Magnesium in PDB 4e2p: Crystal Structure of A Post-Tailoring Hydroxylase (Hmtn) Involved in the Himastatin Biosynthesis

The structure of Crystal Structure of A Post-Tailoring Hydroxylase (Hmtn) Involved in the Himastatin Biosynthesis, PDB code: 4e2p was solved by H.D.Zhang, J.Chen, H.Wang, L.Huang, H.J.Zhang, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	18.38 / 2.36
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	56.140, 72.290, 103.290, 90.00, 90.00, 90.00
R / Rfree (%)	23.9 / 28

The structure of Crystal Structure of A Post-Tailoring Hydroxylase (Hmtn) Involved in the Himastatin Biosynthesis also contains other interesting chemical elements:

Iron

(Fe)

1 atom

The binding sites of Magnesium atom in the Crystal Structure of A Post-Tailoring Hydroxylase (Hmtn) Involved in the Himastatin Biosynthesis (pdb code 4e2p). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 4 binding sites of Magnesium where determined in the Crystal Structure of A Post-Tailoring Hydroxylase (Hmtn) Involved in the Himastatin Biosynthesis, PDB code: 4e2p:
Jump to Magnesium binding site number: 1; 2; 3; 4;

Magnesium binding site 1 out of 4 in the Crystal Structure of A Post-Tailoring Hydroxylase (Hmtn) Involved in the Himastatin Biosynthesis


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure of A Post-Tailoring Hydroxylase (Hmtn) Involved in the Himastatin Biosynthesis within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg402 b:26.8 occ:1.00 CD2 A:PHE69 4.2 28.1 1.0 CG A:PHE69 4.3 27.4 1.0 CB A:PHE69 4.3 26.8 1.0 CE2 A:PHE69 4.8 28.5 1.0

Magnesium binding site 2 out of 4 in the Crystal Structure of A Post-Tailoring Hydroxylase (Hmtn) Involved in the Himastatin Biosynthesis


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Crystal Structure of A Post-Tailoring Hydroxylase (Hmtn) Involved in the Himastatin Biosynthesis within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg403 b:21.9 occ:1.00 OG1 A:THR70 2.5 23.8 1.0 OG A:SER58 2.5 21.0 1.0 NE2 A:HIS56 3.1 19.4 1.0 O A:HOH601 3.1 15.8 1.0 CE1 A:HIS56 3.2 19.1 1.0 CB A:SER58 3.2 21.4 1.0 CG2 A:THR70 3.5 23.5 1.0 CB A:THR70 3.5 23.4 1.0 CD2 A:HIS56 4.1 19.2 1.0 ND1 A:HIS56 4.2 18.7 1.0 CD2 A:PHE69 4.5 28.1 1.0 N A:THR70 4.6 24.4 1.0 CA A:SER58 4.6 21.3 1.0 CA A:THR70 4.6 23.4 1.0 CG A:HIS56 4.7 18.8 1.0 N A:SER58 4.9 20.4 1.0

Magnesium binding site 3 out of 4 in the Crystal Structure of A Post-Tailoring Hydroxylase (Hmtn) Involved in the Himastatin Biosynthesis


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Crystal Structure of A Post-Tailoring Hydroxylase (Hmtn) Involved in the Himastatin Biosynthesis within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg404 b:13.5 occ:1.00 O A:HOH612 2.7 13.3 1.0 CB A:TYR255 3.6 16.7 1.0 CB A:GLU257 3.6 18.4 1.0 CG A:GLN258 3.6 17.0 1.0 N A:GLN258 3.6 17.3 1.0 N A:GLU257 3.7 18.0 1.0 CA A:TYR255 3.8 17.0 1.0 C A:TYR255 3.8 17.2 1.0 CA A:GLU257 4.0 18.1 1.0 CD A:GLN258 4.0 16.7 1.0 N A:PRO256 4.1 17.6 1.0 CE A:MET1 4.1 23.6 1.0 CD1 A:TYR255 4.2 16.8 1.0 O A:TYR255 4.2 17.0 1.0 CD A:PRO256 4.2 17.9 1.0 CB A:GLN258 4.2 16.7 1.0 CG A:GLU257 4.2 18.9 1.0 C A:GLU257 4.3 17.7 1.0 OE1 A:GLN258 4.3 16.9 1.0 CG A:TYR255 4.4 16.6 1.0 CA A:GLN258 4.5 16.9 1.0 NE2 A:GLN258 4.7 16.5 1.0 C A:PRO256 4.7 17.8 1.0 O A:HOH524 4.9 13.2 1.0 CA A:PRO256 5.0 17.8 1.0

Magnesium binding site 4 out of 4 in the Crystal Structure of A Post-Tailoring Hydroxylase (Hmtn) Involved in the Himastatin Biosynthesis


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 4 of Crystal Structure of A Post-Tailoring Hydroxylase (Hmtn) Involved in the Himastatin Biosynthesis within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg405 b:30.0 occ:1.00 O A:HOH642 2.9 14.7 1.0 O A:HOH580 3.1 18.4 1.0 CB A:MET354 3.8 16.3 1.0 CA A:MET354 3.8 15.9 1.0 NE A:ARG357 3.9 16.7 1.0 N A:MET354 4.0 15.6 1.0 CG A:MET354 4.2 16.8 1.0 NH2 A:ARG357 4.4 16.9 1.0 C A:ARG353 4.6 15.4 1.0 CZ A:ARG357 4.6 16.8 1.0 O A:PRO350 4.6 15.3 1.0 CG1 A:VAL98 4.6 17.6 1.0 O A:HOH574 4.6 17.8 1.0 O A:HOH641 4.7 16.7 1.0 CD A:ARG357 4.7 16.4 1.0 O A:ARG353 4.9 15.4 1.0 CB A:ARG353 4.9 15.4 1.0 O A:HOH576 4.9 12.4 1.0

H.D.Zhang, J.Chen, H.Wang, L.Huang, H.J.Zhang. Crystal Structure of A Post-Tailoring Hydroxylase (Hmtn) Involved in the Himastatin Biosynthesis To Be Published.