Iron in PDB 8jkp: SP1746 in Complex with Dtmp

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

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

Resolution Low / High (Å)	19.41 / 2.10
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	68.919, 68.919, 88.332, 90, 90, 120
R / Rfree (%)	16.9 / 20.8

The binding sites of Iron atom in the SP1746 in Complex with Dtmp (pdb code 8jkp). 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 Dtmp, PDB code: 8jkp:
Jump to Iron binding site number: 1; 2;

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


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 Dtmp within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe303 b:24.6 occ:1.00 NE2 A:HIS29 2.0 23.5 1.0 O A:HOH457 2.0 22.5 1.0 NE2 A:HIS58 2.0 22.9 1.0 O A:HOH418 2.1 30.9 1.0 OD1 A:ASP135 2.1 22.9 1.0 OD2 A:ASP59 2.1 22.0 1.0 CD2 A:HIS58 2.9 21.7 1.0 CD2 A:HIS29 3.0 24.1 1.0 CG A:ASP59 3.0 21.4 1.0 CE1 A:HIS29 3.0 23.2 1.0 CE1 A:HIS58 3.1 23.0 1.0 CG A:ASP135 3.1 22.4 1.0 OD1 A:ASP59 3.4 21.4 1.0 OD2 A:ASP135 3.6 22.4 1.0 FE A:FE304 3.8 22.5 1.0 O A:HOH417 3.8 26.5 1.0 NH2 A:ARG26 4.1 40.4 1.0 CB A:ASP59 4.1 22.6 1.0 O3P A:TMP301 4.1 32.4 1.0 CG A:HIS58 4.1 22.2 1.0 ND1 A:HIS29 4.1 23.0 1.0 CG A:HIS29 4.1 23.1 1.0 ND1 A:HIS58 4.2 21.4 1.0 O A:HOH507 4.3 52.2 1.0 CB A:ASP135 4.4 21.9 1.0 CG2 A:VAL33 4.6 20.8 1.0 NE2 A:HIS117 4.6 20.5 1.0 CD2 A:HIS117 4.7 19.2 1.0 O2P A:TMP301 4.9 27.4 1.0 CA A:ASP135 4.9 21.1 1.0 O A:ASP135 5.0 21.2 1.0 P A:TMP301 5.0 31.9 1.0

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


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 Dtmp within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe304 b:22.5 occ:1.00 NE2 A:HIS117 2.0 20.5 1.0 O A:HOH417 2.0 26.5 1.0 NE2 A:HIS91 2.0 22.3 1.0 O A:HOH457 2.1 22.5 1.0 OD1 A:ASP59 2.1 21.4 1.0 O2P A:TMP301 2.1 27.4 1.0 CD2 A:HIS117 3.0 19.2 1.0 CE1 A:HIS91 3.0 22.8 1.0 CE1 A:HIS117 3.0 20.2 1.0 CD2 A:HIS91 3.1 22.4 1.0 CG A:ASP59 3.1 21.4 1.0 P A:TMP301 3.3 31.9 1.0 OD2 A:ASP59 3.4 22.0 1.0 O3P A:TMP301 3.5 32.4 1.0 OG1 A:THR118 3.7 21.1 1.0 FE A:FE303 3.8 24.6 1.0 CD2 A:HIS58 4.0 21.7 1.0 ND1 A:HIS117 4.1 19.7 1.0 CG A:HIS117 4.2 19.4 1.0 ND1 A:HIS91 4.2 22.9 1.0 CG A:HIS91 4.2 22.9 1.0 O A:HOH418 4.2 30.9 1.0 O1P A:TMP301 4.3 31.7 1.0 OD2 A:ASP135 4.4 22.4 1.0 NE2 A:HIS58 4.4 22.9 1.0 O5' A:TMP301 4.5 33.1 1.0 CB A:ASP59 4.5 22.6 1.0 NZ A:LYS62 4.7 36.2 1.0 O A:HIS58 4.7 23.9 1.0 CA A:ASP59 4.8 24.0 1.0 OD1 A:ASP135 4.8 22.9 1.0 C5' A:TMP301 4.9 34.1 1.0 CD A:LYS62 4.9 33.9 1.0 CG A:ASP135 5.0 22.4 1.0

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