Iron in PDB 1cf9: Structure of the Mutant VAL169CYS of Catalase Hpii From Escherichia Coli

All present enzymatic activity of Structure of the Mutant VAL169CYS of Catalase Hpii From Escherichia Coli:
1.11.1.6;

The structure of Structure of the Mutant VAL169CYS of Catalase Hpii From Escherichia Coli, PDB code: 1cf9 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 / 1.80
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	93.470, 133.040, 122.220, 90.00, 109.64, 90.00
R / Rfree (%)	18.1 / 23.7

The binding sites of Iron atom in the Structure of the Mutant VAL169CYS of Catalase Hpii From Escherichia Coli (pdb code 1cf9). 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 VAL169CYS of Catalase Hpii From Escherichia Coli, PDB code: 1cf9:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in the Structure of the Mutant VAL169CYS 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 the Mutant VAL169CYS of Catalase Hpii From Escherichia Coli within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe754 b:12.2 occ:1.00 FE A:HEM754 0.0 12.2 1.0 OH A:TYR415 2.0 12.1 1.0 NC A:HEM754 2.0 10.3 1.0 ND A:HEM754 2.0 12.9 1.0 NB A:HEM754 2.0 12.1 1.0 NA A:HEM754 2.1 10.8 1.0 CZ A:TYR415 2.9 11.3 1.0 C4C A:HEM754 3.0 10.8 1.0 C1C A:HEM754 3.0 13.8 1.0 C4B A:HEM754 3.0 13.7 1.0 C1D A:HEM754 3.1 14.4 1.0 C1B A:HEM754 3.1 12.4 1.0 C4A A:HEM754 3.1 11.5 1.0 C1A A:HEM754 3.1 12.1 1.0 C4D A:HEM754 3.1 12.5 1.0 CHC A:HEM754 3.4 12.9 1.0 CHD A:HEM754 3.5 9.6 1.0 CHB A:HEM754 3.5 11.6 1.0 CHA A:HEM754 3.5 14.9 1.0 CE2 A:TYR415 3.5 8.9 1.0 NE A:ARG411 3.9 8.7 1.0 CE1 A:TYR415 3.9 10.4 1.0 O A:HOH1118 4.1 27.5 1.0 NH2 A:ARG411 4.2 4.9 1.0 C2C A:HEM754 4.2 13.2 1.0 C3C A:HEM754 4.2 10.8 1.0 C2B A:HEM754 4.3 15.7 1.0 C3B A:HEM754 4.3 12.8 1.0 C3D A:HEM754 4.3 13.5 1.0 C2D A:HEM754 4.3 15.3 1.0 C2A A:HEM754 4.3 10.2 1.0 C3A A:HEM754 4.3 11.1 1.0 CZ A:ARG411 4.4 12.8 1.0 CG2 A:VAL127 4.6 10.6 1.0 CZ A:PHE214 4.8 11.4 1.0 CD2 A:TYR415 4.8 13.9 1.0 CD2 A:HIS128 4.9 11.8 1.0 CD A:ARG411 4.9 10.9 1.0

Iron binding site 2 out of 4 in the Structure of the Mutant VAL169CYS 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 the Mutant VAL169CYS of Catalase Hpii From Escherichia Coli within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe754 b:13.6 occ:1.00 FE B:HEM754 0.0 13.6 1.0 OH B:TYR415 2.0 15.1 1.0 NC B:HEM754 2.0 11.5 1.0 NB B:HEM754 2.0 13.0 1.0 ND B:HEM754 2.0 12.0 1.0 NA B:HEM754 2.1 12.6 1.0 CZ B:TYR415 3.0 14.6 1.0 C4C B:HEM754 3.0 10.3 1.0 C1B B:HEM754 3.0 12.4 1.0 C1C B:HEM754 3.0 13.6 1.0 C4B B:HEM754 3.1 13.9 1.0 C1D B:HEM754 3.1 14.8 1.0 C1A B:HEM754 3.1 11.9 1.0 C4A B:HEM754 3.1 10.7 1.0 C4D B:HEM754 3.1 13.2 1.0 CHD B:HEM754 3.4 10.4 1.0 CHB B:HEM754 3.4 10.9 1.0 CHC B:HEM754 3.5 12.5 1.0 CHA B:HEM754 3.5 15.1 1.0 CE2 B:TYR415 3.6 12.7 1.0 CE1 B:TYR415 3.9 13.7 1.0 NE B:ARG411 4.0 11.2 1.0 O B:HOH1285 4.0 30.6 1.0 NH2 B:ARG411 4.1 10.4 1.0 C2C B:HEM754 4.3 13.2 1.0 C2B B:HEM754 4.3 15.5 1.0 C3C B:HEM754 4.3 10.9 1.0 C3B B:HEM754 4.3 12.9 1.0 C2D B:HEM754 4.3 15.2 1.0 C3A B:HEM754 4.3 12.0 1.0 C3D B:HEM754 4.3 14.0 1.0 C2A B:HEM754 4.3 11.4 1.0 CZ B:ARG411 4.4 13.9 1.0 CG2 B:VAL127 4.6 12.3 1.0 CZ B:PHE214 4.8 12.2 1.0 CD2 B:HIS128 4.9 12.3 1.0 CD2 B:TYR415 4.9 13.7 1.0

