Cobalt in PDB 4j35: Molecular Engineering of Organophosphate Hydrolysis Activity From A Weak Promiscuous Lactonase Template

The structure of Molecular Engineering of Organophosphate Hydrolysis Activity From A Weak Promiscuous Lactonase Template, PDB code: 4j35 was solved by R.Sterner, F.Raushel, M.Meier, C.Rajendran, C.Malisi, N.Fox, S.Schlee, D.Barondeau, B.H.Cker, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	47.46 / 1.78
Space group	P 31 2 1
Cell size a, b, c (Å), α, β, γ (°)	61.853, 61.853, 204.786, 90.00, 90.00, 120.00
R / Rfree (%)	20.1 / 22.6

The binding sites of Cobalt atom in the Molecular Engineering of Organophosphate Hydrolysis Activity From A Weak Promiscuous Lactonase Template (pdb code 4j35). This binding sites where shown within 5.0 Angstroms radius around Cobalt atom.
In total 2 binding sites of Cobalt where determined in the Molecular Engineering of Organophosphate Hydrolysis Activity From A Weak Promiscuous Lactonase Template, PDB code: 4j35:
Jump to Cobalt binding site number: 1; 2;

Cobalt binding site 1 out of 2 in the Molecular Engineering of Organophosphate Hydrolysis Activity From A Weak Promiscuous Lactonase Template


Mono view


Stereo pair view

A full contact list of Cobalt with other atoms in the Co binding site number 1 of Molecular Engineering of Organophosphate Hydrolysis Activity From A Weak Promiscuous Lactonase Template within 5.0Å range: probe atom residue distance (Å) B Occ A:Co401 b:31.6 occ:1.00 OQ2 A:KCX143 1.8 28.1 1.0 NE2 A:HIS204 2.0 30.8 1.0 ND1 A:HIS176 2.1 36.4 1.0 HB2 A:HIS176 2.9 44.4 1.0 CD2 A:HIS204 2.9 30.2 1.0 CX A:KCX143 3.0 30.3 1.0 O A:HOH665 3.0 54.4 1.0 CE1 A:HIS204 3.0 28.3 1.0 HD2 A:HIS204 3.1 36.2 1.0 CE1 A:HIS176 3.1 36.6 1.0 CG A:HIS176 3.1 35.9 1.0 HE1 A:HIS176 3.3 43.9 1.0 HE1 A:HIS204 3.3 33.9 1.0 HE1 A:PHE97 3.4 74.2 1.0 CO A:CO402 3.4 27.9 1.0 CB A:HIS176 3.4 37.1 1.0 OQ1 A:KCX143 3.6 27.6 1.0 HE1 A:HIS21 3.7 33.9 1.0 HA A:HIS176 3.9 33.6 1.0 NZ A:KCX143 4.1 27.5 1.0 CG A:HIS204 4.1 32.4 1.0 ND1 A:HIS204 4.1 32.8 1.0 NE2 A:HIS21 4.2 25.9 1.0 CE1 A:HIS21 4.2 28.3 1.0 OD2 A:ASP264 4.2 31.6 1.0 NE2 A:HIS176 4.2 41.3 1.0 CE1 A:PHE97 4.2 61.9 1.0 HZ A:PHE97 4.2 80.5 1.0 HB3 A:HIS176 4.2 44.4 1.0 CA A:HIS176 4.2 28.0 1.0 CD2 A:HIS176 4.3 38.1 1.0 CZ A:PHE97 4.7 67.1 1.0 OD1 A:ASP264 4.7 31.1 1.0 CE A:KCX143 4.7 32.3 1.0 CG A:ASP264 4.8 30.3 1.0 HD1 A:HIS204 4.9 39.4 1.0 HE2 A:HIS176 5.0 49.5 1.0

Cobalt binding site 2 out of 2 in the Molecular Engineering of Organophosphate Hydrolysis Activity From A Weak Promiscuous Lactonase Template


Mono view


Stereo pair view

A full contact list of Cobalt with other atoms in the Co binding site number 2 of Molecular Engineering of Organophosphate Hydrolysis Activity From A Weak Promiscuous Lactonase Template within 5.0Å range: probe atom residue distance (Å) B Occ A:Co402 b:27.9 occ:1.00 NE2 A:HIS23 2.0 29.8 1.0 OQ1 A:KCX143 2.1 27.6 1.0 NE2 A:HIS21 2.1 25.9 1.0 OD1 A:ASP264 2.2 31.1 1.0 CX A:KCX143 2.8 30.3 1.0 OQ2 A:KCX143 2.9 28.1 1.0 CD2 A:HIS23 2.9 27.2 1.0 CE1 A:HIS23 3.0 30.9 1.0 CD2 A:HIS21 3.1 23.0 1.0 HD2 A:HIS23 3.1 32.6 1.0 CG A:ASP264 3.1 30.3 1.0 CE1 A:HIS21 3.2 28.3 1.0 HD2 A:HIS21 3.2 27.5 1.0 HE1 A:HIS23 3.2 37.0 1.0 HE1 A:HIS21 3.4 33.9 1.0 CO A:CO401 3.4 31.6 1.0 HE1 A:HIS204 3.5 33.9 1.0 OD2 A:ASP264 3.5 31.6 1.0 HB3 A:ALA67 3.7 34.0 1.0 NZ A:KCX143 3.9 27.5 1.0 ND1 A:HIS23 4.1 27.6 1.0 CG A:HIS23 4.1 26.3 1.0 CE1 A:HIS204 4.1 28.3 1.0 NE2 A:HIS204 4.2 30.8 1.0 HA A:ASP264 4.2 36.6 1.0 CG A:HIS21 4.3 28.5 1.0 ND1 A:HIS21 4.3 24.7 1.0 CB A:ASP264 4.5 30.5 1.0 HB1 A:ALA67 4.5 34.0 1.0 CB A:ALA67 4.5 28.3 1.0 HB2 A:ASP264 4.7 36.6 1.0 HE2 A:PHE26 4.7 48.3 1.0 CA A:ASP264 4.8 30.5 1.0 HD1 A:HIS23 4.9 33.1 1.0

M.M.Meier, C.Rajendran, C.Malisi, N.G.Fox, C.Xu, S.Schlee, D.P.Barondeau, B.Hocker, R.Sterner, F.M.Raushel. Molecular Engineering of Organophosphate Hydrolysis Activity From A Weak Promiscuous Lactonase Template. J.Am.Chem.Soc. V. 135 11670 2013.
ISSN: ISSN 0002-7863
PubMed: 23837603
DOI: 10.1021/JA405911H