Iron in PDB 3u52: X-Ray Crystal Structure of Xenon-Pressurized Phenol Hydroxylase From Pseudomonas Sp. OX1

The structure of X-Ray Crystal Structure of Xenon-Pressurized Phenol Hydroxylase From Pseudomonas Sp. OX1, PDB code: 3u52 was solved by M.S.Mccormick, S.J.Lippard, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	38.00 / 1.95
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	83.942, 141.761, 181.207, 90.00, 90.00, 90.00
R / Rfree (%)	18.3 / 22.8

The structure of X-Ray Crystal Structure of Xenon-Pressurized Phenol Hydroxylase From Pseudomonas Sp. OX1 also contains other interesting chemical elements:

Xenon	(Xe)	24 atoms
Zinc	(Zn)	2 atoms
Copper	(Cu)	2 atoms

The binding sites of Iron atom in the X-Ray Crystal Structure of Xenon-Pressurized Phenol Hydroxylase From Pseudomonas Sp. OX1 (pdb code 3u52). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 4 binding sites of Iron where determined in the X-Ray Crystal Structure of Xenon-Pressurized Phenol Hydroxylase From Pseudomonas Sp. OX1, PDB code: 3u52:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in the X-Ray Crystal Structure of Xenon-Pressurized Phenol Hydroxylase From Pseudomonas Sp. OX1


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of X-Ray Crystal Structure of Xenon-Pressurized Phenol Hydroxylase From Pseudomonas Sp. OX1 within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe512 b:33.4 occ:1.00 OE2 A:GLU138 2.2 28.2 1.0 OE2 A:GLU108 2.3 24.6 1.0 ND1 A:HIS141 2.4 23.5 1.0 O2 A:GOL516 2.5 37.9 1.0 O A:HOH531 2.8 28.1 1.0 CD A:GLU138 3.1 25.4 1.0 CD A:GLU108 3.1 27.8 1.0 CE1 A:HIS141 3.3 22.9 1.0 OE1 A:GLU108 3.3 30.7 1.0 CG A:HIS141 3.4 22.3 1.0 OE1 A:GLU138 3.4 29.9 1.0 FE A:FE513 3.5 34.6 1.0 CB A:HIS141 3.7 17.6 1.0 C2 A:GOL516 3.8 40.1 1.0 OE1 A:GLU233 3.8 39.4 1.0 O A:HOH597 3.9 40.1 1.0 NE2 A:HIS141 4.4 24.1 1.0 CG A:GLU138 4.5 18.1 1.0 CD2 A:HIS141 4.5 22.2 1.0 CG A:GLU108 4.5 18.6 1.0 CA A:GLU138 4.6 17.8 1.0 O1 A:GOL516 4.7 44.6 1.0 CD A:GLU233 4.7 36.1 1.0 O3 A:GOL516 4.7 43.7 1.0 C3 A:GOL516 4.8 40.5 1.0 OE1 A:GLU199 4.8 34.6 1.0 CB A:GLU138 4.8 17.6 1.0 C1 A:GOL516 4.8 39.7 1.0 OE2 A:GLU233 4.8 35.7 1.0 CB A:GLU108 4.9 20.0 1.0 ND1 A:HIS236 4.9 19.0 1.0 CE1 A:HIS236 5.0 19.6 1.0

Iron binding site 2 out of 4 in the X-Ray Crystal Structure of Xenon-Pressurized Phenol Hydroxylase From Pseudomonas Sp. OX1


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of X-Ray Crystal Structure of Xenon-Pressurized Phenol Hydroxylase From Pseudomonas Sp. OX1 within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe513 b:34.6 occ:1.00 OE2 A:GLU233 2.0 35.7 1.0 OE1 A:GLU199 2.1 34.6 1.0 ND1 A:HIS236 2.4 19.0 1.0 OE1 A:GLU233 2.5 39.4 1.0 CD A:GLU233 2.6 36.1 1.0 O A:HOH597 2.8 40.1 1.0 CD A:GLU199 3.0 36.0 1.0 OE2 A:GLU199 3.2 41.8 1.0 CE1 A:HIS236 3.3 19.6 1.0 OE1 A:GLU138 3.3 29.9 1.0 CG A:HIS236 3.4 19.5 1.0 FE A:FE512 3.5 33.4 1.0 CB A:HIS236 3.7 19.6 1.0 NE2 A:GLN134 4.0 25.8 1.0 O2 A:GOL516 4.0 37.9 1.0 CD A:GLU138 4.2 25.4 1.0 CG A:GLU233 4.2 31.7 1.0 CE1 A:HIS141 4.2 22.9 1.0 OE2 A:GLU138 4.3 28.2 1.0 CG A:GLU199 4.4 31.3 1.0 NE2 A:HIS236 4.4 17.6 1.0 ND1 A:HIS141 4.4 23.5 1.0 O1 A:GOL516 4.5 44.6 1.0 O A:HOH532 4.5 36.6 1.0 CD2 A:HIS236 4.5 16.6 1.0 CA A:GLU233 4.8 27.4 1.0 O A:HOH531 4.8 28.1 1.0 CB A:GLU233 4.9 27.6 1.0

