Cobalt in PDB 5vsa: Crystal Structure of Ssopox ASA1 Mutant (C258L-I261F-W263A)

All present enzymatic activity of Crystal Structure of Ssopox ASA1 Mutant (C258L-I261F-W263A):
3.1.8.1;

The structure of Crystal Structure of Ssopox ASA1 Mutant (C258L-I261F-W263A), PDB code: 5vsa was solved by J.Hiblot, G.Gotthard, P.Jacquet, D.Daude, C.Bergonzi, E.Chabriere, M.Elias, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	48.81 / 2.00
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	86.600, 103.100, 151.800, 90.00, 90.00, 90.00
R / Rfree (%)	15.8 / 20.4

The structure of Crystal Structure of Ssopox ASA1 Mutant (C258L-I261F-W263A) also contains other interesting chemical elements:

Iron

(Fe)

4 atoms

The binding sites of Cobalt atom in the Crystal Structure of Ssopox ASA1 Mutant (C258L-I261F-W263A) (pdb code 5vsa). 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 Ssopox ASA1 Mutant (C258L-I261F-W263A), PDB code: 5vsa:
Jump to Cobalt binding site number: 1; 2; 3; 4;

Cobalt binding site 1 out of 4 in the Crystal Structure of Ssopox ASA1 Mutant (C258L-I261F-W263A)


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 Ssopox ASA1 Mutant (C258L-I261F-W263A) within 5.0Å range: probe atom residue distance (Å) B Occ A:Co402 b:19.2 occ:1.00 OQ2 A:KCX137 1.9 16.8 1.0 NE2 A:HIS199 2.0 18.7 1.0 ND1 A:HIS170 2.1 19.6 1.0 O A:HOH506 2.2 19.8 1.0 CE1 A:HIS199 2.9 20.5 1.0 O2 A:GOL405 3.0 52.4 1.0 CX A:KCX137 3.0 15.1 1.0 CE1 A:HIS170 3.0 20.7 1.0 CD2 A:HIS199 3.1 18.5 1.0 CG A:HIS170 3.1 18.1 1.0 OQ1 A:KCX137 3.3 15.3 1.0 FE A:FE401 3.4 15.9 1.0 CB A:HIS170 3.5 17.4 1.0 NH2 A:ARG223 3.7 22.6 1.0 CE1 A:HIS22 4.0 16.4 1.0 OD2 A:ASP256 4.0 19.2 1.0 OH A:TYR97 4.1 25.5 1.0 ND1 A:HIS199 4.1 20.4 1.0 NE2 A:HIS22 4.1 15.0 1.0 NE2 A:HIS170 4.1 20.9 1.0 NZ A:KCX137 4.2 15.6 1.0 CE2 A:TYR97 4.2 21.9 1.0 CG A:HIS199 4.2 18.9 1.0 CA A:HIS170 4.2 16.9 1.0 CD2 A:HIS170 4.2 19.4 1.0 CZ A:ARG223 4.4 21.2 1.0 C2 A:GOL405 4.5 56.9 1.0 O3 A:GOL405 4.6 48.6 1.0 OD1 A:ASP256 4.6 17.5 1.0 NE A:ARG223 4.6 19.3 1.0 CZ A:TYR97 4.7 24.2 1.0 CE A:KCX137 4.7 17.6 1.0 CG A:ASP256 4.7 18.6 1.0

Cobalt binding site 2 out of 4 in the Crystal Structure of Ssopox ASA1 Mutant (C258L-I261F-W263A)


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 Ssopox ASA1 Mutant (C258L-I261F-W263A) within 5.0Å range: probe atom residue distance (Å) B Occ B:Co402 b:20.1 occ:1.00 OQ1 B:KCX137 1.9 18.3 1.0 NE2 B:HIS199 2.0 17.1 1.0 ND1 B:HIS170 2.1 22.6 1.0 O B:HOH506 2.1 19.9 1.0 O B:HOH625 2.8 39.7 1.0 CX B:KCX137 2.9 15.9 1.0 CE1 B:HIS199 2.9 17.8 1.0 CE1 B:HIS170 3.0 21.9 1.0 CG B:HIS170 3.1 19.6 1.0 CD2 B:HIS199 3.1 17.9 1.0 OQ2 B:KCX137 3.3 15.7 1.0 FE B:FE401 3.4 14.1 1.0 CB B:HIS170 3.4 17.0 1.0 NH2 B:ARG223 3.9 25.1 1.0 CE1 B:HIS22 4.0 16.9 1.0 ND1 B:HIS199 4.1 17.7 1.0 NE2 B:HIS22 4.1 16.1 1.0 OD2 B:ASP256 4.1 18.6 1.0 NZ B:KCX137 4.1 15.7 1.0 NE2 B:HIS170 4.1 20.9 1.0 CE2 B:TYR97 4.2 22.3 1.0 CD2 B:HIS170 4.2 20.1 1.0 CG B:HIS199 4.2 18.1 1.0 OH B:TYR97 4.2 24.5 1.0 CA B:HIS170 4.3 17.4 1.0 O B:HOH660 4.4 49.0 1.0 CZ B:ARG223 4.5 22.6 1.0 OD1 B:ASP256 4.6 18.2 1.0 CE B:KCX137 4.6 16.8 1.0 O B:HOH557 4.7 44.8 1.0 CZ B:TYR97 4.7 25.4 1.0 CG B:ASP256 4.7 18.4 1.0 NE B:ARG223 4.8 22.0 1.0

