Zinc in PDB 7dg2: NSE1-NSE3-NSE4 Complex

All present enzymatic activity of NSE1-NSE3-NSE4 Complex:
2.3.2.27;

The structure of NSE1-NSE3-NSE4 Complex, PDB code: 7dg2 was solved by Y.Cho, A.Jo, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	41.59 / 1.70
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	53.486, 66.161, 168.367, 90, 90, 90
R / Rfree (%)	19 / 21.8

The binding sites of Zinc atom in the NSE1-NSE3-NSE4 Complex (pdb code 7dg2). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the NSE1-NSE3-NSE4 Complex, PDB code: 7dg2:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the NSE1-NSE3-NSE4 Complex


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of NSE1-NSE3-NSE4 Complex within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn304 b:31.4 occ:1.00 ND1 A:HIS206 2.1 26.1 1.0 SG A:CYS188 2.2 34.8 1.0 SG A:CYS185 2.3 28.5 1.0 SG A:CYS209 2.4 35.0 1.0 CB A:CYS185 3.0 27.8 1.0 CE1 A:HIS206 3.1 30.5 1.0 CG A:HIS206 3.1 26.2 1.0 CB A:CYS188 3.3 34.0 1.0 CB A:CYS209 3.4 39.3 1.0 CB A:HIS206 3.4 27.9 1.0 N A:CYS188 3.8 34.4 1.0 N A:HIS206 4.0 26.5 1.0 CA A:CYS188 4.1 34.1 1.0 NE2 A:HIS206 4.2 25.3 1.0 CD2 A:HIS206 4.3 26.6 1.0 CA A:HIS206 4.3 31.8 1.0 CA A:CYS185 4.5 26.3 1.0 CA A:CYS209 4.8 39.4 1.0 CB A:VAL187 4.8 34.4 1.0 C A:CYS188 4.8 36.9 1.0 C A:VAL187 4.8 39.3 1.0 N A:ARG189 5.0 32.5 1.0

Zinc binding site 2 out of 2 in the NSE1-NSE3-NSE4 Complex


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of NSE1-NSE3-NSE4 Complex within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn305 b:27.8 occ:1.00 SG A:CYS222 2.3 32.5 1.0 SG A:CYS201 2.3 26.6 1.0 SG A:CYS225 2.4 27.8 1.0 SG A:CYS198 2.4 29.0 1.0 CB A:CYS198 3.1 28.1 1.0 CB A:CYS222 3.2 36.7 1.0 CB A:CYS225 3.3 37.0 1.0 CB A:CYS201 3.3 29.6 1.0 N A:CYS225 3.7 35.3 1.0 N A:CYS201 3.8 27.2 1.0 CA A:CYS225 4.0 38.3 1.0 CA A:CYS201 4.1 28.8 1.0 CG1 A:ILE203 4.3 27.8 1.0 CB A:ASN224 4.5 35.8 1.0 CA A:CYS198 4.6 25.3 1.0 C A:ASN224 4.6 41.1 1.0 CA A:CYS222 4.6 39.2 1.0 C A:CYS201 4.7 32.7 1.0 C A:CYS225 4.7 36.3 1.0 CB A:ASN200 4.7 32.5 1.0 ND2 A:ASN200 4.8 33.8 1.0 ND2 A:ASN224 4.8 36.6 1.0 N A:GLY202 4.8 28.1 1.0 C A:ASN200 4.9 30.6 1.0 N A:ASN226 4.9 40.6 1.0 CA A:ASN224 4.9 40.1 1.0 N A:ASN224 4.9 41.0 1.0

A.Jo, S.Li, J.W.Shin, X.Zhao, Y.Cho. Structure Basis For Shaping the NSE4 Protein By the NSE1 and NSE3 Dimer Within the SMC5/6 Complex. J.Mol.Biol. V. 433 66910 2021.
ISSN: ESSN 1089-8638
PubMed: 33676928
DOI: 10.1016/J.JMB.2021.166910