Zinc in PDB 2iux: Human Tace Mutant G1234

All present enzymatic activity of Human Tace Mutant G1234:
3.4.15.1;

The structure of Human Tace Mutant G1234, PDB code: 2iux was solved by J.M.Watermeyer, B.T.Swell, 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)	50.0 / 2.8
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	56.436, 85.149, 133.424, 90.00, 90.00, 90.00
R / Rfree (%)	20.06 / 23.69

The structure of Human Tace Mutant G1234 also contains other interesting chemical elements:

Chlorine

(Cl)

2 atoms

The binding sites of Zinc atom in the Human Tace Mutant G1234 (pdb code 2iux). 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 Mutant G1234, PDB code: 2iux:

Zinc binding site 1 out of 1 in the Human Tace Mutant G1234


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Human Tace Mutant G1234 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1621 b:13.1 occ:1.00 NE2 A:HIS387 2.2 9.4 1.0 OE1 A:GLU411 2.2 19.7 1.0 NE2 A:HIS383 2.2 15.7 1.0 OXT A:ACT1620 2.5 28.1 1.0 O A:ACT1620 2.7 27.6 1.0 CD A:GLU411 2.9 18.8 1.0 C A:ACT1620 3.0 26.9 1.0 CE1 A:HIS387 3.0 12.0 1.0 OE2 A:GLU411 3.0 19.2 1.0 CE1 A:HIS383 3.1 13.9 1.0 CD2 A:HIS383 3.2 15.0 1.0 CD2 A:HIS387 3.3 10.8 1.0 CE2 A:TYR523 4.1 12.8 1.0 OD2 A:NXA1624 4.2 32.1 1.0 ND1 A:HIS387 4.2 11.7 1.0 ND1 A:HIS383 4.3 13.2 1.0 CG A:HIS383 4.3 13.7 1.0 CG A:GLU411 4.4 16.6 1.0 OH A:TYR523 4.4 16.7 1.0 CG A:HIS387 4.4 9.8 1.0 CH3 A:ACT1620 4.4 25.3 1.0 OE2 A:GLU384 4.5 7.9 1.0 C1 A:NXA1624 4.5 32.0 1.0 CA A:GLU411 4.6 17.3 1.0 CZ A:TYR523 4.7 13.1 1.0 CB A:GLU411 4.8 16.2 1.0 OD1 A:NXA1624 4.9 32.0 1.0 N A:NXA1624 5.0 30.3 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