Iron in PDB 5jy9: An Iron-Bound Structure of the Salicylate Synthase IRP9

The structure of An Iron-Bound Structure of the Salicylate Synthase IRP9, PDB code: 5jy9 was solved by K.M.Meneely, A.L.Lamb, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	36.52 / 2.16
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	56.392, 145.351, 58.437, 90.00, 108.02, 90.00
R / Rfree (%)	17.2 / 23.5

The binding sites of Iron atom in the An Iron-Bound Structure of the Salicylate Synthase IRP9 (pdb code 5jy9). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the An Iron-Bound Structure of the Salicylate Synthase IRP9, PDB code: 5jy9:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the An Iron-Bound Structure of the Salicylate Synthase IRP9


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of An Iron-Bound Structure of the Salicylate Synthase IRP9 within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe501 b:78.7 occ:1.00 OXT A:ACT503 2.6 42.3 1.0 OE2 A:GLU420 2.7 33.3 1.0 HZ2 A:LYS280 2.9 49.3 1.0 OE2 A:GLU284 2.9 50.6 1.0 OE1 A:GLU284 3.0 46.3 1.0 HZ3 A:LYS280 3.0 49.3 1.0 HZ1 A:LYS280 3.0 49.3 1.0 NZ A:LYS280 3.2 41.1 1.0 O A:ACT503 3.3 31.8 1.0 H A:GLY407 3.3 27.8 1.0 OE1 A:GLU420 3.3 39.1 1.0 CD A:GLU284 3.3 43.8 1.0 CD A:GLU420 3.4 34.9 1.0 C A:ACT503 3.4 27.4 1.0 O A:GLY407 3.7 26.2 1.0 OE1 A:GLU281 3.8 37.1 1.0 HA2 A:GLY257 3.9 30.1 1.0 OE1 A:GLU417 3.9 33.8 1.0 H A:GLY257 3.9 29.1 1.0 N A:GLY407 4.0 23.1 1.0 HA3 A:GLY407 4.1 26.3 1.0 HZ1 A:LYS424 4.1 36.6 1.0 HB1 A:ALA406 4.2 28.9 1.0 HB A:THR258 4.2 33.5 1.0 H A:THR258 4.3 26.9 1.0 HG1 A:THR258 4.3 29.6 1.0 CA A:GLY407 4.4 21.9 1.0 C A:GLY407 4.5 23.3 1.0 HA A:ALA406 4.6 27.8 1.0 N A:GLY257 4.6 24.3 1.0 CA A:GLY257 4.6 25.1 1.0 HZ2 A:LYS424 4.6 36.6 1.0 CE A:LYS280 4.7 37.5 1.0 CD A:GLU281 4.7 30.4 1.0 N A:THR258 4.7 22.4 1.0 OE2 A:GLU417 4.7 37.0 1.0 CD A:GLU417 4.8 33.9 1.0 OE2 A:GLU281 4.8 34.3 1.0 NZ A:LYS424 4.8 30.5 1.0 CH3 A:ACT503 4.8 34.0 1.0 CG A:GLU284 4.9 31.0 1.0 CG A:GLU420 4.9 29.5 1.0 OG1 A:THR258 4.9 24.7 1.0 CB A:THR258 5.0 27.9 1.0 C A:ALA406 5.0 26.4 1.0

Iron binding site 2 out of 2 in the An Iron-Bound Structure of the Salicylate Synthase IRP9


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of An Iron-Bound Structure of the Salicylate Synthase IRP9 within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe501 b:46.8 occ:1.00 O B:HOH602 2.2 28.7 1.0 O B:HOH606 2.3 24.1 1.0 OE2 B:GLU284 2.3 31.1 1.0 O3 B:SO4502 2.4 26.4 1.0 OE2 B:GLU420 2.4 20.9 1.0 O4 B:SO4502 2.5 26.2 1.0 S B:SO4502 3.0 42.8 1.0 CD B:GLU284 3.1 36.8 1.0 OE1 B:GLU284 3.1 35.3 1.0 CD B:GLU420 3.2 31.9 1.0 H B:GLY407 3.3 25.4 1.0 OE1 B:GLU420 3.3 32.0 1.0 HZ3 B:LYS424 3.5 37.7 1.0 H B:GLY257 3.5 28.1 1.0 HA2 B:GLY257 3.6 25.9 1.0 HZ3 B:LYS280 3.7 45.2 1.0 O1 B:SO4502 3.9 35.1 1.0 H B:THR258 3.9 37.1 1.0 HB B:THR258 3.9 30.3 1.0 HZ2 B:LYS280 3.9 45.2 1.0 N B:GLY407 4.0 21.1 1.0 NZ B:LYS280 4.1 37.6 1.0 HZ1 B:LYS280 4.1 45.2 1.0 O2 B:SO4502 4.1 37.0 1.0 HZ1 B:LYS424 4.2 37.7 1.0 HB1 B:ALA406 4.2 31.5 1.0 OE1 B:GLU281 4.2 31.4 1.0 HA B:ALA406 4.2 23.4 1.0 N B:GLY257 4.2 23.4 1.0 NZ B:LYS424 4.3 31.4 1.0 OG1 B:THR258 4.3 24.9 1.0 O B:HOH607 4.3 30.2 1.0 N B:THR258 4.3 30.9 1.0 CA B:GLY257 4.3 21.6 1.0 O B:GLY407 4.3 24.4 1.0 HA3 B:GLY407 4.4 27.3 1.0 OE1 B:GLU417 4.5 34.9 1.0 CG B:GLU284 4.5 25.7 1.0 CB B:THR258 4.5 25.3 1.0 C B:GLY257 4.6 23.9 1.0 CG B:GLU420 4.7 31.1 1.0 CA B:GLY407 4.7 22.7 1.0 O B:HOH621 4.7 30.3 1.0 HG2 B:GLU284 4.7 30.8 1.0 HZ2 B:LYS424 4.8 37.7 1.0 CA B:ALA406 4.8 19.5 1.0 HG2 B:GLU420 4.8 37.3 1.0 HG3 B:GLU284 4.9 30.8 1.0 C B:ALA406 4.9 25.9 1.0 CB B:ALA406 4.9 26.3 1.0 HE3 B:LYS424 4.9 32.9 1.0 HG1 B:THR258 5.0 29.9 1.0 C B:GLY407 5.0 28.3 1.0

K.M.Meneely, J.A.Sundlov, A.M.Gulick, G.R.Moran, A.L.Lamb. An Open and Shut Case: the Interaction of Magnesium with Mst Enzymes. J.Am.Chem.Soc. V. 138 9277 2016.
ISSN: ESSN 1520-5126
PubMed: 27373320
DOI: 10.1021/JACS.6B05134