Nickel in PDB 5ln5: Crystal Structure of the WSS1 E203Q Mutant From S. Pombe

The structure of Crystal Structure of the WSS1 E203Q Mutant From S. Pombe, PDB code: 5ln5 was solved by M.Groll, J.Stingele, S.J.Boulton, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	15.00 / 1.75
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	41.160, 57.260, 50.640, 90.00, 113.01, 90.00
R / Rfree (%)	17.3 / 19.5

The binding sites of Nickel atom in the Crystal Structure of the WSS1 E203Q Mutant From S. Pombe (pdb code 5ln5). This binding sites where shown within 5.0 Angstroms radius around Nickel atom.
In total 2 binding sites of Nickel where determined in the Crystal Structure of the WSS1 E203Q Mutant From S. Pombe, PDB code: 5ln5:
Jump to Nickel binding site number: 1; 2;

Nickel binding site 1 out of 2 in the Crystal Structure of the WSS1 E203Q Mutant From S. Pombe


Mono view


Stereo pair view

A full contact list of Nickel with other atoms in the Ni binding site number 1 of Crystal Structure of the WSS1 E203Q Mutant From S. Pombe within 5.0Å range: probe atom residue distance (Å) B Occ A:Ni201 b:53.5 occ:1.00 NE2 A:HIS101 2.2 42.3 1.0 NE2 A:HIS97 2.2 48.1 1.0 NE2 A:HIS107 2.3 74.5 1.0 C A:CO3202 2.3 50.3 1.0 O3 A:CO3202 2.4 52.6 1.0 O1 A:CO3202 2.6 48.0 1.0 O2 A:CO3202 2.7 55.0 1.0 CE1 A:HIS107 2.9 78.8 1.0 CD2 A:HIS101 3.1 41.0 1.0 CD2 A:HIS97 3.1 41.2 1.0 CE1 A:HIS101 3.2 44.8 1.0 CE1 A:HIS97 3.2 52.8 1.0 CD2 A:HIS107 3.4 76.2 1.0 ND1 A:HIS107 4.1 82.2 1.0 CG A:HIS101 4.2 39.3 1.0 ND1 A:HIS101 4.3 41.6 1.0 CG A:HIS97 4.3 41.6 1.0 ND1 A:HIS97 4.3 51.0 1.0 CG A:HIS107 4.4 80.2 1.0 CZ A:PHE111 4.8 44.3 1.0 NE2 A:GLN98 4.8 28.9 1.0 CE1 A:PHE111 4.9 40.9 1.0 OE1 A:GLN98 4.9 35.8 1.0 O A:HOH323 4.9 47.8 1.0

Nickel binding site 2 out of 2 in the Crystal Structure of the WSS1 E203Q Mutant From S. Pombe


Mono view


Stereo pair view

A full contact list of Nickel with other atoms in the Ni binding site number 2 of Crystal Structure of the WSS1 E203Q Mutant From S. Pombe within 5.0Å range: probe atom residue distance (Å) B Occ B:Ni201 b:29.2 occ:1.00 O B:HOH334 2.1 39.2 1.0 NE2 B:HIS97 2.1 29.8 1.0 NE2 B:HIS101 2.2 26.6 1.0 O B:HOH358 2.2 32.3 1.0 NE2 B:HIS107 2.2 34.2 1.0 O B:HOH311 2.3 31.1 1.0 CD2 B:HIS101 3.1 26.8 1.0 CE1 B:HIS97 3.1 32.6 1.0 CD2 B:HIS97 3.1 26.4 1.0 CE1 B:HIS107 3.1 38.4 1.0 CE1 B:HIS101 3.2 28.5 1.0 CD2 B:HIS107 3.3 35.4 1.0 O B:HOH337 4.0 40.2 1.0 ND1 B:HIS97 4.2 30.6 1.0 CG B:HIS101 4.2 24.7 1.0 CG B:HIS97 4.3 24.6 1.0 ND1 B:HIS101 4.3 27.4 1.0 ND1 B:HIS107 4.3 41.2 1.0 CG B:HIS107 4.4 36.6 1.0 O B:HOH340 4.4 33.5 1.0 NE2 B:GLN98 4.6 20.0 1.0 CZ B:PHE111 4.7 25.1 1.0 CE1 B:PHE111 4.8 26.3 1.0

J.Stingele, R.Bellelli, F.Alte, G.Hewitt, G.Sarek, S.L.Maslen, S.E.Tsutakawa, A.Borg, S.Kjr, J.A.Tainer, J.M.Skehel, M.Groll, S.J.Boulton. Mechanism and Regulation of Dna-Protein Crosslink Repair By the Dna-Dependent Metalloprotease Sprtn. Mol.Cell V. 64 688 2016.
ISSN: ISSN 1097-2765
PubMed: 27871365
DOI: 10.1016/J.MOLCEL.2016.09.031