Zinc in PDB 5ofb: Crystal Structure of Human MORC2 (Residues 1-603) with Spinal Muscular Atrophy Mutation S87L

The structure of Crystal Structure of Human MORC2 (Residues 1-603) with Spinal Muscular Atrophy Mutation S87L, PDB code: 5ofb was solved by C.H.Douse, Y.Liu, Y.Modis, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	79.63 / 2.02
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	69.850, 124.680, 80.360, 90.00, 97.73, 90.00
R / Rfree (%)	19.8 / 22.8

The structure of Crystal Structure of Human MORC2 (Residues 1-603) with Spinal Muscular Atrophy Mutation S87L also contains other interesting chemical elements:

Magnesium

(Mg)

3 atoms

The binding sites of Zinc atom in the Crystal Structure of Human MORC2 (Residues 1-603) with Spinal Muscular Atrophy Mutation S87L (pdb code 5ofb). 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 MORC2 (Residues 1-603) with Spinal Muscular Atrophy Mutation S87L, PDB code: 5ofb:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Crystal Structure of Human MORC2 (Residues 1-603) with Spinal Muscular Atrophy Mutation S87L


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 MORC2 (Residues 1-603) with Spinal Muscular Atrophy Mutation S87L within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn701 b:38.0 occ:1.00 SG B:CYS525 2.3 39.9 1.0 SG B:CYS502 2.3 36.1 1.0 SG B:CYS536 2.3 39.6 1.0 SG B:CYS499 2.3 36.5 1.0 CB B:CYS499 3.1 36.2 1.0 CB B:CYS536 3.2 42.9 1.0 CB B:CYS525 3.2 41.7 1.0 CB B:CYS502 3.3 38.1 1.0 CA B:CYS536 3.5 42.4 1.0 N B:CYS525 3.8 40.6 1.0 N B:CYS502 3.9 38.1 1.0 CA B:CYS525 4.1 41.5 1.0 CA B:CYS502 4.2 39.0 1.0 N B:CYS536 4.2 41.1 1.0 O B:HOH944 4.5 43.3 1.0 CA B:CYS499 4.6 35.3 1.0 CB B:LEU501 4.7 46.9 1.0 C B:CYS536 4.7 45.7 1.0 O B:CYS536 4.8 43.7 1.0 C B:CYS502 4.9 38.5 1.0 NH2 B:ARG506 4.9 40.9 1.0 C B:ARG535 4.9 44.6 1.0 C B:VAL524 5.0 40.9 1.0 C B:LEU501 5.0 43.3 1.0 N B:LEU503 5.0 39.4 1.0

Zinc binding site 2 out of 2 in the Crystal Structure of Human MORC2 (Residues 1-603) with Spinal Muscular Atrophy Mutation S87L


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 MORC2 (Residues 1-603) with Spinal Muscular Atrophy Mutation S87L within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn701 b:48.3 occ:1.00 SG A:CYS502 2.2 51.1 1.0 SG A:CYS525 2.3 54.5 1.0 SG A:CYS536 2.4 59.9 1.0 SG A:CYS499 2.4 48.6 1.0 CB A:CYS499 3.0 48.9 1.0 CB A:CYS536 3.2 62.1 1.0 CB A:CYS502 3.3 53.0 1.0 CB A:CYS525 3.3 54.6 1.0 CA A:CYS536 3.5 64.8 1.0 N A:CYS525 3.8 51.1 1.0 N A:CYS502 3.9 53.2 1.0 CA A:CYS502 4.1 50.6 1.0 CA A:CYS525 4.2 53.8 1.0 N A:CYS536 4.3 65.0 1.0 O A:HOH867 4.5 59.3 1.0 CA A:CYS499 4.5 47.1 1.0 C A:CYS536 4.6 65.2 1.0 O A:CYS536 4.7 63.4 1.0 C A:CYS502 4.8 50.0 1.0 CB A:LEU501 4.8 55.3 1.0 N A:LEU503 4.9 49.6 1.0 NH2 A:ARG506 4.9 54.6 1.0 C A:LEU501 5.0 54.9 1.0 C A:VAL524 5.0 49.3 1.0

C.H.Douse, S.Bloor, Y.Liu, M.Shamin, I.A.Tchasovnikarova, R.T.Timms, P.J.Lehner, Y.Modis. Neuropathic MORC2 Mutations Perturb Ghkl Atpase Dimerization Dynamics and Epigenetic Silencing By Multiple Structural Mechanisms. Nat Commun V. 9 651 2018.
ISSN: ESSN 2041-1723
PubMed: 29440755
DOI: 10.1038/S41467-018-03045-X