Cobalt in PDB 2hp5: Crystal Structure of the Oxa-10 W154G Mutant at pH 7.0

All present enzymatic activity of Crystal Structure of the Oxa-10 W154G Mutant at pH 7.0:
3.5.2.6;

The structure of Crystal Structure of the Oxa-10 W154G Mutant at pH 7.0, PDB code: 2hp5 was solved by F.Kerff, C.Falzone, R.Herman, E.Sauvage, P.Charlier, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	46.47 / 2.70
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	47.110, 125.400, 92.360, 90.00, 99.80, 90.00
R / Rfree (%)	21 / 26.7

The binding sites of Cobalt atom in the Crystal Structure of the Oxa-10 W154G Mutant at pH 7.0 (pdb code 2hp5). This binding sites where shown within 5.0 Angstroms radius around Cobalt atom.
In total 4 binding sites of Cobalt where determined in the Crystal Structure of the Oxa-10 W154G Mutant at pH 7.0, PDB code: 2hp5:
Jump to Cobalt binding site number: 1; 2; 3; 4;

Cobalt binding site 1 out of 4 in the Crystal Structure of the Oxa-10 W154G Mutant at pH 7.0


Mono view


Stereo pair view

A full contact list of Cobalt with other atoms in the Co binding site number 1 of Crystal Structure of the Oxa-10 W154G Mutant at pH 7.0 within 5.0Å range: probe atom residue distance (Å) B Occ A:Co269 b:24.1 occ:1.00 OE1 B:GLU190 2.0 33.3 1.0 OE1 A:GLU227 2.1 28.9 1.0 NE2 A:HIS203 2.3 34.5 1.0 O B:HOH278 2.7 2.0 1.0 CE1 A:HIS203 2.9 32.7 1.0 CD B:GLU190 3.1 32.2 1.0 CD A:GLU227 3.2 27.8 1.0 CD2 A:HIS203 3.2 32.2 1.0 O A:HOH288 3.6 2.0 1.0 CD2 A:LEU201 3.7 20.9 1.0 OE2 A:GLU227 3.8 30.7 1.0 OE2 B:GLU190 3.8 33.7 1.0 ND1 A:HIS203 3.9 32.5 1.0 NE1 A:TRP225 4.0 27.8 1.0 CG A:HIS203 4.1 31.8 1.0 CG B:GLU190 4.2 31.2 1.0 CG A:GLU227 4.4 26.0 1.0 CZ2 A:TRP225 4.4 26.7 1.0 CE2 A:TRP225 4.6 28.6 1.0 CG A:LEU201 4.8 22.9 1.0

Cobalt binding site 2 out of 4 in the Crystal Structure of the Oxa-10 W154G Mutant at pH 7.0


Mono view


Stereo pair view

A full contact list of Cobalt with other atoms in the Co binding site number 2 of Crystal Structure of the Oxa-10 W154G Mutant at pH 7.0 within 5.0Å range: probe atom residue distance (Å) B Occ B:Co270 b:27.4 occ:1.00 OE2 A:GLU190 2.0 39.0 1.0 NE2 B:HIS203 2.1 19.3 1.0 OE2 B:GLU227 2.2 37.0 1.0 O A:HOH283 2.3 2.0 1.0 CD2 B:HIS203 2.9 21.2 1.0 CE1 B:HIS203 3.0 17.8 1.0 CD A:GLU190 3.1 39.6 1.0 CD B:GLU227 3.4 35.2 1.0 CD2 B:LEU201 3.6 29.9 1.0 OE1 A:GLU190 3.6 41.0 1.0 O A:HOH271 4.0 30.8 1.0 CG B:HIS203 4.0 21.1 1.0 ND1 B:HIS203 4.0 20.3 1.0 NE1 B:TRP225 4.1 37.9 1.0 CG B:GLU227 4.2 31.1 1.0 OE1 B:GLU227 4.3 36.5 1.0 CG A:GLU190 4.4 36.9 1.0 CG B:LEU201 4.7 28.9 1.0 CZ2 B:TRP225 4.7 38.5 1.0 CE2 B:TRP225 4.8 37.7 1.0

Cobalt binding site 3 out of 4 in the Crystal Structure of the Oxa-10 W154G Mutant at pH 7.0


Mono view


Stereo pair view

A full contact list of Cobalt with other atoms in the Co binding site number 3 of Crystal Structure of the Oxa-10 W154G Mutant at pH 7.0 within 5.0Å range: probe atom residue distance (Å) B Occ C:Co269 b:29.1 occ:1.00 OE1 C:GLU227 2.0 35.6 1.0 OE1 D:GLU190 2.2 45.6 1.0 NE2 C:HIS203 2.5 37.9 1.0 O C:HOH275 2.5 2.0 1.0 CE1 C:HIS203 3.0 35.9 1.0 CD C:GLU227 3.2 34.9 1.0 CD D:GLU190 3.3 44.8 1.0 CD2 C:HIS203 3.5 34.7 1.0 OE2 D:GLU190 3.6 46.4 1.0 OE2 C:GLU227 3.8 35.5 1.0 NE1 C:TRP225 3.9 25.4 1.0 CD2 C:LEU201 4.0 34.7 1.0 ND1 C:HIS203 4.0 35.2 1.0 CG C:GLU227 4.3 34.3 1.0 CG C:HIS203 4.3 33.9 1.0 CZ2 C:TRP225 4.5 24.3 1.0 CG D:GLU190 4.6 42.8 1.0 CE2 C:TRP225 4.6 22.8 1.0 CE1 C:TYR174 4.8 28.1 1.0 CD1 C:TYR174 4.9 29.6 1.0 CD1 C:TRP225 5.0 25.1 1.0

Cobalt binding site 4 out of 4 in the Crystal Structure of the Oxa-10 W154G Mutant at pH 7.0


Mono view


Stereo pair view

A full contact list of Cobalt with other atoms in the Co binding site number 4 of Crystal Structure of the Oxa-10 W154G Mutant at pH 7.0 within 5.0Å range: probe atom residue distance (Å) B Occ D:Co270 b:43.5 occ:1.00 OE2 D:GLU227 2.0 42.2 1.0 NE2 D:HIS203 2.2 28.9 1.0 O C:HOH270 2.4 3.3 1.0 CD D:GLU227 2.9 41.0 1.0 CE1 D:HIS203 3.0 27.9 1.0 OE2 C:GLU190 3.0 41.0 1.0 OE1 D:GLU227 3.1 41.6 1.0 CD2 D:HIS203 3.1 26.8 1.0 CD C:GLU190 3.7 41.1 1.0 CD2 D:LEU201 3.9 28.4 1.0 ND1 D:HIS203 4.0 29.1 1.0 NE1 D:TRP225 4.1 26.8 1.0 CG D:HIS203 4.1 27.2 1.0 CG C:GLU190 4.2 38.3 1.0 CG D:GLU227 4.3 37.9 1.0 OE1 C:GLU190 4.6 42.3 1.0 CZ2 D:TRP225 4.6 25.1 1.0 CE2 D:TRP225 4.7 25.0 1.0 O C:HOH276 4.9 28.4 1.0

S.Baurin, L.Vercheval, F.Bouillenne, C.Falzone, A.Brans, L.Jacquamet, J.L.Ferrer, E.Sauvage, D.Dehareng, J.M.Frere, P.Charlier, M.Galleni, F.Kerff. Critical Role of Tryptophan 154 For the Activity and Stability of Class D Beta-Lactamases. Biochemistry V. 48 11252 2009.
ISSN: ISSN 0006-2960
PubMed: 19860471
DOI: 10.1021/BI901548C