Zinc in PDB 7sr2: Crystal Structure of the Human SNX25 Regulator of G-Protein Signalling (Rgs) Domain

The structure of Crystal Structure of the Human SNX25 Regulator of G-Protein Signalling (Rgs) Domain, PDB code: 7sr2 was solved by B.M.Collins, B.Paul, S.Weeratunga, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	41.57 / 2.42
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	44.035, 75.864, 51.109, 90, 109.27, 90
R / Rfree (%)	21.1 / 24.7

The binding sites of Zinc atom in the Crystal Structure of the Human SNX25 Regulator of G-Protein Signalling (Rgs) Domain (pdb code 7sr2). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the Crystal Structure of the Human SNX25 Regulator of G-Protein Signalling (Rgs) Domain, PDB code: 7sr2:

Zinc binding site 1 out of 1 in the Crystal Structure of the Human SNX25 Regulator of G-Protein Signalling (Rgs) Domain


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of the Human SNX25 Regulator of G-Protein Signalling (Rgs) Domain within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn590 b:34.6 occ:1.00 OE1 A:GLU494 1.8 40.7 1.0 NE2 B:HIS486 1.9 41.5 1.0 OE2 B:GLU494 1.9 40.7 1.0 NE2 A:HIS486 2.0 35.4 1.0 CD B:GLU494 2.7 36.9 1.0 OE1 B:GLU494 2.7 51.3 1.0 CE1 B:HIS486 2.8 38.1 1.0 CD A:GLU494 2.8 38.5 1.0 CE1 A:HIS486 2.9 37.3 1.0 CD2 B:HIS486 3.1 34.0 1.0 CD2 A:HIS486 3.1 38.3 1.0 OE2 A:GLU494 3.3 52.1 1.0 ND1 B:HIS486 4.0 43.6 1.0 CG A:GLU494 4.0 30.8 1.0 ND1 A:HIS486 4.1 43.7 1.0 CG B:GLU494 4.1 39.7 1.0 CG B:HIS486 4.1 32.2 1.0 CG A:HIS486 4.2 33.3 1.0 CB B:ALA490 4.2 43.1 1.0 CB A:ALA490 4.3 37.3 1.0 CA B:ALA490 4.5 46.8 1.0 CA A:ALA490 4.6 42.0 1.0 CD1 B:LEU498 4.9 38.9 1.0

S.Weeratunga, B.Paul, W.M.Henne, B.M.Collins. Structures of the Snx-Rgs Proteins Revealed By ALPHAFOLD2 Suggest They Are A New Class of Lipid Transfer Protein To Be Published.