Cobalt in PDB 3e3h: Crystal Structure of the Op Hydrolase Mutant From Brevundimonas Diminuta

All present enzymatic activity of Crystal Structure of the Op Hydrolase Mutant From Brevundimonas Diminuta:
3.1.8.1;

The structure of Crystal Structure of the Op Hydrolase Mutant From Brevundimonas Diminuta, PDB code: 3e3h was solved by P.Li, T.E.Reeves, J.K.Grimsley, J.R.Wild, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.00 / 2.15
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	128.797, 90.596, 69.145, 90.00, 91.74, 90.00
R / Rfree (%)	18.9 / 21.8

The binding sites of Cobalt atom in the Crystal Structure of the Op Hydrolase Mutant From Brevundimonas Diminuta (pdb code 3e3h). 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 Op Hydrolase Mutant From Brevundimonas Diminuta, PDB code: 3e3h:
Jump to Cobalt binding site number: 1; 2; 3; 4;

Cobalt binding site 1 out of 4 in the Crystal Structure of the Op Hydrolase Mutant From Brevundimonas Diminuta


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 Op Hydrolase Mutant From Brevundimonas Diminuta within 5.0Å range: probe atom residue distance (Å) B Occ A:Co601 b:26.6 occ:1.00 OQ1 A:KCX169 1.9 37.9 1.0 NE2 A:HIS230 2.1 23.2 1.0 ND1 A:HIS201 2.2 23.4 1.0 CX A:KCX169 2.8 37.2 1.0 CE1 A:HIS230 3.0 24.3 1.0 CE1 A:HIS201 3.0 25.6 1.0 O A:HOH804 3.1 48.5 1.0 CD2 A:HIS230 3.1 23.2 1.0 CG A:HIS201 3.2 24.2 1.0 OQ2 A:KCX169 3.2 35.1 1.0 NH2 A:ARG254 3.5 25.0 1.0 CO A:CO602 3.5 23.9 1.0 CB A:HIS201 3.6 21.8 1.0 NZ A:KCX169 3.8 35.7 1.0 NE2 A:HIS55 4.1 18.5 1.0 ND1 A:HIS230 4.2 22.5 1.0 NE2 A:HIS201 4.2 25.4 1.0 CE1 A:HIS55 4.2 19.0 1.0 NE1 A:TRP131 4.2 28.5 1.0 CG A:HIS230 4.2 23.1 1.0 CD2 A:HIS201 4.3 24.2 1.0 OD1 A:ASP301 4.3 18.1 1.0 CZ A:ARG254 4.4 27.7 1.0 CA A:HIS201 4.4 22.2 1.0 NE A:ARG254 4.8 24.2 1.0 O A:HOH791 4.9 40.1 1.0 CD1 A:TRP131 5.0 27.2 1.0 CE A:KCX169 5.0 31.5 1.0 OD2 A:ASP301 5.0 19.1 1.0

Cobalt binding site 2 out of 4 in the Crystal Structure of the Op Hydrolase Mutant From Brevundimonas Diminuta


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 Op Hydrolase Mutant From Brevundimonas Diminuta within 5.0Å range: probe atom residue distance (Å) B Occ A:Co602 b:23.9 occ:1.00 NE2 A:HIS57 2.1 17.6 1.0 NE2 A:HIS55 2.2 18.5 1.0 OD2 A:ASP301 2.3 19.1 1.0 OQ2 A:KCX169 2.8 35.1 1.0 CD2 A:HIS55 3.0 17.3 1.0 CD2 A:HIS57 3.0 16.3 1.0 CE1 A:HIS57 3.1 17.5 1.0 CG A:ASP301 3.2 17.8 1.0 CE1 A:HIS55 3.3 19.0 1.0 OD1 A:ASP301 3.4 18.1 1.0 CO A:CO601 3.5 26.6 1.0 CX A:KCX169 3.7 37.2 1.0 OQ1 A:KCX169 3.9 37.9 1.0 CG2 A:VAL101 4.0 17.7 1.0 CE1 A:HIS230 4.1 24.3 1.0 ND1 A:HIS57 4.2 15.1 1.0 CG A:HIS57 4.2 16.0 1.0 CG A:HIS55 4.2 17.9 1.0 ND1 A:HIS55 4.3 16.6 1.0 NE2 A:HIS230 4.4 23.2 1.0 CB A:ASP301 4.5 17.8 1.0 O A:HOH791 4.7 40.1 1.0 NZ A:KCX169 4.8 35.7 1.0 CA A:ASP301 4.8 18.3 1.0 O A:HOH804 4.9 48.5 1.0 CE A:KCX169 4.9 31.5 1.0

