Iron in PDB 1dgg: Human Erythrocyte Catalse Cyanide Complex

All present enzymatic activity of Human Erythrocyte Catalse Cyanide Complex:
1.11.1.6;

The structure of Human Erythrocyte Catalse Cyanide Complex, PDB code: 1dgg was solved by C.D.Putnam, A.S.Arvai, Y.Bourne, J.A.Tainer, 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 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	83.862, 140.608, 231.591, 90.00, 90.00, 90.00
R / Rfree (%)	17.8 / 22.1

The binding sites of Iron atom in the Human Erythrocyte Catalse Cyanide Complex (pdb code 1dgg). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 4 binding sites of Iron where determined in the Human Erythrocyte Catalse Cyanide Complex, PDB code: 1dgg:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in the Human Erythrocyte Catalse Cyanide Complex


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Human Erythrocyte Catalse Cyanide Complex within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe2000 b:40.3 occ:1.00 FE A:HEM2000 0.0 40.3 1.0 C A:CYN4000 1.6 39.9 1.0 OH A:TYR358 1.7 38.0 1.0 NB A:HEM2000 1.8 39.9 1.0 NA A:HEM2000 2.0 39.9 1.0 ND A:HEM2000 2.1 40.0 1.0 NC A:HEM2000 2.1 40.0 1.0 N A:CYN4000 2.6 40.6 1.0 C1B A:HEM2000 2.8 39.9 1.0 CZ A:TYR358 2.9 38.2 1.0 C4B A:HEM2000 2.9 39.9 1.0 C4A A:HEM2000 3.0 40.0 1.0 C1C A:HEM2000 3.1 39.8 1.0 C1A A:HEM2000 3.1 40.0 1.0 C4D A:HEM2000 3.1 39.9 1.0 C1D A:HEM2000 3.1 39.9 1.0 C4C A:HEM2000 3.1 39.9 1.0 CHB A:HEM2000 3.3 39.9 1.0 CHC A:HEM2000 3.4 40.0 1.0 CHA A:HEM2000 3.5 40.0 1.0 CHD A:HEM2000 3.5 39.9 1.0 CE1 A:TYR358 3.6 38.1 1.0 CE2 A:TYR358 3.8 38.1 1.0 NH2 A:ARG354 3.9 37.1 1.0 NE A:ARG354 4.0 37.4 1.0 C2B A:HEM2000 4.1 39.9 1.0 C3B A:HEM2000 4.1 39.8 1.0 C3A A:HEM2000 4.3 40.0 1.0 C2A A:HEM2000 4.3 40.1 1.0 C3D A:HEM2000 4.3 40.0 1.0 C2C A:HEM2000 4.3 39.8 1.0 C2D A:HEM2000 4.3 39.9 1.0 C3C A:HEM2000 4.4 39.9 1.0 CZ A:ARG354 4.4 37.4 1.0 O A:HOH4256 4.4 58.0 1.0 CZ A:PHE161 4.6 39.0 1.0 NE2 A:HIS75 4.6 38.2 1.0 CD2 A:HIS75 4.9 38.1 1.0 CD1 A:TYR358 4.9 37.9 1.0 CG2 A:VAL74 4.9 37.6 1.0 CD A:ARG354 5.0 37.5 1.0

Iron binding site 2 out of 4 in the Human Erythrocyte Catalse Cyanide Complex


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Human Erythrocyte Catalse Cyanide Complex within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe2001 b:39.5 occ:1.00 FE B:HEM2001 0.0 39.5 1.0 C B:CYN4001 1.6 39.3 1.0 OH B:TYR358 1.8 37.9 1.0 ND B:HEM2001 1.9 39.4 1.0 NA B:HEM2001 1.9 39.3 1.0 NB B:HEM2001 2.0 39.1 1.0 NC B:HEM2001 2.1 39.4 1.0 N B:CYN4001 2.7 40.0 1.0 C4D B:HEM2001 2.9 39.3 1.0 CZ B:TYR358 2.9 38.0 1.0 C4A B:HEM2001 2.9 39.1 1.0 C1A B:HEM2001 2.9 39.2 1.0 C1D B:HEM2001 2.9 39.4 1.0 C1B B:HEM2001 3.0 39.0 1.0 C4C B:HEM2001 3.1 39.2 1.0 C4B B:HEM2001 3.1 39.2 1.0 C1C B:HEM2001 3.1 39.2 1.0 CHA B:HEM2001 3.3 39.3 1.0 CHB B:HEM2001 3.3 39.1 1.0 CHD B:HEM2001 3.4 39.3 1.0 CHC B:HEM2001 3.5 39.2 1.0 CE1 B:TYR358 3.6 38.0 1.0 CE2 B:TYR358 3.9 38.0 1.0 NH2 B:ARG354 4.0 38.4 1.0 NE B:ARG354 4.0 38.9 1.0 C2D B:HEM2001 4.2 39.3 1.0 C3D B:HEM2001 4.2 39.5 1.0 C3A B:HEM2001 4.2 39.0 1.0 C2A B:HEM2001 4.2 39.2 1.0 C2B B:HEM2001 4.2 39.1 1.0 C3B B:HEM2001 4.3 39.2 1.0 C3C B:HEM2001 4.3 39.2 1.0 C2C B:HEM2001 4.4 39.1 1.0 O B:HOH4055 4.4 59.1 1.0 CZ B:ARG354 4.4 38.7 1.0 CZ B:PHE161 4.7 38.2 1.0 NE2 B:HIS75 4.7 37.8 1.0 CD2 B:HIS75 4.8 37.7 1.0 CG2 B:VAL74 4.9 37.5 1.0 CD1 B:TYR358 4.9 38.0 1.0

