Zinc in PDB 2eod: Solution Structure of Traf-Type Zinc Finger Domains (190- 248) From Human Tnf Receptor-Associated Factor 4

The binding sites of Zinc atom in the Solution Structure of Traf-Type Zinc Finger Domains (190- 248) From Human Tnf Receptor-Associated Factor 4 (pdb code 2eod). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Solution Structure of Traf-Type Zinc Finger Domains (190- 248) From Human Tnf Receptor-Associated Factor 4, PDB code: 2eod:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Solution Structure of Traf-Type Zinc Finger Domains (190- 248) From Human Tnf Receptor-Associated Factor 4


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Solution Structure of Traf-Type Zinc Finger Domains (190- 248) From Human Tnf Receptor-Associated Factor 4 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn300 b:0.0 occ:1.00 NE2 A:HIS210 2.0 0.0 1.0 SG A:CYS214 2.3 0.0 1.0 SG A:CYS198 2.3 0.0 1.0 SG A:CYS195 2.3 0.0 1.0 H A:CYS198 2.8 0.0 1.0 CE1 A:HIS210 2.8 0.0 1.0 HE1 A:HIS210 2.9 0.0 1.0 HB2 A:CYS214 2.9 0.0 1.0 HB3 A:CYS195 3.0 0.0 1.0 CB A:CYS195 3.1 0.0 1.0 HB2 A:TYR197 3.1 0.0 1.0 HB2 A:CYS195 3.2 0.0 1.0 CB A:CYS214 3.2 0.0 1.0 CD2 A:HIS210 3.2 0.0 1.0 HB3 A:CYS198 3.2 0.0 1.0 CB A:CYS198 3.4 0.0 1.0 HD2 A:TYR197 3.5 0.0 1.0 HD2 A:HIS210 3.6 0.0 1.0 N A:CYS198 3.6 0.0 1.0 HB3 A:CYS214 3.8 0.0 1.0 ND1 A:HIS210 4.0 0.0 1.0 CA A:CYS198 4.1 0.0 1.0 HA A:CYS214 4.2 0.0 1.0 CG A:HIS210 4.2 0.0 1.0 CB A:TYR197 4.2 0.0 1.0 HB2 A:CYS198 4.2 0.0 1.0 H A:TYR197 4.3 0.0 1.0 HE2 A:PHE202 4.3 0.0 1.0 CA A:CYS214 4.3 0.0 1.0 CD2 A:TYR197 4.5 0.0 1.0 HA A:GLN211 4.6 0.0 1.0 CA A:CYS195 4.6 0.0 1.0 HD2 A:PHE202 4.7 0.0 1.0 HD2 A:PRO215 4.7 0.0 1.0 HD12 A:ILE207 4.7 0.0 1.0 C A:TYR197 4.7 0.0 1.0 CE2 A:PHE202 4.7 0.0 1.0 HB3 A:TYR197 4.8 0.0 1.0 H A:LYS200 4.8 0.0 1.0 HB2 A:LYS200 4.8 0.0 1.0 HD1 A:HIS210 4.8 0.0 1.0 CG A:TYR197 4.9 0.0 1.0 CA A:TYR197 4.9 0.0 1.0 N A:TYR197 4.9 0.0 1.0 HA A:CYS198 4.9 0.0 1.0 HA A:CYS195 4.9 0.0 1.0 CD2 A:PHE202 4.9 0.0 1.0 H A:THR199 5.0 0.0 1.0 H A:CYS214 5.0 0.0 1.0 HD11 A:ILE207 5.0 0.0 1.0 HB2 A:ARG216 5.0 0.0 1.0

Zinc binding site 2 out of 2 in the Solution Structure of Traf-Type Zinc Finger Domains (190- 248) From Human Tnf Receptor-Associated Factor 4


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Solution Structure of Traf-Type Zinc Finger Domains (190- 248) From Human Tnf Receptor-Associated Factor 4 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn400 b:0.0 occ:1.00 NE2 A:HIS238 2.0 0.0 1.0 SG A:CYS225 2.3 0.0 1.0 SG A:CYS221 2.3 0.0 1.0 SG A:CYS243 2.3 0.0 1.0 CE1 A:HIS238 2.9 0.0 1.0 HB2 A:CYS243 3.0 0.0 1.0 HA A:CYS243 3.1 0.0 1.0 HE1 A:HIS238 3.1 0.0 1.0 CB A:CYS243 3.1 0.0 1.0 CD2 A:HIS238 3.1 0.0 1.0 HB3 A:CYS225 3.2 0.0 1.0 HB2 A:ASN223 3.3 0.0 1.0 HB2 A:CYS221 3.4 0.0 1.0 CB A:CYS225 3.4 0.0 1.0 CB A:CYS221 3.4 0.0 1.0 HD2 A:HIS238 3.5 0.0 1.0 H A:CYS225 3.5 0.0 1.0 HG11 A:VAL227 3.5 0.0 1.0 HB3 A:CYS221 3.6 0.0 1.0 CA A:CYS243 3.6 0.0 1.0 H A:ASN244 4.0 0.0 1.0 HG12 A:VAL227 4.1 0.0 1.0 HB2 A:CYS225 4.1 0.0 1.0 HD21 A:ASN223 4.1 0.0 1.0 ND1 A:HIS238 4.1 0.0 1.0 HB3 A:CYS243 4.1 0.0 1.0 HD23 A:LEU239 4.2 0.0 1.0 CG A:HIS238 4.2 0.0 1.0 CG1 A:VAL227 4.3 0.0 1.0 HD21 A:LEU239 4.3 0.0 1.0 N A:CYS225 4.3 0.0 1.0 H A:ASN223 4.4 0.0 1.0 CB A:ASN223 4.4 0.0 1.0 CA A:CYS225 4.5 0.0 1.0 N A:CYS243 4.5 0.0 1.0 H A:CYS243 4.6 0.0 1.0 H A:GLY226 4.6 0.0 1.0 HB3 A:ASN223 4.6 0.0 1.0 HA A:LEU239 4.6 0.0 1.0 HD2 A:PRO222 4.7 0.0 1.0 CD2 A:LEU239 4.7 0.0 1.0 N A:ASN244 4.7 0.0 1.0 C A:CYS243 4.7 0.0 1.0 CA A:CYS221 4.8 0.0 1.0 HG13 A:VAL227 4.8 0.0 1.0 HD1 A:HIS238 4.9 0.0 1.0 HG A:LEU239 5.0 0.0 1.0 ND2 A:ASN223 5.0 0.0 1.0 HG1 A:THR245 5.0 0.0 1.0 HA A:CYS221 5.0 0.0 1.0

T.Nagashima, F.Hayashi, S.Yokoyama. Solution Structure of Traf-Type Zinc Finger Domains (190 - 248) From Human Tnf Receptor-Associated Factor 4 To Be Published.