Iron in PDB 3v92: S663A Stable-5-Lox

All present enzymatic activity of S663A Stable-5-Lox:
1.13.11.34;

The structure of S663A Stable-5-Lox, PDB code: 3v92 was solved by N.C.Gilbert, Z.Rui, D.B.Neau, M.Waight, S.G.Bartlett, W.E.Boeglin, A.R.Brash, M.E.Newcomer, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	41.47 / 2.74
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	55.191, 202.375, 76.986, 90.00, 109.91, 90.00
R / Rfree (%)	18.3 / 23.8

The binding sites of Iron atom in the S663A Stable-5-Lox (pdb code 3v92). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the S663A Stable-5-Lox, PDB code: 3v92:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the S663A Stable-5-Lox


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of S663A Stable-5-Lox within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe701 b:32.6 occ:1.00 O B:ILE673 2.3 71.5 1.0 NE2 B:HIS372 2.5 35.4 1.0 NE2 B:HIS550 2.5 19.6 1.0 NE2 B:HIS367 2.6 50.4 1.0 CD2 B:HIS372 3.1 25.6 1.0 CD2 B:HIS550 3.2 13.7 1.0 C B:ILE673 3.2 71.9 1.0 OD1 B:ASN554 3.3 49.7 1.0 OXT B:ILE673 3.4 69.7 1.0 CD2 B:HIS367 3.4 39.5 1.0 CE1 B:HIS367 3.5 60.7 1.0 CE1 B:HIS550 3.6 34.4 1.0 CE1 B:HIS372 3.7 42.6 1.0 CG B:ASN554 3.8 38.5 1.0 CB B:ASN554 4.2 27.9 1.0 CG1 B:VAL671 4.3 39.4 1.0 CG B:HIS372 4.4 26.8 1.0 CG B:HIS367 4.4 50.1 1.0 ND1 B:HIS367 4.4 59.9 1.0 CG B:HIS550 4.4 28.2 1.0 ND1 B:HIS550 4.6 38.6 1.0 ND1 B:HIS372 4.7 36.3 1.0 CA B:ILE673 4.7 63.2 1.0 ND2 B:ASN554 4.7 36.5 1.0 CG2 B:ILE673 4.9 54.0 1.0

Iron binding site 2 out of 2 in the S663A Stable-5-Lox


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of S663A Stable-5-Lox within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe701 b:33.3 occ:1.00 OXT A:ILE673 2.3 28.8 1.0 O A:ILE673 2.5 59.8 1.0 NE2 A:HIS372 2.5 15.7 1.0 NE2 A:HIS550 2.6 13.8 1.0 C A:ILE673 2.7 53.6 1.0 NE2 A:HIS367 2.9 50.0 1.0 CD2 A:HIS372 2.9 10.6 1.0 CD2 A:HIS550 3.0 0.9 1.0 OD1 A:ASN554 3.1 33.1 1.0 CE1 A:HIS367 3.3 51.5 1.0 CD2 A:HIS367 3.5 45.7 1.0 CE1 A:HIS372 3.7 31.7 1.0 CG A:ASN554 3.8 18.5 1.0 CE1 A:HIS550 3.8 21.6 1.0 ND1 A:HIS367 4.0 50.2 1.0 CB A:ASN554 4.1 18.8 1.0 CG A:HIS367 4.1 47.4 1.0 CG A:HIS372 4.2 18.9 1.0 CA A:ILE673 4.2 64.3 1.0 CG A:HIS550 4.3 13.5 1.0 CG1 A:VAL671 4.6 25.1 1.0 ND1 A:HIS372 4.6 28.6 1.0 ND1 A:HIS550 4.7 21.2 1.0 OG1 A:THR371 4.8 35.3 1.0 ND2 A:ASN554 4.9 16.0 1.0 CB A:ILE673 4.9 62.2 1.0 N A:ILE673 5.0 65.0 1.0

N.C.Gilbert, Z.Rui, D.B.Neau, M.T.Waight, S.G.Bartlett, W.E.Boeglin, A.R.Brash, M.E.Newcomer. Conversion of Human 5-Lipoxygenase to A 15-Lipoxygenase By A Point Mutation to Mimic Phosphorylation at Serine-663. Faseb J. V. 26 3222 2012.
ISSN: ISSN 0892-6638
PubMed: 22516296
DOI: 10.1096/FJ.12-205286