Iron binding site 3 out of 4 in the Human Erythrocyte Catalse Cyanide Complex


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Human Erythrocyte Catalse Cyanide Complex within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe2002 b:39.4 occ:1.00 FE C:HEM2002 0.0 39.4 1.0 C C:CYN4002 1.6 39.8 1.0 OH C:TYR358 1.8 39.3 1.0 ND C:HEM2002 1.8 39.6 1.0 NC C:HEM2002 1.9 39.6 1.0 NB C:HEM2002 2.0 39.6 1.0 NA C:HEM2002 2.0 39.6 1.0 N C:CYN4002 2.7 40.5 1.0 C4D C:HEM2002 2.9 39.5 1.0 C1D C:HEM2002 2.9 39.5 1.0 CZ C:TYR358 2.9 39.3 1.0 C4C C:HEM2002 2.9 39.6 1.0 C1C C:HEM2002 3.0 39.4 1.0 C1A C:HEM2002 3.0 39.5 1.0 C4B C:HEM2002 3.0 39.5 1.0 C1B C:HEM2002 3.1 39.4 1.0 C4A C:HEM2002 3.1 39.5 1.0 CHA C:HEM2002 3.3 39.5 1.0 CHD C:HEM2002 3.3 39.5 1.0 CHC C:HEM2002 3.4 39.5 1.0 CHB C:HEM2002 3.5 39.5 1.0 CE1 C:TYR358 3.7 39.3 1.0 CE2 C:TYR358 3.9 39.2 1.0 NH2 C:ARG354 4.1 38.1 1.0 NE C:ARG354 4.1 38.3 1.0 C2D C:HEM2002 4.1 39.6 1.0 C3D C:HEM2002 4.1 39.8 1.0 C3C C:HEM2002 4.2 39.6 1.0 C2C C:HEM2002 4.2 39.4 1.0 C2A C:HEM2002 4.3 39.4 1.0 C2B C:HEM2002 4.3 39.3 1.0 C3B C:HEM2002 4.3 39.4 1.0 C3A C:HEM2002 4.3 39.3 1.0 O C:HOH4180 4.4 40.8 1.0 CZ C:ARG354 4.4 38.2 1.0 CZ C:PHE161 4.6 39.1 1.0 CG2 C:VAL74 4.6 38.3 1.0 NE2 C:HIS75 4.6 38.3 1.0 CD2 C:HIS75 4.7 38.3 1.0 CD1 C:TYR358 5.0 39.1 1.0

Iron binding site 4 out of 4 in the Human Erythrocyte Catalse Cyanide Complex


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Human Erythrocyte Catalse Cyanide Complex within 5.0Å range: probe atom residue distance (Å) B Occ D:Fe2003 b:38.6 occ:1.00 FE D:HEM2003 0.0 38.6 1.0 C D:CYN4003 1.6 39.4 1.0 OH D:TYR358 1.8 36.5 1.0 ND D:HEM2003 1.9 39.5 1.0 NC D:HEM2003 1.9 39.4 1.0 NB D:HEM2003 2.0 39.4 1.0 NA D:HEM2003 2.1 39.4 1.0 N D:CYN4003 2.8 39.9 1.0 C1D D:HEM2003 2.9 39.3 1.0 CZ D:TYR358 2.9 36.6 1.0 C4C D:HEM2003 2.9 39.3 1.0 C4B D:HEM2003 3.0 39.4 1.0 C1C D:HEM2003 3.0 39.2 1.0 C4D D:HEM2003 3.0 39.3 1.0 C1B D:HEM2003 3.0 39.2 1.0 C1A D:HEM2003 3.1 39.2 1.0 C4A D:HEM2003 3.1 39.2 1.0 CHD D:HEM2003 3.3 39.2 1.0 CHC D:HEM2003 3.3 39.3 1.0 CHA D:HEM2003 3.4 39.2 1.0 CHB D:HEM2003 3.5 39.2 1.0 CE1 D:TYR358 3.7 36.6 1.0 CE2 D:TYR358 3.8 36.6 1.0 NE D:ARG354 4.0 39.1 1.0 NH2 D:ARG354 4.0 39.1 1.0 C2D D:HEM2003 4.1 39.2 1.0 C3D D:HEM2003 4.2 39.3 1.0 C2C D:HEM2003 4.2 39.1 1.0 C3C D:HEM2003 4.2 39.3 1.0 C3B D:HEM2003 4.2 39.3 1.0 C2B D:HEM2003 4.2 39.1 1.0 C2A D:HEM2003 4.3 39.1 1.0 C3A D:HEM2003 4.3 39.0 1.0 CZ D:ARG354 4.4 39.1 1.0 O D:HOH4068 4.4 46.6 1.0 CZ D:PHE161 4.6 39.1 1.0 NE2 D:HIS75 4.7 38.3 1.0 CG2 D:VAL74 4.8 38.3 1.0 CD2 D:HIS75 4.8 38.2 1.0 CD D:ARG354 4.9 39.1 1.0 CD1 D:TYR358 5.0 36.7 1.0

C.D.Putnam, A.S.Arvai, Y.Bourne, J.A.Tainer. Active and Inhibited Human Catalase Structures: Ligand and Nadph Binding and Catalytic Mechanism. J.Mol.Biol. V. 296 295 2000.
ISSN: ISSN 0022-2836
PubMed: 10656833
DOI: 10.1006/JMBI.1999.3458