Iron in PDB 1qqw: Crystal Structure of Human Erythrocyte Catalase

All present enzymatic activity of Crystal Structure of Human Erythrocyte Catalase:
1.11.1.6;

The structure of Crystal Structure of Human Erythrocyte Catalase, PDB code: 1qqw was solved by T.P.Ko, M.K.Safo, F.N.Musayev, C.Wang, S.H.Wu, D.J.Abraham, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	40.00 / 2.75
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	84.904, 141.674, 232.460, 90.00, 90.00, 90.00
R / Rfree (%)	20.6 / 27.2

The binding sites of Iron atom in the Crystal Structure of Human Erythrocyte Catalase (pdb code 1qqw). 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 Human Erythrocyte Catalase, PDB code: 1qqw:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in the Crystal Structure of Human Erythrocyte Catalase


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 Human Erythrocyte Catalase within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe600 b:15.9 occ:1.00 FE A:HEM600 0.0 15.9 1.0 NC A:HEM600 1.9 14.0 1.0 ND A:HEM600 2.0 13.6 1.0 NB A:HEM600 2.0 13.5 1.0 NA A:HEM600 2.0 13.5 1.0 OH A:TYR358 2.0 12.9 1.0 C4C A:HEM600 3.0 14.1 1.0 C1C A:HEM600 3.0 14.1 1.0 C1D A:HEM600 3.0 13.7 1.0 C4D A:HEM600 3.0 13.7 1.0 C4B A:HEM600 3.0 13.6 1.0 C1A A:HEM600 3.1 13.5 1.0 C1B A:HEM600 3.1 13.4 1.0 C4A A:HEM600 3.1 13.4 1.0 CZ A:TYR358 3.1 13.4 1.0 CHD A:HEM600 3.4 14.1 1.0 CHC A:HEM600 3.4 14.1 1.0 CHA A:HEM600 3.4 13.8 1.0 CHB A:HEM600 3.5 13.6 1.0 CE2 A:TYR358 3.8 13.2 1.0 NH2 A:ARG354 3.9 12.6 1.0 O A:HOH616 4.0 16.4 1.0 CE1 A:TYR358 4.1 13.3 1.0 NE A:ARG354 4.1 12.9 1.0 C2C A:HEM600 4.2 14.3 1.0 C3C A:HEM600 4.2 14.2 1.0 C2D A:HEM600 4.3 13.7 1.0 NE2 A:HIS75 4.3 12.2 1.0 C3D A:HEM600 4.3 13.7 1.0 C2B A:HEM600 4.3 13.3 1.0 C3B A:HEM600 4.3 13.5 1.0 C2A A:HEM600 4.3 13.3 1.0 C3A A:HEM600 4.3 13.5 1.0 CD2 A:HIS75 4.4 12.0 1.0 CZ A:ARG354 4.4 12.8 1.0 CG2 A:VAL74 4.8 11.4 1.0 CZ A:PHE161 4.9 13.5 1.0

Iron binding site 2 out of 4 in the Crystal Structure of Human Erythrocyte Catalase


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 Human Erythrocyte Catalase within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe600 b:14.3 occ:1.00 FE B:HEM600 0.0 14.3 1.0 NA B:HEM600 2.0 13.9 1.0 NB B:HEM600 2.0 13.7 1.0 ND B:HEM600 2.0 13.9 1.0 NC B:HEM600 2.0 13.8 1.0 OH B:TYR358 2.7 11.7 1.0 C1A B:HEM600 3.0 13.8 1.0 C4A B:HEM600 3.0 13.8 1.0 C1C B:HEM600 3.1 13.6 1.0 C4D B:HEM600 3.1 13.9 1.0 C1B B:HEM600 3.1 13.8 1.0 C4B B:HEM600 3.1 13.7 1.0 C1D B:HEM600 3.1 13.7 1.0 C4C B:HEM600 3.1 13.6 1.0 CHA B:HEM600 3.4 14.1 1.0 CHC B:HEM600 3.5 13.8 1.0 CHB B:HEM600 3.5 13.9 1.0 CHD B:HEM600 3.5 13.7 1.0 CZ B:TYR358 3.6 12.0 1.0 O B:HOH621 3.8 10.3 1.0 NE2 B:HIS75 4.2 13.2 1.0 CE2 B:TYR358 4.2 12.0 1.0 CD2 B:HIS75 4.2 13.1 1.0 C2A B:HEM600 4.3 13.6 1.0 C3A B:HEM600 4.3 13.7 1.0 C2C B:HEM600 4.3 13.6 1.0 C3D B:HEM600 4.3 13.9 1.0 C2B B:HEM600 4.3 13.7 1.0 C3B B:HEM600 4.3 13.7 1.0 C2D B:HEM600 4.3 13.8 1.0 C3C B:HEM600 4.3 13.4 1.0 CZ B:PHE161 4.4 13.3 1.0 CE1 B:TYR358 4.5 12.1 1.0 CG2 B:VAL74 4.5 13.6 1.0 NE B:ARG354 4.6 12.3 1.0 NH2 B:ARG354 4.6 12.3 1.0 CE1 B:PHE161 4.8 13.2 1.0

