Iron in PDB 1zz8: Crystal Structure of Feii Hppe in Complex with Substrate Form 2

The structure of Crystal Structure of Feii Hppe in Complex with Substrate Form 2, PDB code: 1zz8 was solved by L.J.Higgins, F.Yan, P.Liu, H.W.Liu, C.L.Drennan, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.00 / 2.30
Space group	P 42 21 2
Cell size a, b, c (Å), α, β, γ (°)	111.649, 111.649, 152.069, 90.00, 90.00, 90.00
R / Rfree (%)	22.5 / 25.2

The binding sites of Iron atom in the Crystal Structure of Feii Hppe in Complex with Substrate Form 2 (pdb code 1zz8). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 3 binding sites of Iron where determined in the Crystal Structure of Feii Hppe in Complex with Substrate Form 2, PDB code: 1zz8:
Jump to Iron binding site number: 1; 2; 3;

Iron binding site 1 out of 3 in the Crystal Structure of Feii Hppe in Complex with Substrate Form 2


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 Feii Hppe in Complex with Substrate Form 2 within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe199 b:31.2 occ:1.00 O14 A:S0H1001 2.1 32.1 1.0 OE2 A:GLU142 2.2 32.5 1.0 NE2 A:HIS138 2.4 35.7 1.0 NE2 A:HIS180 2.4 36.1 1.0 O6 A:S0H1001 2.6 34.3 1.0 O A:HOH1039 3.0 40.8 1.0 CD2 A:HIS138 3.1 37.2 1.0 CD A:GLU142 3.1 34.8 1.0 P1 A:S0H1001 3.3 33.8 1.0 CE1 A:HIS180 3.3 36.8 1.0 C3 A:S0H1001 3.4 35.5 1.0 CD2 A:HIS180 3.5 35.9 1.0 OE1 A:GLU142 3.5 34.1 1.0 CE1 A:HIS138 3.5 38.4 1.0 C2 A:S0H1001 3.6 34.2 1.0 O B:HOH1031 3.9 53.4 1.0 O13 A:S0H1001 3.9 33.5 1.0 ND2 A:ASN135 4.1 41.3 1.0 CG A:HIS138 4.3 38.4 1.0 OD1 A:ASN197 4.4 42.0 1.0 O15 A:S0H1001 4.4 33.6 1.0 C1 A:S0H1001 4.4 38.5 1.0 ND1 A:HIS180 4.4 36.2 1.0 CG A:GLU142 4.5 31.6 1.0 ND1 A:HIS138 4.5 37.4 1.0 CG A:HIS180 4.6 35.9 1.0 CB A:GLU142 4.8 30.2 1.0

Iron binding site 2 out of 3 in the Crystal Structure of Feii Hppe in Complex with Substrate Form 2


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 Feii Hppe in Complex with Substrate Form 2 within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe199 b:29.0 occ:1.00 O15 B:S0H1003 1.9 31.9 1.0 OE1 B:GLU142 2.1 29.3 1.0 NE2 B:HIS180 2.3 28.0 1.0 NE2 B:HIS138 2.3 28.5 1.0 O6 B:S0H1003 2.5 25.9 1.0 CD B:GLU142 3.0 31.1 1.0 CD2 B:HIS138 3.2 30.2 1.0 CE1 B:HIS180 3.2 30.2 1.0 P1 B:S0H1003 3.3 31.6 1.0 OE2 B:GLU142 3.3 30.7 1.0 CD2 B:HIS180 3.3 29.8 1.0 CE1 B:HIS138 3.4 30.1 1.0 C3 B:S0H1003 3.5 31.9 1.0 C2 B:S0H1003 3.7 30.5 1.0 O14 B:S0H1003 3.7 31.6 1.0 ND2 B:ASN135 4.1 41.8 1.0 ND1 B:HIS180 4.4 29.8 1.0 CG B:HIS138 4.4 32.9 1.0 CG B:GLU142 4.4 28.9 1.0 O13 B:S0H1003 4.4 32.7 1.0 C1 B:S0H1003 4.4 32.3 1.0 CG B:HIS180 4.4 29.1 1.0 ND1 B:HIS138 4.5 31.0 1.0 OD1 B:ASN197 4.5 26.4 1.0 CB B:GLU142 4.7 28.2 1.0

Iron binding site 3 out of 3 in the Crystal Structure of Feii Hppe in Complex with Substrate Form 2


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 Feii Hppe in Complex with Substrate Form 2 within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe199 b:29.9 occ:1.00 O14 C:S0H1002 1.9 33.8 1.0 OE1 C:GLU142 2.2 26.2 1.0 NE2 C:HIS138 2.4 29.1 1.0 NE2 C:HIS180 2.4 29.9 1.0 O6 C:S0H1002 2.4 30.0 1.0 O C:HOH1060 2.9 26.6 1.0 CD C:GLU142 3.1 26.8 1.0 P1 C:S0H1002 3.2 33.8 1.0 CD2 C:HIS138 3.2 30.8 1.0 CD2 C:HIS180 3.3 31.0 1.0 CE1 C:HIS180 3.3 29.4 1.0 OE2 C:GLU142 3.3 27.1 1.0 CE1 C:HIS138 3.4 30.4 1.0 C3 C:S0H1002 3.5 32.5 1.0 C2 C:S0H1002 3.6 33.7 1.0 O13 C:S0H1002 3.9 35.2 1.0 ND2 C:ASN135 4.1 32.9 1.0 O15 C:S0H1002 4.2 34.9 1.0 C1 C:S0H1002 4.3 29.6 1.0 CG C:HIS138 4.4 29.4 1.0 ND1 C:HIS180 4.5 29.9 1.0 CG C:HIS180 4.5 29.8 1.0 ND1 C:HIS138 4.5 30.6 1.0 CG C:GLU142 4.5 24.9 1.0 OD1 C:ASN197 4.5 34.5 1.0 CB C:GLU142 4.9 25.0 1.0

L.J.Higgins, F.Yan, P.Liu, H.W.Liu, C.L.Drennan. Structural Insight Into Antibiotic Fosfomycin Biosynthesis By A Mononuclear Iron Enzyme Nature V. 437 838 2005.
ISSN: ISSN 0028-0836
PubMed: 16015285
DOI: 10.1038/NATURE03924