Iron in PDB 8jkr: SP1746 in Complex with Ump

All present enzymatic activity of SP1746 in Complex with Ump:
3.6.1.41;

The structure of SP1746 in Complex with Ump, PDB code: 8jkr was solved by Y.Jin, L.Niu, J.Ke, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.66 / 2.00
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	69.884, 69.884, 87.967, 90, 90, 120
R / Rfree (%)	19.1 / 22.5

The binding sites of Iron atom in the SP1746 in Complex with Ump (pdb code 8jkr). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the SP1746 in Complex with Ump, PDB code: 8jkr:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the SP1746 in Complex with Ump


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of SP1746 in Complex with Ump within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe307 b:33.1 occ:1.00 O A:HOH450 2.0 27.5 1.0 O A:HOH452 2.0 31.2 1.0 NE2 A:HIS117 2.2 33.3 1.0 OD1 A:ASP59 2.2 34.2 1.0 NE2 A:HIS91 2.2 39.0 1.0 O1P A:U5P301 2.2 35.8 1.0 CD2 A:HIS117 3.0 31.6 1.0 CG A:ASP59 3.1 33.9 1.0 CE1 A:HIS91 3.1 41.0 1.0 CD2 A:HIS91 3.2 37.0 1.0 CE1 A:HIS117 3.3 33.3 1.0 OD2 A:ASP59 3.3 32.2 1.0 P A:U5P301 3.3 41.5 1.0 O2P A:U5P301 3.6 41.2 1.0 O A:HOH401 3.7 48.8 1.0 FE A:FE308 3.7 35.2 1.0 OG1 A:THR118 3.7 32.5 1.0 CD2 A:HIS58 4.0 30.5 1.0 CG A:HIS117 4.2 32.1 1.0 O A:HOH456 4.2 42.4 1.0 ND1 A:HIS91 4.3 41.2 1.0 OD2 A:ASP135 4.3 36.2 1.0 ND1 A:HIS117 4.3 34.5 1.0 CG A:HIS91 4.3 41.0 1.0 O3P A:U5P301 4.4 39.6 1.0 O5' A:U5P301 4.4 44.4 1.0 NE2 A:HIS58 4.4 29.0 1.0 CB A:ASP59 4.5 34.3 1.0 C5' A:U5P301 4.6 43.6 1.0 NZ A:LYS62 4.6 46.9 1.0 O A:HIS58 4.8 35.4 1.0 CA A:ASP59 4.9 34.7 1.0 CD A:LYS62 4.9 44.4 1.0 OD1 A:ASP135 5.0 33.9 1.0 CG A:ASP135 5.0 34.7 1.0

Iron binding site 2 out of 2 in the SP1746 in Complex with Ump


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of SP1746 in Complex with Ump within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe308 b:35.2 occ:1.00 O A:HOH450 1.9 27.5 1.0 NE2 A:HIS29 2.0 30.9 1.0 O A:HOH456 2.1 42.4 1.0 OD1 A:ASP135 2.2 33.9 1.0 NE2 A:HIS58 2.2 29.0 1.0 OD2 A:ASP59 2.3 32.2 1.0 CD2 A:HIS29 3.0 31.5 1.0 CE1 A:HIS29 3.0 30.9 1.0 CG A:ASP135 3.1 34.7 1.0 CD2 A:HIS58 3.1 30.5 1.0 CG A:ASP59 3.1 33.9 1.0 CE1 A:HIS58 3.2 29.1 1.0 OD2 A:ASP135 3.4 36.2 1.0 O A:HOH452 3.5 31.2 1.0 O A:HOH401 3.5 48.8 1.0 OD1 A:ASP59 3.6 34.2 1.0 FE A:FE307 3.7 33.1 1.0 NH2 A:ARG26 4.0 56.3 1.0 ND1 A:HIS29 4.1 31.8 1.0 CG A:HIS29 4.2 32.0 1.0 CG A:HIS58 4.2 30.5 1.0 CB A:ASP59 4.2 34.3 1.0 ND1 A:HIS58 4.3 30.2 1.0 O2P A:U5P301 4.3 41.2 1.0 CB A:ASP135 4.3 34.4 1.0 O A:HOH496 4.4 47.5 1.0 CG2 A:VAL33 4.7 28.2 1.0 CD2 A:HIS117 4.8 31.6 1.0 NE2 A:HIS117 4.8 33.3 1.0 CA A:ASP135 4.8 32.5 1.0 O A:ASP135 4.9 34.5 1.0 O1P A:U5P301 4.9 35.8 1.0 P A:U5P301 5.0 41.5 1.0

Y.Jin, J.Ke, L.Niu. Structural and Biochemical Characterization of A Novel Hydrolase From Streptococcus Pneumoniae To Be Published.