Zinc in PDB 7sp0: Crystal Structure of Human Sfpq L534I Mutant in Complex with Zinc

The structure of Crystal Structure of Human Sfpq L534I Mutant in Complex with Zinc, PDB code: 7sp0 was solved by M.Lee, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	45.96 / 1.83
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	61.607, 62.717, 67.793, 90, 96.08, 90
R / Rfree (%)	17.9 / 21.6

The binding sites of Zinc atom in the Crystal Structure of Human Sfpq L534I Mutant in Complex with Zinc (pdb code 7sp0). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Crystal Structure of Human Sfpq L534I Mutant in Complex with Zinc, PDB code: 7sp0:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Crystal Structure of Human Sfpq L534I Mutant in Complex with Zinc


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 Human Sfpq L534I Mutant in Complex with Zinc within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn601 b:22.4 occ:1.00 NE2 A:HIS483 2.0 20.7 1.0 NE2 B:HIS530 2.1 20.0 1.0 CE1 B:HIS530 3.0 23.6 1.0 CE1 A:HIS483 3.0 23.2 1.0 CD2 A:HIS483 3.1 21.7 1.0 CD2 B:HIS530 3.1 19.8 1.0 ND1 B:HIS530 4.1 25.0 1.0 ND1 A:HIS483 4.1 22.9 1.0 CG A:HIS483 4.2 22.7 1.0 CG B:HIS530 4.2 19.9 1.0 O A:HOH749 4.5 25.8 1.0

Zinc binding site 2 out of 2 in the Crystal Structure of Human Sfpq L534I Mutant in Complex with Zinc


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Crystal Structure of Human Sfpq L534I Mutant in Complex with Zinc within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn601 b:28.1 occ:0.50 ND1 B:HIS483 2.1 29.2 0.5 OE1 B:GLU489 2.1 24.4 1.0 CE1 B:HIS483 2.6 30.8 0.5 CD B:GLU489 2.9 27.1 1.0 OE2 B:GLU489 3.2 27.1 1.0 CG B:HIS483 3.4 29.9 0.5 NE2 B:HIS483 3.8 30.5 0.5 N B:GLY484 4.1 24.0 1.0 CB B:HIS483 4.1 29.3 0.5 CE2 B:TYR488 4.1 28.4 1.0 CD2 B:HIS483 4.2 29.8 0.5 CB B:HIS483 4.3 34.8 0.5 CG B:GLU489 4.3 24.5 1.0 CD2 B:TYR488 4.5 24.4 1.0 CA B:HIS483 4.5 27.8 0.5 CA B:HIS483 4.5 29.8 0.5 C B:HIS483 4.7 27.6 1.0 CA B:GLY484 4.7 23.8 1.0 CG B:HIS483 4.9 37.2 0.5 CD2 B:HIS483 4.9 41.3 0.5

J.Widagdo, S.Udagedara, N.Bhembre, J.Z.A.Tan, L.Neureiter, J.Huang, V.Anggono, M.Lee. Familial Als-Associated Sfpq Variants Promote the Formation of Sfpq Cytoplasmic Aggregates in Primary Neurons. Open Biology V. 12 20187 2022.
ISSN: ESSN 2046-2441
PubMed: 36168806
DOI: 10.1098/RSOB.220187