Iron in PDB 1qwm: Structure of Helicobacter Pylori Catalase with Formic Acid Bound

All present enzymatic activity of Structure of Helicobacter Pylori Catalase with Formic Acid Bound:
1.11.1.6;

The structure of Structure of Helicobacter Pylori Catalase with Formic Acid Bound, PDB code: 1qwm was solved by P.C.Loewen, X.Carpena, R.Perez-Luque, C.Rovira, R.Haas, S.Odenbreit, P.Nicholls, I.Fita, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	29.88 / 1.60
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	64.756, 154.961, 96.163, 90.00, 90.00, 90.00
R / Rfree (%)	19.4 / 22.7

The binding sites of Iron atom in the Structure of Helicobacter Pylori Catalase with Formic Acid Bound (pdb code 1qwm). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Structure of Helicobacter Pylori Catalase with Formic Acid Bound, PDB code: 1qwm:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Structure of Helicobacter Pylori Catalase with Formic Acid Bound


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Structure of Helicobacter Pylori Catalase with Formic Acid Bound within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe550 b:10.6 occ:1.00 FE A:HEM550 0.0 10.6 1.0 OH A:TYR339 1.9 11.7 1.0 ND A:HEM550 2.0 11.1 1.0 NA A:HEM550 2.0 8.2 1.0 NB A:HEM550 2.1 11.0 1.0 NC A:HEM550 2.1 11.4 1.0 O2 A:FMT1701 2.6 29.2 1.0 CZ A:TYR339 2.9 9.0 1.0 C1D A:HEM550 3.0 12.8 1.0 C4A A:HEM550 3.0 11.2 1.0 C4C A:HEM550 3.0 13.2 1.0 C1A A:HEM550 3.1 10.2 1.0 C1B A:HEM550 3.1 11.7 1.0 C4D A:HEM550 3.1 11.2 1.0 C4B A:HEM550 3.1 12.6 1.0 C1C A:HEM550 3.1 12.4 1.0 CHD A:HEM550 3.4 12.5 1.0 CHB A:HEM550 3.5 9.4 1.0 CHA A:HEM550 3.5 9.8 1.0 CHC A:HEM550 3.5 13.4 1.0 C A:FMT1701 3.6 28.9 1.0 CE1 A:TYR339 3.6 9.0 1.0 CE2 A:TYR339 3.8 10.3 1.0 NE A:ARG335 4.1 8.7 1.0 O1 A:FMT1701 4.1 26.8 1.0 NH2 A:ARG335 4.2 10.8 1.0 C2D A:HEM550 4.2 10.8 1.0 C2A A:HEM550 4.3 9.8 1.0 C3D A:HEM550 4.3 10.1 1.0 C3A A:HEM550 4.3 9.8 1.0 C3C A:HEM550 4.3 14.7 1.0 C3B A:HEM550 4.3 14.6 1.0 C2B A:HEM550 4.3 12.7 1.0 C2C A:HEM550 4.3 12.4 1.0 CZ A:PHE142 4.4 13.2 1.0 CZ A:ARG335 4.6 11.0 1.0 CG2 A:VAL55 4.7 6.2 1.0 NE2 A:HIS56 4.8 12.1 1.0 CD2 A:HIS56 4.8 12.0 1.0 CE2 A:PHE142 4.9 13.3 1.0 CD1 A:TYR339 4.9 10.1 1.0 CE1 A:PHE142 4.9 10.8 1.0

Iron binding site 2 out of 2 in the Structure of Helicobacter Pylori Catalase with Formic Acid Bound


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Structure of Helicobacter Pylori Catalase with Formic Acid Bound within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe550 b:8.6 occ:1.00 FE B:HEM550 0.0 8.6 1.0 OH B:TYR339 1.9 9.6 1.0 ND B:HEM550 2.0 9.2 1.0 NA B:HEM550 2.0 7.2 1.0 NB B:HEM550 2.1 10.4 1.0 NC B:HEM550 2.1 10.2 1.0 CZ B:TYR339 2.9 7.2 1.0 C4A B:HEM550 3.0 8.3 1.0 C4C B:HEM550 3.0 13.2 1.0 C1D B:HEM550 3.0 9.7 1.0 C1B B:HEM550 3.0 10.8 1.0 C4D B:HEM550 3.0 8.5 1.0 C1A B:HEM550 3.1 6.2 1.0 C4B B:HEM550 3.1 12.7 1.0 C1C B:HEM550 3.1 14.4 1.0 CHB B:HEM550 3.4 10.5 1.0 CHD B:HEM550 3.4 9.1 1.0 CHA B:HEM550 3.5 7.0 1.0 CHC B:HEM550 3.5 14.8 1.0 CE1 B:TYR339 3.7 7.4 1.0 CE2 B:TYR339 3.8 7.5 1.0 O2 B:FMT1702 3.9 38.2 1.0 NE B:ARG335 4.1 10.6 1.0 NH2 B:ARG335 4.2 9.2 1.0 C3D B:HEM550 4.2 8.7 1.0 C3C B:HEM550 4.3 15.9 1.0 C2D B:HEM550 4.3 9.1 1.0 C3A B:HEM550 4.3 7.9 1.0 C2B B:HEM550 4.3 9.5 1.0 C3B B:HEM550 4.3 10.5 1.0 C2A B:HEM550 4.3 7.9 1.0 C2C B:HEM550 4.3 12.9 1.0 CZ B:PHE142 4.4 9.2 1.0 CZ B:ARG335 4.6 13.2 1.0 CG2 B:VAL55 4.7 7.8 1.0 NE2 B:HIS56 4.7 10.0 1.0 CD2 B:HIS56 4.8 11.3 1.0 CE1 B:PHE142 4.8 7.2 1.0 CE2 B:PHE142 4.9 9.6 1.0 CD1 B:TYR339 4.9 5.3 1.0

P.C.Loewen, X.Carpena, C.Rovira, A.Ivancich, R.Perez-Luque, R.Haas, S.Obenbreit, P.Nicholls, I.Fita. Structure of Helicobacter Pylori Catalase, with and Without Formic Acid Bound, at 1.6 A Resolution Biochemistry V. 43 3089 2004.
ISSN: ISSN 0006-2960
PubMed: 15023060
DOI: 10.1021/BI035663I