Zinc in PDB 2n5k: Regnase-1 Zinc Finger Domain

The binding sites of Zinc atom in the Regnase-1 Zinc Finger Domain (pdb code 2n5k). 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 Regnase-1 Zinc Finger Domain, PDB code: 2n5k:

Zinc binding site 1 out of 1 in the Regnase-1 Zinc Finger Domain


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Regnase-1 Zinc Finger Domain within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn400 b:21.5 occ:1.00 HE2 A:HIS322 1.5 0.0 1.0 NE2 A:HIS322 2.1 14.1 1.0 SG A:CYS318 2.3 32.4 1.0 SG A:CYS312 2.3 50.2 1.0 SG A:CYS306 2.3 22.1 1.0 CE1 A:HIS322 2.7 24.4 1.0 HE1 A:HIS322 2.7 44.5 1.0 HB2 A:CYS318 2.9 0.0 1.0 HB2 A:CYS312 3.1 0.0 1.0 CB A:CYS312 3.1 71.5 1.0 CB A:CYS318 3.1 12.0 1.0 CD2 A:HIS322 3.2 12.4 1.0 HB3 A:CYS312 3.2 44.5 1.0 HB3 A:CYS306 3.2 11.1 1.0 HD2 A:TYR314 3.4 53.3 1.0 HD2 A:PRO307 3.4 0.0 1.0 CB A:CYS306 3.4 45.2 1.0 H A:GLY309 3.5 20.2 1.0 HB3 A:CYS318 3.5 3.2 1.0 HD2 A:HIS322 3.7 64.5 1.0 HB2 A:TYR314 3.7 0.0 1.0 ND1 A:HIS322 3.8 2.5 1.0 H A:GLY315 3.8 50.3 1.0 HB2 A:CYS306 3.9 0.0 1.0 HA2 A:GLY309 4.0 0.5 1.0 CG A:HIS322 4.1 41.1 1.0 HB2 A:PHE320 4.2 0.0 1.0 H A:TYR308 4.3 2.4 1.0 N A:GLY309 4.3 73.2 1.0 CD2 A:TYR314 4.4 72.4 1.0 CD A:PRO307 4.5 3.0 1.0 CA A:CYS318 4.5 52.1 1.0 HG2 A:PRO307 4.6 0.0 1.0 HD1 A:HIS322 4.6 32.5 1.0 HB2 A:TYR308 4.6 0.0 1.0 HA A:CYS318 4.6 32.4 1.0 CA A:CYS312 4.6 31.4 1.0 CA A:GLY309 4.6 41.4 1.0 N A:GLY315 4.7 43.1 1.0 CA A:CYS306 4.7 12.5 1.0 HA A:CYS306 4.8 61.1 1.0 CB A:TYR314 4.8 71.2 1.0 H A:PHE320 4.8 62.5 1.0 HA2 A:GLY315 4.8 0.3 1.0 O A:GLY309 4.8 31.1 1.0 HA A:CYS312 4.9 30.1 1.0 H A:TYR314 4.9 71.4 1.0

M.Yokogawa, T.Tsushima, N.N.Noda, H.Kumeta, Y.Enokizono, K.Yamashita, D.M.Standley, O.Takeuchi, S.Akira, F.Inagaki. Structural Basis For the Regulation of Enzymatic Activity of Regnase-1 By Domain-Domain Interactions Sci Rep V. 6 22324 2016.
ISSN: ESSN 2045-2322
PubMed: 26927947
DOI: 10.1038/SREP22324