Zinc in PDB 3v38: Carboxypeptidase T Mutant L254N

All present enzymatic activity of Carboxypeptidase T Mutant L254N:
3.4.17.18;

The structure of Carboxypeptidase T Mutant L254N, PDB code: 3v38 was solved by V.I.Timofeev, S.A.Kuznetsov, V.K.Akparov, I.P.Kuranova, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	10.00 / 1.50
Space group	P 63 2 2
Cell size a, b, c (Å), α, β, γ (°)	157.829, 157.829, 103.625, 90.00, 90.00, 120.00
R / Rfree (%)	15 / 16.7

The binding sites of Zinc atom in the Carboxypeptidase T Mutant L254N (pdb code 3v38). 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 Carboxypeptidase T Mutant L254N, PDB code: 3v38:

Zinc binding site 1 out of 1 in the Carboxypeptidase T Mutant L254N


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Carboxypeptidase T Mutant L254N within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn401 b:12.3 occ:1.00 O A:HOH544 1.9 12.3 1.0 ND1 A:HIS69 2.1 8.9 1.0 ND1 A:HIS204 2.1 9.2 1.0 OE1 A:GLU72 2.2 9.3 1.0 OE2 A:GLU72 2.3 9.9 1.0 CD A:GLU72 2.5 9.4 1.0 CE1 A:HIS69 3.0 9.5 1.0 CE1 A:HIS204 3.0 9.8 1.0 CG A:HIS204 3.1 8.6 1.0 CG A:HIS69 3.1 8.8 1.0 CB A:HIS204 3.5 8.5 1.0 CB A:HIS69 3.6 9.5 1.0 O A:HOH537 3.9 11.8 1.0 O A:THR205 4.0 8.8 1.0 O4 A:SO4402 4.0 13.2 1.0 O A:HOH796 4.0 6.8 0.3 O2 A:SO4402 4.1 16.2 1.0 CG A:GLU72 4.1 9.8 1.0 NE2 A:HIS69 4.1 9.5 1.0 NE2 A:HIS204 4.2 9.9 1.0 CD2 A:HIS204 4.2 9.0 1.0 CD2 A:HIS69 4.2 9.4 1.0 CA A:HIS204 4.3 8.3 1.0 S A:SO4402 4.4 12.8 1.0 O A:HOH507 4.4 12.7 1.0 O1 A:SO4402 4.5 11.9 1.0 N A:THR205 4.5 8.6 1.0 NH1 A:ARG129 4.5 10.5 1.0 C1 A:GOL408 4.6 22.3 0.7 OE1 A:GLU277 4.7 18.0 0.9 N A:HIS69 4.8 10.2 1.0 CA A:HIS69 4.8 9.8 1.0 CB A:GLU72 4.9 9.4 1.0 C A:HIS204 4.9 8.3 1.0 OE2 A:GLU277 5.0 22.5 0.9

V.I.Timofeev, S.A.Kuznetsov, V.K.Akparov, I.P.Kuranova. Carboxypeptidase T Mutant L254N To Be Published.