Cobalt binding site 3 out of 4 in the Crystal Structure of the Op Hydrolase Mutant From Brevundimonas Diminuta


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 Op Hydrolase Mutant From Brevundimonas Diminuta within 5.0Å range: probe atom residue distance (Å) B Occ B:Co603 b:22.6 occ:1.00 NE2 B:HIS57 2.0 19.1 1.0 NE2 B:HIS55 2.2 14.3 1.0 O B:HOH743 2.2 26.7 1.0 OD2 B:ASP301 2.4 24.3 1.0 OQ2 B:KCX169 2.7 27.8 1.0 CD2 B:HIS57 3.0 16.2 1.0 CD2 B:HIS55 3.0 17.5 1.0 CE1 B:HIS57 3.1 20.2 1.0 CE1 B:HIS55 3.2 16.5 1.0 CG B:ASP301 3.2 24.2 1.0 CO B:CO604 3.4 29.6 1.0 OD1 B:ASP301 3.5 22.9 1.0 CX B:KCX169 3.5 33.3 1.0 OQ1 B:KCX169 3.7 32.3 1.0 O B:HOH862 3.8 52.4 1.0 CG2 B:VAL101 4.0 13.6 1.0 CE1 B:HIS230 4.1 26.6 1.0 CG B:HIS57 4.2 16.8 1.0 ND1 B:HIS57 4.2 15.5 1.0 CG B:HIS55 4.2 17.1 1.0 ND1 B:HIS55 4.3 17.4 1.0 NE2 B:HIS230 4.3 27.4 1.0 CB B:ASP301 4.5 20.9 1.0 NZ B:KCX169 4.6 32.5 1.0 O B:HOH753 4.8 45.2 1.0 CE B:KCX169 4.8 32.3 1.0 O B:HOH805 4.8 45.2 1.0 CA B:ASP301 4.9 19.8 1.0

Cobalt binding site 4 out of 4 in the Crystal Structure of the Op Hydrolase Mutant From Brevundimonas Diminuta


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 Op Hydrolase Mutant From Brevundimonas Diminuta within 5.0Å range: probe atom residue distance (Å) B Occ B:Co604 b:29.6 occ:1.00 OQ1 B:KCX169 1.8 32.3 1.0 NE2 B:HIS230 2.1 27.4 1.0 ND1 B:HIS201 2.3 24.8 1.0 O B:HOH743 2.3 26.7 1.0 CX B:KCX169 2.8 33.3 1.0 CE1 B:HIS230 3.0 26.6 1.0 O B:HOH805 3.1 45.2 1.0 CD2 B:HIS230 3.1 26.4 1.0 CE1 B:HIS201 3.1 26.8 1.0 CG B:HIS201 3.2 27.3 1.0 OQ2 B:KCX169 3.3 27.8 1.0 CO B:CO603 3.4 22.6 1.0 NH2 B:ARG254 3.5 31.3 1.0 CB B:HIS201 3.6 24.1 1.0 NZ B:KCX169 3.9 32.5 1.0 NE2 B:HIS55 4.1 14.3 1.0 ND1 B:HIS230 4.2 26.5 1.0 NE1 B:TRP131 4.2 29.4 1.0 NE2 B:HIS201 4.2 27.7 1.0 CE1 B:HIS55 4.2 16.5 1.0 CG B:HIS230 4.2 27.1 1.0 CD2 B:HIS201 4.3 26.4 1.0 OD1 B:ASP301 4.3 22.9 1.0 CZ B:ARG254 4.4 32.3 1.0 CA B:HIS201 4.5 24.3 1.0 NE B:ARG254 4.8 29.3 1.0 O B:HOH862 4.8 52.4 1.0 O B:HOH753 4.9 45.2 1.0 CD1 B:TRP131 5.0 27.1 1.0 OD2 B:ASP301 5.0 24.3 1.0 CG B:ASP301 5.0 24.2 1.0

T.E.Reeves, M.E.Wales, J.K.Grimsley, P.Li, D.M.Cerasoli, J.R.Wild. Balancing the Stability and the Catalytic Specificities of Op Hydrolases with Enhanced V-Agent Activities. Protein Eng.Des.Sel. V. 21 405 2008.
ISSN: ISSN 1741-0126
PubMed: 18434422
DOI: 10.1093/PROTEIN/GZN019