Magnesium in PDB 4ygy: Crystal Structure of Human SCP1 Bound to Trans-Proline Peptidomimetic Ctd Phospho-SER5 Peptide

All present enzymatic activity of Crystal Structure of Human SCP1 Bound to Trans-Proline Peptidomimetic Ctd Phospho-SER5 Peptide:
3.1.3.16;

The structure of Crystal Structure of Human SCP1 Bound to Trans-Proline Peptidomimetic Ctd Phospho-SER5 Peptide, PDB code: 4ygy was solved by J.E.Mayfield, Y.Zhang, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	64.86 / 2.36
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	125.280, 78.335, 63.031, 90.00, 112.59, 90.00
R / Rfree (%)	18.3 / 24.6

The binding sites of Magnesium atom in the Crystal Structure of Human SCP1 Bound to Trans-Proline Peptidomimetic Ctd Phospho-SER5 Peptide (pdb code 4ygy). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Crystal Structure of Human SCP1 Bound to Trans-Proline Peptidomimetic Ctd Phospho-SER5 Peptide, PDB code: 4ygy:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Crystal Structure of Human SCP1 Bound to Trans-Proline Peptidomimetic Ctd Phospho-SER5 Peptide


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 Human SCP1 Bound to Trans-Proline Peptidomimetic Ctd Phospho-SER5 Peptide within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg301 b:51.3 occ:1.00 O06 C:4CG5 1.8 51.1 1.0 O A:ASP98 2.0 40.5 1.0 OD1 A:ASN96 2.1 39.7 1.0 O A:HOH412 2.2 46.1 1.0 O A:HOH411 2.3 39.4 1.0 OD1 A:ASN207 2.6 46.4 1.0 CG A:ASN96 3.1 38.8 1.0 C A:ASP98 3.1 39.4 1.0 P05 C:4CG5 3.3 52.7 1.0 ND2 A:ASN96 3.4 35.7 1.0 CG A:ASN207 3.5 47.7 1.0 CA A:ASP98 3.8 39.3 1.0 ND2 A:ASN207 3.9 47.5 1.0 N A:ASP98 3.9 35.3 1.0 O08 C:4CG5 4.0 54.3 1.0 O07 C:4CG5 4.0 41.7 1.0 CB A:ASP98 4.0 46.1 1.0 OG1 A:THR100 4.1 35.2 1.0 OD1 A:ASP206 4.2 49.6 1.0 N A:GLU99 4.2 39.1 1.0 OE1 A:GLU99 4.3 40.7 1.0 CB A:GLU99 4.3 48.2 1.0 O04 C:4CG5 4.4 58.8 1.0 CB A:ASN96 4.5 39.1 1.0 C A:LEU97 4.6 35.6 1.0 N A:THR100 4.6 48.8 1.0 CA A:GLU99 4.7 44.9 1.0 C03 C:4CG5 4.7 68.0 1.0 C A:GLU99 4.9 49.3 1.0 CB A:ASN207 4.9 46.8 1.0 CB A:THR100 4.9 37.7 1.0 CG A:ASP206 5.0 47.1 1.0

Magnesium binding site 2 out of 2 in the Crystal Structure of Human SCP1 Bound to Trans-Proline Peptidomimetic Ctd Phospho-SER5 Peptide


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 Human SCP1 Bound to Trans-Proline Peptidomimetic Ctd Phospho-SER5 Peptide within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg301 b:55.8 occ:1.00 O08 D:4CG5 1.9 53.8 1.0 O B:HOH411 2.1 54.4 1.0 O B:HOH408 2.1 40.0 1.0 O B:ASP98 2.4 34.5 1.0 ND2 B:ASN96 2.5 34.3 1.0 OD1 B:ASN207 2.5 36.0 1.0 O D:HOH101 2.7 53.7 1.0 CG B:ASN207 3.3 32.6 1.0 ND2 B:ASN207 3.3 36.6 1.0 P05 D:4CG5 3.4 53.3 1.0 C B:ASP98 3.5 36.0 1.0 CG B:ASN96 3.6 38.6 1.0 OD1 B:ASN96 4.0 31.5 1.0 O06 D:4CG5 4.0 44.9 1.0 OE1 B:GLU99 4.0 40.9 1.0 O04 D:4CG5 4.2 59.1 1.0 CA B:ASP98 4.2 32.9 1.0 OD1 B:ASP206 4.2 42.2 1.0 CB B:ASP98 4.3 34.5 1.0 CB B:GLU99 4.3 35.4 1.0 N B:ASP98 4.3 33.9 1.0 O07 D:4CG5 4.3 48.1 1.0 N B:GLU99 4.6 34.5 1.0 OG1 B:THR100 4.6 34.8 1.0 CB B:ASN207 4.8 31.4 1.0 CA B:GLU99 4.8 34.0 1.0 CB B:ASN96 4.9 34.1 1.0 CD B:GLU99 4.9 38.0 1.0 C03 D:4CG5 5.0 72.2 1.0

J.E.Mayfield, S.Fan, S.Wei, M.Zhang, B.Li, A.D.Ellington, F.A.Etzkorn, Y.J.Zhang. Chemical Tools to Decipher Regulation of Phosphatases By Proline Isomerization on Eukaryotic Rna Polymerase II. Acs Chem.Biol. V. 10 2405 2015.
ISSN: ESSN 1554-8937
PubMed: 26332362
DOI: 10.1021/ACSCHEMBIO.5B00296