Iron binding site 3 out of 4 in the X-Ray Crystal Structure of Xenon-Pressurized Phenol Hydroxylase From Pseudomonas Sp. OX1


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of X-Ray Crystal Structure of Xenon-Pressurized Phenol Hydroxylase From Pseudomonas Sp. OX1 within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe512 b:31.4 occ:1.00 OE1 B:GLU108 2.0 28.3 1.0 OE2 B:GLU138 2.2 30.1 1.0 O B:HOH532 2.3 28.7 1.0 ND1 B:HIS141 2.3 18.1 1.0 O2 B:GOL519 2.6 43.6 1.0 CD B:GLU108 3.0 28.2 1.0 CE1 B:HIS141 3.1 20.9 1.0 CD B:GLU138 3.2 24.3 1.0 OE2 B:GLU108 3.3 33.5 1.0 CG B:HIS141 3.4 18.8 1.0 OE1 B:GLU138 3.4 32.9 1.0 FE B:FE513 3.5 36.5 1.0 O B:HOH533 3.5 40.6 1.0 C2 B:GOL519 3.8 45.7 1.0 CB B:HIS141 3.8 17.2 1.0 OE2 B:GLU233 3.9 35.4 1.0 NE2 B:HIS141 4.3 20.7 1.0 O B:HOH578 4.4 53.6 1.0 CG B:GLU108 4.5 24.2 1.0 CD2 B:HIS141 4.5 18.4 1.0 CG B:GLU138 4.5 21.2 1.0 O3 B:GOL519 4.6 50.2 1.0 O1 B:GOL519 4.6 45.8 1.0 CA B:GLU138 4.7 17.9 1.0 C3 B:GOL519 4.7 46.6 1.0 C1 B:GOL519 4.8 45.6 1.0 CB B:GLU108 4.9 20.6 1.0 CE1 B:HIS236 4.9 24.2 1.0 CD B:GLU233 4.9 33.4 1.0 OE2 B:GLU199 4.9 41.8 1.0 CB B:GLU138 4.9 17.8 1.0 ND1 B:HIS236 4.9 24.4 1.0

Iron binding site 4 out of 4 in the X-Ray Crystal Structure of Xenon-Pressurized Phenol Hydroxylase From Pseudomonas Sp. OX1


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of X-Ray Crystal Structure of Xenon-Pressurized Phenol Hydroxylase From Pseudomonas Sp. OX1 within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe513 b:36.5 occ:1.00 OE1 B:GLU233 2.2 35.0 1.0 OE2 B:GLU199 2.2 41.8 1.0 ND1 B:HIS236 2.3 24.4 1.0 O B:HOH533 2.4 40.6 1.0 OE2 B:GLU233 2.6 35.4 1.0 CD B:GLU233 2.7 33.4 1.0 CD B:GLU199 3.0 36.5 1.0 OE1 B:GLU199 3.1 42.8 1.0 CE1 B:HIS236 3.2 24.2 1.0 OE1 B:GLU138 3.3 32.9 1.0 CG B:HIS236 3.4 24.7 1.0 FE B:FE512 3.5 31.4 1.0 CB B:HIS236 3.7 25.0 1.0 O2 B:GOL519 4.0 43.6 1.0 O B:HOH532 4.1 28.7 1.0 NE2 B:GLN134 4.2 27.3 1.0 CD B:GLU138 4.2 24.3 1.0 CE1 B:HIS141 4.2 20.9 1.0 CG B:GLU233 4.3 30.5 1.0 OE2 B:GLU138 4.3 30.1 1.0 CG B:GLU199 4.4 33.1 1.0 NE2 B:HIS236 4.4 24.4 1.0 O B:HOH581 4.4 40.1 1.0 CD2 B:HIS236 4.5 23.2 1.0 ND1 B:HIS141 4.6 18.1 1.0 O1 B:GOL519 4.6 45.8 1.0 CA B:GLU233 4.8 30.0 1.0 O B:HOH578 4.9 53.6 1.0 CB B:GLU233 5.0 30.2 1.0

M.S.Mccormick, S.J.Lippard. Analysis of Substrate Access to Active Sites in Bacterial Multicomponent Monooxygenase Hydroxylases: X-Ray Crystal Structure of Xenon-Pressurized Phenol Hydroxylase From Pseudomonas Sp. OX1. Biochemistry V. 50 11058 2011.
ISSN: ISSN 0006-2960
PubMed: 22136180
DOI: 10.1021/BI201248B