Iron in PDB 8jka: SP1746 in Complex with Amp

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

The structure of SP1746 in Complex with Amp, PDB code: 8jka 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)	50.01 / 2.25
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	69.557, 69.557, 88.539, 90, 90, 120
R / Rfree (%)	18 / 23.1

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

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


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 Amp within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe402 b:36.7 occ:1.00 O A:HOH524 1.9 31.1 1.0 NE2 A:HIS29 2.0 31.5 1.0 NE2 A:HIS58 2.1 29.1 1.0 OD2 A:ASP59 2.2 30.7 1.0 OD1 A:ASP135 2.2 35.4 1.0 O A:HOH501 2.7 33.7 1.0 CE1 A:HIS29 3.0 29.8 1.0 CD2 A:HIS58 3.0 26.2 1.0 CG A:ASP59 3.0 30.9 1.0 CD2 A:HIS29 3.1 32.5 1.0 CG A:ASP135 3.1 33.7 1.0 CE1 A:HIS58 3.1 28.3 1.0 OD1 A:ASP59 3.4 33.0 1.0 OD2 A:ASP135 3.4 35.3 1.0 O A:HOH518 3.4 29.4 1.0 FE A:FE403 3.7 32.8 1.0 O1P A:AMP404 3.8 52.8 1.0 NH2 A:ARG26 4.0 62.5 1.0 ND1 A:HIS29 4.1 29.9 1.0 CG A:HIS58 4.2 25.9 1.0 CG A:HIS29 4.2 32.0 1.0 ND1 A:HIS58 4.2 26.5 1.0 CB A:ASP59 4.3 30.7 1.0 CB A:ASP135 4.4 33.0 1.0 O A:HOH568 4.4 42.6 1.0 P A:AMP404 4.7 64.1 1.0 O2P A:AMP404 4.7 45.0 1.0 NE2 A:HIS117 4.8 32.0 1.0 CG2 A:VAL33 4.8 26.6 1.0 CD2 A:HIS117 4.8 30.9 1.0 O A:ASP135 4.9 31.7 1.0 CA A:ASP135 4.9 31.2 1.0

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


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 Amp within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe403 b:32.8 occ:1.00 O A:HOH518 1.9 29.4 1.0 O A:HOH524 2.1 31.1 1.0 OD1 A:ASP59 2.1 33.0 1.0 NE2 A:HIS91 2.1 37.0 1.0 NE2 A:HIS117 2.1 32.0 1.0 O2P A:AMP404 2.2 45.0 1.0 CD2 A:HIS117 3.0 30.9 1.0 CD2 A:HIS91 3.1 33.2 1.0 CE1 A:HIS91 3.1 36.2 1.0 CG A:ASP59 3.1 30.9 1.0 CE1 A:HIS117 3.2 31.2 1.0 P A:AMP404 3.3 64.1 1.0 OD2 A:ASP59 3.5 30.7 1.0 O1P A:AMP404 3.6 52.8 1.0 FE A:FE402 3.7 36.7 1.0 OG1 A:THR118 3.7 32.6 1.0 O A:HOH501 3.8 33.7 1.0 CD2 A:HIS58 3.9 26.2 1.0 CG A:HIS117 4.2 31.1 1.0 CG A:HIS91 4.2 36.5 1.0 ND1 A:HIS91 4.2 39.0 1.0 ND1 A:HIS117 4.3 32.3 1.0 NE2 A:HIS58 4.3 29.1 1.0 O3P A:AMP404 4.4 58.5 1.0 OD2 A:ASP135 4.4 35.3 1.0 O5' A:AMP404 4.4 60.5 1.0 CB A:ASP59 4.5 30.7 1.0 C5' A:AMP404 4.6 59.9 1.0 O A:HIS58 4.8 30.9 1.0 CA A:ASP59 4.8 31.9 1.0 CD A:LYS62 4.9 42.6 1.0 OD1 A:ASP135 5.0 35.4 1.0 CB A:THR118 5.0 31.5 1.0 CG A:ASP135 5.0 33.7 1.0

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