Zinc in PDB 5lg7: Solution uc(Nmr) Structure of Tryptophan to Arginine Mutant of Arkadia Ring Domain

The binding sites of Zinc atom in the Solution uc(Nmr) Structure of Tryptophan to Arginine Mutant of Arkadia Ring Domain (pdb code 5lg7). 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 uc(Nmr) Structure of Tryptophan to Arginine Mutant of Arkadia Ring Domain, PDB code: 5lg7:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Solution uc(Nmr) Structure of Tryptophan to Arginine Mutant of Arkadia Ring Domain


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Solution uc(Nmr) Structure of Tryptophan to Arginine Mutant of Arkadia Ring Domain within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn101 b:0.7 occ:1.00 SG A:CYS43 2.0 1.7 1.0 SG A:CYS20 2.1 1.3 1.0 ND1 A:HIS40 2.1 0.7 1.0 SG A:CYS17 2.2 0.5 1.0 HB3 A:CYS20 2.9 0.9 1.0 HB3 A:HIS40 3.0 1.2 1.0 CG A:HIS40 3.1 0.6 1.0 HB2 A:CYS43 3.1 1.3 1.0 CB A:CYS20 3.1 0.8 1.0 CE1 A:HIS40 3.1 0.9 1.0 CB A:CYS43 3.2 1.3 1.0 HB2 A:HIS40 3.2 1.2 1.0 CB A:HIS40 3.4 0.8 1.0 H A:CYS20 3.4 0.6 1.0 CB A:CYS17 3.4 0.4 1.0 HE1 A:HIS40 3.4 1.0 1.0 HB2 A:CYS17 3.5 0.6 1.0 HB3 A:CYS17 3.6 0.5 1.0 HB3 A:CYS43 3.6 1.8 1.0 HB2 A:CYS20 3.8 1.0 1.0 H A:CYS43 3.8 0.8 1.0 HB A:ILE19 4.0 0.5 1.0 N A:CYS20 4.1 0.6 1.0 HD22 A:LEU24 4.2 1.4 1.0 CA A:CYS20 4.2 0.7 1.0 NE2 A:HIS40 4.3 0.9 1.0 CD2 A:HIS40 4.3 0.7 1.0 CA A:CYS43 4.4 0.9 1.0 N A:CYS43 4.5 0.7 1.0 HB A:VAL42 4.6 0.8 1.0 H A:HIS40 4.8 1.6 1.0 CA A:CYS17 4.8 0.4 1.0 CA A:HIS40 4.9 0.6 1.0 HA A:CYS43 4.9 1.2 1.0 H A:ILE19 4.9 0.5 1.0 OG A:SER22 4.9 1.1 1.0 HG A:SER22 5.0 1.2 1.0 HA A:CYS17 5.0 0.4 1.0

Zinc binding site 2 out of 2 in the Solution uc(Nmr) Structure of Tryptophan to Arginine Mutant of Arkadia Ring Domain


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Solution uc(Nmr) Structure of Tryptophan to Arginine Mutant of Arkadia Ring Domain within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn102 b:0.7 occ:1.00 O A:CYS35 1.8 0.8 1.0 ND1 A:HIS37 2.1 0.8 1.0 SG A:CYS57 2.2 1.0 1.0 SG A:CYS35 2.2 1.2 1.0 SG A:CYS54 2.2 0.8 1.0 C A:CYS35 2.8 0.7 1.0 HB2 A:CYS35 3.0 1.1 1.0 CB A:CYS35 3.1 0.7 1.0 CE1 A:HIS37 3.1 1.1 1.0 O A:MET36 3.2 0.9 1.0 CG A:HIS37 3.2 0.8 1.0 HB2 A:HIS37 3.2 0.6 1.0 HE1 A:HIS37 3.3 1.2 1.0 CB A:CYS57 3.4 1.0 1.0 C A:MET36 3.5 0.8 1.0 CA A:CYS35 3.5 0.7 1.0 HB2 A:CYS57 3.5 1.4 1.0 CB A:CYS54 3.6 0.7 1.0 CB A:HIS37 3.7 0.7 1.0 HB3 A:CYS57 3.7 1.6 1.0 HB3 A:CYS54 3.7 1.0 1.0 N A:MET36 3.8 0.8 1.0 HB2 A:CYS54 3.9 0.9 1.0 N A:HIS37 3.9 0.7 1.0 HB3 A:CYS35 4.1 0.9 1.0 HA A:CYS35 4.1 0.9 1.0 CA A:MET36 4.2 0.8 1.0 H A:CYS57 4.2 1.6 1.0 NE2 A:HIS37 4.3 1.3 1.0 CD2 A:HIS37 4.3 1.1 1.0 CA A:HIS37 4.3 0.7 1.0 HB2 A:MET36 4.4 1.2 1.0 HB2 A:LEU33 4.5 1.1 1.0 H A:HIS37 4.5 0.7 1.0 N A:CYS35 4.5 0.6 1.0 H A:CYS35 4.6 0.6 1.0 HB3 A:HIS37 4.6 0.8 1.0 HD12 A:LEU33 4.6 3.0 1.0 HA A:HIS37 4.6 0.8 1.0 H A:MET36 4.7 0.8 1.0 HD11 A:ILE61 4.7 1.4 1.0 CA A:CYS57 4.8 1.1 1.0 HA A:CYS54 4.9 0.7 1.0 N A:CYS57 4.9 1.1 1.0 CB A:MET36 4.9 0.9 1.0 CA A:CYS54 4.9 0.6 1.0

M.Birkou, C.T.Chasapis, K.D.Marousis, A.K.Loutsidou, D.Bentrop, M.Lelli, T.Herrmann, J.M.Carthy, V.Episkopou, G.A.Spyroulias. A Residue Specific Insight Into the Arkadia E3 Ubiquitin Ligase Activity and Conformational Plasticity. J. Mol. Biol. V. 429 2373 2017.
ISSN: ESSN 1089-8638
PubMed: 28647409
DOI: 10.1016/J.JMB.2017.06.012