Chlorine 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:

Zinc

(Zn)

1 atom

The binding sites of Chlorine atom in the Human Tace G13 Mutant (pdb code 2iul). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Human Tace G13 Mutant, PDB code: 2iul:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in the Human Tace G13 Mutant


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Human Tace G13 Mutant within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl1629 b:11.1 occ:1.00 NE A:ARG186 3.2 12.3 1.0 NE1 A:TRP485 3.3 12.2 1.0 NH1 A:ARG489 3.3 11.8 1.0 NH1 A:ARG186 3.3 12.0 1.0 O A:HOH2260 3.3 11.3 1.0 CZ2 A:TRP486 3.5 11.8 1.0 CZ A:ARG186 3.7 11.9 1.0 NE A:ARG489 3.8 10.7 1.0 CB A:ASP507 3.8 11.1 1.0 CZ A:ARG489 3.8 13.3 1.0 CH2 A:TRP486 4.0 10.0 1.0 CE2 A:TRP485 4.1 11.9 1.0 CZ2 A:TRP485 4.2 11.7 1.0 CE2 A:TRP486 4.3 11.2 1.0 CD1 A:TRP485 4.3 12.0 1.0 CD A:ARG186 4.3 13.2 1.0 CZ2 A:TRP182 4.4 10.2 1.0 O A:ASP507 4.5 10.6 1.0 CG A:ASP507 4.6 11.2 1.0 NE1 A:TRP486 4.7 13.1 1.0 C A:ASP507 4.8 10.5 1.0 O A:HOH2140 4.8 11.1 1.0 CA A:ASP507 4.8 10.9 1.0 CD A:ARG489 4.9 11.9 1.0 NH2 A:ARG489 4.9 10.2 1.0 OD2 A:ASP507 5.0 13.0 1.0 CE2 A:TRP182 5.0 10.3 1.0

Chlorine binding site 2 out of 2 in the Human Tace G13 Mutant


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Human Tace G13 Mutant within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl1630 b:10.3 occ:1.00 OH A:TYR224 2.9 12.8 1.0 O A:HOH2098 3.1 10.4 1.0 NE A:ARG522 3.1 9.1 1.0 N A:ARG522 3.6 9.0 1.0 CB A:ARG522 3.6 9.4 1.0 NH2 A:ARG522 3.6 11.0 1.0 CE1 A:TYR224 3.6 12.5 1.0 CB A:PRO519 3.7 9.4 1.0 CB A:PRO407 3.7 10.5 1.0 CZ A:TYR224 3.7 12.8 1.0 CG2 A:ILE521 3.7 7.9 1.0 CE A:MET223 3.8 20.0 1.0 CZ A:ARG522 3.8 10.9 1.0 CG A:PRO407 3.9 10.7 1.0 CA A:ARG522 4.0 9.4 1.0 CG A:ARG522 4.0 10.1 1.0 CD A:ARG522 4.2 9.3 1.0 C A:ILE521 4.5 9.2 1.0 N A:ILE521 4.5 8.6 1.0 C A:PRO519 4.6 9.4 1.0 CG A:PRO519 4.6 10.2 1.0 SD A:MET223 4.7 20.7 1.0 O A:PRO519 4.7 9.2 1.0 CA A:PRO519 4.8 9.7 1.0 CD A:PRO407 4.8 10.8 1.0 CA A:ILE521 4.9 8.8 1.0 N A:TYR520 4.9 8.8 1.0 CD1 A:TYR224 4.9 11.9 1.0 O A:HOH2230 4.9 9.2 1.0 CB A:ILE521 4.9 9.1 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