754 3.0 13.2 1.0
C4B D:HEM754 3.0 17.3 1.0
C1A D:HEM754 3.0 15.0 1.0
C4A D:HEM754 3.1 16.0 1.0
C4C D:HEM754 3.1 15.7 1.0
C1D D:HEM754 3.1 16.6 1.0
C1C D:HEM754 3.1 15.0 1.0
CHB D:HEM754 3.4 11.2 1.0
CHA D:HEM754 3.4 12.7 1.0
CHC D:HEM754 3.4 14.0 1.0
CHD D:HEM754 3.5 12.4 1.0
CE2 D:TYR415 3.8 16.5 1.0
CE1 D:TYR415 3.8 16.4 1.0
NE D:ARG411 4.0 14.8 1.0
NH2 D:ARG411 4.1 9.6 1.0
C2B D:HEM754 4.2 18.8 1.0
C3B D:HEM754 4.2 19.1 1.0
C3D D:HEM754 4.3 13.9 1.0
C2A D:HEM754 4.3 16.3 1.0
C3A D:HEM754 4.3 16.2 1.0
C2D D:HEM754 4.3 17.0 1.0
C3C D:HEM754 4.3 17.6 1.0
C2C D:HEM754 4.3 18.7 1.0
CZ D:ARG411 4.5 15.2 1.0
CZ D:PHE214 4.7 15.4 1.0
O D:HOH1438 4.7 22.1 1.0
CG2 D:VAL127 4.7 10.1 1.0
NE2 D:HIS128 4.8 11.4 1.0
CD2 D:HIS128 4.8 7.0 1.0

Reference:

M.J.Mate, M.S.Sevinc, B.Hu, J.Bujons, J.Bravo, J.Switala, W.Ens, P.C.Loewen, I.Fita. Mutants That Alter the Covalent Structure of Catalase Hydroperoxidase II From Escherichia Coli. J.Biol.Chem. V. 274 27717 1999.
ISSN: ISSN 0021-9258
PubMed: 10488114
DOI: 10.1074/JBC.274.39.27717
Page generated: Sat Aug 3 13:24:09 2024

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