Iron binding site 3 out of 4 in the Crystal Structure of Human Erythrocyte Catalase


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 Human Erythrocyte Catalase within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe600 b:12.8 occ:1.00 FE C:HEM600 0.0 12.8 1.0 ND C:HEM600 2.0 12.4 1.0 NA C:HEM600 2.0 12.7 1.0 NB C:HEM600 2.0 12.9 1.0 NC C:HEM600 2.0 12.8 1.0 OH C:TYR358 2.8 10.7 1.0 C4D C:HEM600 3.0 12.6 1.0 C1C C:HEM600 3.0 12.9 1.0 C1A C:HEM600 3.0 12.5 1.0 C4A C:HEM600 3.0 12.9 1.0 C1D C:HEM600 3.0 12.5 1.0 C4B C:HEM600 3.1 13.0 1.0 C4C C:HEM600 3.1 12.7 1.0 C1B C:HEM600 3.1 13.1 1.0 CHA C:HEM600 3.4 12.5 1.0 CHC C:HEM600 3.4 12.9 1.0 CHD C:HEM600 3.4 12.6 1.0 CHB C:HEM600 3.5 12.9 1.0 CZ C:TYR358 3.6 11.3 1.0 O C:HOH628 3.9 7.1 1.0 CE2 C:TYR358 4.1 11.3 1.0 NE2 C:HIS75 4.1 11.2 1.0 CD2 C:HIS75 4.2 11.2 1.0 C3A C:HEM600 4.3 12.8 1.0 C2C C:HEM600 4.3 13.0 1.0 C3D C:HEM600 4.3 12.5 1.0 C2D C:HEM600 4.3 12.5 1.0 C2A C:HEM600 4.3 12.6 1.0 C3C C:HEM600 4.3 12.9 1.0 C2B C:HEM600 4.3 13.2 1.0 C3B C:HEM600 4.3 13.2 1.0 CE1 C:TYR358 4.5 11.5 1.0 CZ C:PHE161 4.6 11.4 1.0 NE C:ARG354 4.6 12.5 1.0 CG2 C:VAL74 4.8 11.9 1.0 NH2 C:ARG354 4.9 12.5 1.0

Iron binding site 4 out of 4 in the Crystal Structure of Human Erythrocyte Catalase


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 Human Erythrocyte Catalase within 5.0Å range: probe atom residue distance (Å) B Occ D:Fe600 b:14.2 occ:1.00 FE D:HEM600 0.0 14.2 1.0 NC D:HEM600 2.0 13.7 1.0 ND D:HEM600 2.0 13.9 1.0 NB D:HEM600 2.0 13.9 1.0 NA D:HEM600 2.0 13.6 1.0 OH D:TYR358 2.8 10.6 1.0 C1C D:HEM600 3.0 13.8 1.0 C4C D:HEM600 3.1 13.8 1.0 C1D D:HEM600 3.1 13.8 1.0 C4D D:HEM600 3.1 13.9 1.0 C1A D:HEM600 3.1 13.6 1.0 C4B D:HEM600 3.1 13.7 1.0 C1B D:HEM600 3.1 13.9 1.0 C4A D:HEM600 3.1 13.5 1.0 CHC D:HEM600 3.4 13.8 1.0 CHA D:HEM600 3.5 13.8 1.0 CHD D:HEM600 3.5 13.9 1.0 CHB D:HEM600 3.5 13.8 1.0 CZ D:TYR358 3.7 11.2 1.0 NE2 D:HIS75 3.8 14.2 1.0 CD2 D:HIS75 3.9 14.0 1.0 O D:HOH623 4.2 17.5 1.0 C2C D:HEM600 4.3 13.7 1.0 C3C D:HEM600 4.3 13.6 1.0 C2D D:HEM600 4.3 13.9 1.0 C3D D:HEM600 4.3 14.0 1.0 C3B D:HEM600 4.3 13.9 1.0 C2B D:HEM600 4.3 14.0 1.0 C3A D:HEM600 4.3 13.4 1.0 C2A D:HEM600 4.3 13.4 1.0 CE2 D:TYR358 4.4 11.2 1.0 CZ D:PHE161 4.5 12.7 1.0 CG2 D:VAL74 4.6 12.3 1.0 CE1 D:TYR358 4.6 11.3 1.0 NH2 D:ARG354 4.6 11.4 1.0 NE D:ARG354 4.6 11.8 1.0 CE1 D:PHE161 4.9 12.8 1.0 CE1 D:HIS75 4.9 14.2 1.0

T.P.Ko, M.K.Safo, F.N.Musayev, M.L.Di Salvo, C.Wang, S.H.Wu, D.J.Abraham. Structure of Human Erythrocyte Catalase. Acta Crystallogr.,Sect.D V. 56 241 2000.
ISSN: ISSN 0907-4449
PubMed: 10666617
DOI: 10.1107/S0907444999015930