Cobalt binding site 3 out of 4 in the Crystal Structure of Ssopox ASA1 Mutant (C258L-I261F-W263A)


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 Ssopox ASA1 Mutant (C258L-I261F-W263A) within 5.0Å range: probe atom residue distance (Å) B Occ C:Co402 b:20.1 occ:1.00 OQ1 C:KCX137 1.9 16.7 1.0 ND1 C:HIS170 2.0 19.8 1.0 O C:HOH518 2.1 18.2 1.0 NE2 C:HIS199 2.1 17.6 1.0 O2 C:GOL404 2.6 36.9 1.0 CX C:KCX137 2.9 16.8 1.0 CE1 C:HIS170 3.0 20.9 1.0 CE1 C:HIS199 3.0 16.5 1.0 CG C:HIS170 3.1 19.3 1.0 CD2 C:HIS199 3.1 18.1 1.0 OQ2 C:KCX137 3.3 17.9 1.0 FE C:FE401 3.5 16.4 1.0 CB C:HIS170 3.5 18.8 1.0 NH2 C:ARG223 3.7 25.3 1.0 C2 C:GOL404 3.9 46.1 1.0 OD2 C:ASP256 4.1 20.0 1.0 NE2 C:HIS170 4.1 18.8 1.0 CE1 C:HIS22 4.1 17.4 1.0 NZ C:KCX137 4.1 17.9 1.0 CE2 C:TYR97 4.1 24.3 1.0 ND1 C:HIS199 4.2 16.2 1.0 OH C:TYR97 4.2 28.3 1.0 CD2 C:HIS170 4.2 21.2 1.0 CA C:HIS170 4.2 18.0 1.0 NE2 C:HIS22 4.2 19.1 1.0 CG C:HIS199 4.2 18.0 1.0 O3 C:GOL404 4.2 35.8 1.0 CZ C:ARG223 4.4 22.6 1.0 OD1 C:ASP256 4.6 16.4 1.0 NE C:ARG223 4.7 21.1 1.0 CE C:KCX137 4.7 17.9 1.0 C3 C:GOL404 4.7 41.4 1.0 CZ C:TYR97 4.7 24.9 1.0 CG C:ASP256 4.8 18.6 1.0

Cobalt binding site 4 out of 4 in the Crystal Structure of Ssopox ASA1 Mutant (C258L-I261F-W263A)


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 Ssopox ASA1 Mutant (C258L-I261F-W263A) within 5.0Å range: probe atom residue distance (Å) B Occ D:Co402 b:24.4 occ:1.00 OQ2 D:KCX137 2.0 23.9 1.0 ND1 D:HIS170 2.0 23.4 1.0 NE2 D:HIS199 2.1 25.3 1.0 O D:HOH510 2.1 23.4 1.0 O D:HOH579 2.8 32.6 1.0 CE1 D:HIS170 2.9 27.7 1.0 CX D:KCX137 3.0 19.1 1.0 CE1 D:HIS199 3.0 24.5 1.0 CG D:HIS170 3.1 25.1 1.0 CD2 D:HIS199 3.1 23.6 1.0 OQ1 D:KCX137 3.3 20.9 1.0 CB D:HIS170 3.5 23.2 1.0 FE D:FE401 3.5 19.2 1.0 NH2 D:ARG223 3.8 36.0 1.0 OD2 D:ASP256 4.0 21.2 1.0 NE2 D:HIS170 4.1 25.7 1.0 CE2 D:TYR97 4.1 24.5 1.0 OH D:TYR97 4.1 28.3 1.0 ND1 D:HIS199 4.1 23.9 1.0 CD2 D:HIS170 4.2 24.7 1.0 CE1 D:HIS22 4.2 17.2 1.0 NZ D:KCX137 4.2 20.0 1.0 CG D:HIS199 4.2 24.2 1.0 CA D:HIS170 4.2 23.4 1.0 NE2 D:HIS22 4.3 19.9 1.0 CZ D:ARG223 4.5 32.5 1.0 CZ D:TYR97 4.6 25.8 1.0 OD1 D:ASP256 4.7 20.3 1.0 CE D:KCX137 4.7 20.8 1.0 CG D:ASP256 4.7 22.0 1.0 O D:HOH639 4.8 38.8 1.0 NE D:ARG223 4.8 31.9 1.0

P.Jacquet, J.Hiblot, D.Daude, C.Bergonzi, G.Gotthard, N.Armstrong, E.Chabriere, M.Elias. Rational Engineering of A Native Hyperthermostable Lactonase Into A Broad Spectrum Phosphotriesterase. Sci Rep V. 7 16745 2017.
ISSN: ESSN 2045-2322
PubMed: 29196634
DOI: 10.1038/S41598-017-16841-0