Iron binding site 3 out of 4 in the Structure of the Mutant VAL169CYS 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 the Mutant VAL169CYS of Catalase Hpii From Escherichia Coli within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe754 b:12.9 occ:1.00 FE C:HEM754 0.0 12.9 1.0 OH C:TYR415 2.0 15.2 1.0 NA C:HEM754 2.0 11.4 1.0 NB C:HEM754 2.0 12.4 1.0 ND C:HEM754 2.0 12.9 1.0 NC C:HEM754 2.1 11.2 1.0 CZ C:TYR415 3.0 13.6 1.0 C4A C:HEM754 3.0 11.0 1.0 C1B C:HEM754 3.0 12.8 1.0 C1A C:HEM754 3.0 12.0 1.0 C4B C:HEM754 3.1 14.0 1.0 C4C C:HEM754 3.1 10.2 1.0 C1C C:HEM754 3.1 13.6 1.0 C1D C:HEM754 3.1 14.0 1.0 C4D C:HEM754 3.1 12.4 1.0 CHB C:HEM754 3.4 11.2 1.0 CHA C:HEM754 3.4 15.3 1.0 CHD C:HEM754 3.4 9.7 1.0 CHC C:HEM754 3.5 13.4 1.0 CE2 C:TYR415 3.6 9.3 1.0 CE1 C:TYR415 3.8 13.6 1.0 NE C:ARG411 4.0 10.4 1.0 NH2 C:ARG411 4.1 6.9 1.0 C2B C:HEM754 4.2 15.8 1.0 C3B C:HEM754 4.2 12.9 1.0 C3A C:HEM754 4.3 11.5 1.0 C2A C:HEM754 4.3 11.3 1.0 C2C C:HEM754 4.3 13.4 1.0 C3C C:HEM754 4.3 11.2 1.0 C2D C:HEM754 4.3 15.7 1.0 C3D C:HEM754 4.3 13.6 1.0 CZ C:ARG411 4.4 11.8 1.0 CG2 C:VAL127 4.7 11.1 1.0 CZ C:PHE214 4.7 10.2 1.0 CD2 C:TYR415 4.9 9.5 1.0 CD2 C:HIS128 4.9 10.5 1.0 CD C:ARG411 4.9 10.7 1.0

Iron binding site 4 out of 4 in the Structure of the Mutant VAL169CYS 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 the Mutant VAL169CYS of Catalase Hpii From Escherichia Coli within 5.0Å range: probe atom residue distance (Å) B Occ D:Fe754 b:12.9 occ:1.00 FE D:HEM754 0.0 12.9 1.0 OH D:TYR415 2.0 13.9 1.0 ND D:HEM754 2.0 12.2 1.0 NC D:HEM754 2.0 11.7 1.0 NB D:HEM754 2.0 12.0 1.0 NA D:HEM754 2.1 11.8 1.0 CZ D:TYR415 3.0 13.0 1.0 C4C D:HEM754 3.0 10.0 1.0 C1D D:HEM754 3.0 13.8 1.0 C4D D:HEM754 3.0 12.6 1.0 C1C D:HEM754 3.1 13.3 1.0 C4B D:HEM754 3.1 14.2 1.0 C1B D:HEM754 3.1 12.7 1.0 C1A D:HEM754 3.1 11.7 1.0 C4A D:HEM754 3.1 11.4 1.0 CHA D:HEM754 3.4 14.9 1.0 CHC D:HEM754 3.4 12.8 1.0 CHD D:HEM754 3.4 10.1 1.0 CHB D:HEM754 3.5 10.5 1.0 CE2 D:TYR415 3.7 9.9 1.0 CE1 D:TYR415 3.9 12.1 1.0 NE D:ARG411 3.9 9.1 1.0 NH2 D:ARG411 4.1 8.4 1.0 C3D D:HEM754 4.2 13.5 1.0 C2D D:HEM754 4.2 15.1 1.0 C2C D:HEM754 4.3 13.4 1.0 C3C D:HEM754 4.3 11.7 1.0 C3B D:HEM754 4.3 13.0 1.0 C2B D:HEM754 4.3 15.5 1.0 C2A D:HEM754 4.3 11.3 1.0 C3A D:HEM754 4.3 11.2 1.0 O D:HOH1446 4.4 29.3 1.0 CZ D:ARG411 4.5 10.2 1.0 CG2 D:VAL127 4.6 10.0 1.0 CZ D:PHE214 4.7 9.0 1.0 CD2 D:TYR415 4.9 11.6 1.0 CD2 D:HIS128 4.9 10.3 1.0 CD D:ARG411 5.0 8.8 1.0

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