Zinc in PDB 2iul: Human Tace G13 Mutant

All present enzymatic activity of Human Tace G13 Mutant:
3.4.15.1;

The structure of Human Tace G13 Mutant, PDB code: 2iul was solved by J.M.Watermeyer, B.T.Sewell, R.Natesh, H.R.Corradi, K.R.Acharya, E.D.Sturrock, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	71.61 / 2.01
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	56.633, 84.723, 134.466, 90.00, 90.00, 90.00
R / Rfree (%)	18 / 22

The structure of Human Tace G13 Mutant also contains other interesting chemical elements:

Chlorine

(Cl)

2 atoms

The binding sites of Zinc atom in the Human Tace G13 Mutant (pdb code 2iul). 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 Human Tace G13 Mutant, PDB code: 2iul:

Zinc binding site 1 out of 1 in the Human Tace G13 Mutant


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Human Tace G13 Mutant within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1634 b:14.8 occ:1.00 OE1 A:GLU411 2.0 9.5 1.0 O A:ACT1627 2.0 16.2 1.0 NE2 A:HIS383 2.1 12.7 1.0 NE2 A:HIS387 2.1 13.4 1.0 OXT A:ACT1627 2.5 16.4 1.0 C A:ACT1627 2.7 16.6 1.0 CD A:GLU411 2.9 8.4 1.0 CE1 A:HIS387 3.0 12.7 1.0 CE1 A:HIS383 3.0 13.1 1.0 CD2 A:HIS383 3.1 12.2 1.0 CD2 A:HIS387 3.1 13.2 1.0 OE2 A:GLU411 3.2 8.4 1.0 ND1 A:HIS383 4.1 12.2 1.0 ND1 A:HIS387 4.1 14.0 1.0 CH3 A:ACT1627 4.1 16.4 1.0 CG A:HIS383 4.1 12.0 1.0 CG A:HIS387 4.2 12.9 1.0 CE2 A:TYR523 4.2 11.6 1.0 O A:HOH2332 4.3 39.5 1.0 CG A:GLU411 4.3 8.9 1.0 O A:HOH2214 4.4 13.2 1.0 OE2 A:GLU384 4.4 11.4 1.0 OH A:TYR523 4.5 11.8 1.0 O A:HOH2182 4.5 13.2 1.0 CA A:GLU411 4.5 10.4 1.0 CB A:GLU411 4.6 10.7 1.0 CZ A:TYR523 4.8 11.4 1.0 OE1 A:GLU384 5.0 12.3 1.0 CD A:GLU384 5.0 11.3 1.0

J.M.Watermeyer, B.T.Sewell, S.L.Schwager, R.Natesh, H.R.Corradi, K.R.Acharya, E.D.Sturrock. Structure of Testis Ace Glycosylation Mutants and Evidence For Conserved Domain Movement. Biochemistry V. 45 12654 2006.
ISSN: ISSN 0006-2960
PubMed: 17042482
DOI: 10.1021/BI061146Z