Iron in PDB 4j1w: Crystal Structure of Fe(II)-Hppe with Alternative Substrate (R)-1-Hpp

The structure of Crystal Structure of Fe(II)-Hppe with Alternative Substrate (R)-1-Hpp, PDB code: 4j1w was solved by C.L.Drennan, M.Dey, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.00 / 2.72
Space group	P 42 21 2
Cell size a, b, c (Å), α, β, γ (°)	111.489, 111.489, 151.484, 90.00, 90.00, 90.00
R / Rfree (%)	24.2 / 27.8

The binding sites of Iron atom in the Crystal Structure of Fe(II)-Hppe with Alternative Substrate (R)-1-Hpp (pdb code 4j1w). 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 Fe(II)-Hppe with Alternative Substrate (R)-1-Hpp, PDB code: 4j1w:
Jump to Iron binding site number: 1; 2; 3;

Iron binding site 1 out of 3 in the Crystal Structure of Fe(II)-Hppe with Alternative Substrate (R)-1-Hpp


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 Fe(II)-Hppe with Alternative Substrate (R)-1-Hpp within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe201 b:55.5 occ:1.00 O3 A:FFQ202 2.1 80.1 1.0 O1 A:FFQ202 2.1 79.6 1.0 NE2 A:HIS138 2.2 56.9 1.0 OE1 A:GLU142 2.2 55.5 1.0 NE2 A:HIS180 2.3 53.8 1.0 P1 A:FFQ202 3.1 80.5 1.0 C2 A:FFQ202 3.1 79.7 1.0 CD A:GLU142 3.1 53.8 1.0 CD2 A:HIS138 3.1 57.8 1.0 CE1 A:HIS180 3.2 52.8 1.0 CE1 A:HIS138 3.2 57.3 1.0 OE2 A:GLU142 3.3 55.7 1.0 CD2 A:HIS180 3.3 52.8 1.0 O A:HOH309 3.6 65.3 1.0 O4 A:FFQ202 3.8 80.5 1.0 ND2 A:ASN135 3.9 73.5 1.0 OD1 A:ASN197 4.3 57.6 1.0 C1 A:FFQ202 4.3 79.4 1.0 O2 A:FFQ202 4.3 79.5 1.0 CG A:HIS138 4.3 59.6 1.0 ND1 A:HIS138 4.3 58.5 1.0 ND1 A:HIS180 4.4 53.5 1.0 CG A:HIS180 4.5 52.4 1.0 CG A:GLU142 4.5 51.0 1.0 CB A:GLU142 4.8 49.5 1.0

Iron binding site 2 out of 3 in the Crystal Structure of Fe(II)-Hppe with Alternative Substrate (R)-1-Hpp


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 Fe(II)-Hppe with Alternative Substrate (R)-1-Hpp within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe201 b:51.0 occ:1.00 O4 B:FFQ202 2.2 79.6 1.0 OE1 B:GLU142 2.2 53.2 1.0 NE2 B:HIS180 2.2 50.7 1.0 NE2 B:HIS138 2.3 54.7 1.0 O1 B:FFQ202 2.4 77.7 1.0 CD B:GLU142 3.1 51.7 1.0 P1 B:FFQ202 3.2 79.6 1.0 CE1 B:HIS180 3.2 50.0 1.0 CD2 B:HIS138 3.2 56.2 1.0 CD2 B:HIS180 3.2 49.8 1.0 OE2 B:GLU142 3.2 52.5 1.0 C2 B:FFQ202 3.3 78.6 1.0 CE1 B:HIS138 3.3 55.9 1.0 O B:HOH309 3.4 61.9 1.0 O2 B:FFQ202 3.8 80.8 1.0 ND2 B:ASN135 3.9 72.6 1.0 OD1 B:ASN197 4.3 53.9 1.0 ND1 B:HIS180 4.3 50.9 1.0 CG B:HIS180 4.4 49.8 1.0 CG B:HIS138 4.4 57.9 1.0 ND1 B:HIS138 4.4 56.7 1.0 O3 B:FFQ202 4.4 80.0 1.0 CG B:GLU142 4.5 49.1 1.0 C1 B:FFQ202 4.5 78.0 1.0 CB B:GLU142 4.8 48.1 1.0

Iron binding site 3 out of 3 in the Crystal Structure of Fe(II)-Hppe with Alternative Substrate (R)-1-Hpp


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 Fe(II)-Hppe with Alternative Substrate (R)-1-Hpp within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe201 b:50.2 occ:1.00 O2 C:FFQ202 1.9 47.3 1.0 OE1 C:GLU142 2.2 50.5 1.0 NE2 C:HIS138 2.2 54.9 1.0 O1 C:FFQ202 2.3 48.0 1.0 NE2 C:HIS180 2.4 50.0 1.0 P1 C:FFQ202 2.9 47.0 1.0 CD C:GLU142 3.0 50.2 1.0 C2 C:FFQ202 3.1 47.5 1.0 OE2 C:GLU142 3.2 50.1 1.0 CD2 C:HIS138 3.2 56.0 1.0 CE1 C:HIS138 3.2 55.5 1.0 CE1 C:HIS180 3.3 49.7 1.0 CD2 C:HIS180 3.4 49.4 1.0 O3 C:FFQ202 3.9 48.2 1.0 ND2 C:ASN135 4.0 71.6 1.0 O4 C:FFQ202 4.2 47.6 1.0 OD1 C:ASN197 4.2 54.0 1.0 C1 C:FFQ202 4.3 47.2 1.0 CG C:HIS138 4.4 57.2 1.0 ND1 C:HIS138 4.4 56.7 1.0 CG C:GLU142 4.4 48.3 1.0 ND1 C:HIS180 4.5 51.0 1.0 CG C:HIS180 4.5 49.4 1.0 CB C:GLU142 4.8 46.6 1.0

W.C.Chang, M.Dey, P.Liu, S.O.Mansoorabadi, S.J.Moon, Z.K.Zhao, C.L.Drennan, H.W.Liu. Mechanistic Studies of An Unprecedented Enzyme-Catalysed 1,2-Phosphono-Migration Reaction. Nature V. 496 114 2013.
ISSN: ISSN 0028-0836
PubMed: 23552950
DOI: 10.1038/NATURE11998