Cadmium in PDB 7c85: Esterase ALINE4 Mutant-S13A

The structure of Esterase ALINE4 Mutant-S13A, PDB code: 7c85 was solved by Z.Li, J.Li, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	39.90 / 1.75
Space group	P 42 21 2
Cell size a, b, c (Å), α, β, γ (°)	79.810, 79.810, 60.820, 90.00, 90.00, 90.00
R / Rfree (%)	12.1 / 17.7

The binding sites of Cadmium atom in the Esterase ALINE4 Mutant-S13A (pdb code 7c85). This binding sites where shown within 5.0 Angstroms radius around Cadmium atom.
In total 6 binding sites of Cadmium where determined in the Esterase ALINE4 Mutant-S13A, PDB code: 7c85:
Jump to Cadmium binding site number: 1; 2; 3; 4; 5; 6;

Cadmium binding site 1 out of 6 in the Esterase ALINE4 Mutant-S13A


Mono view


Stereo pair view

A full contact list of Cadmium with other atoms in the Cd binding site number 1 of Esterase ALINE4 Mutant-S13A within 5.0Å range: probe atom residue distance (Å) B Occ A:Cd201 b:14.9 occ:0.93 OE2 A:GLU91 2.1 15.3 1.0 CD A:GLU91 2.8 14.4 1.0 OE1 A:GLU91 2.8 17.2 1.0 CG A:GLU91 4.3 13.5 1.0 O A:HOH325 5.0 17.9 1.0

Cadmium binding site 2 out of 6 in the Esterase ALINE4 Mutant-S13A


Mono view


Stereo pair view

A full contact list of Cadmium with other atoms in the Cd binding site number 2 of Esterase ALINE4 Mutant-S13A within 5.0Å range: probe atom residue distance (Å) B Occ A:Cd202 b:32.0 occ:0.64 OE2 A:GLU172 2.3 20.2 1.0 O A:HOH425 2.3 35.8 1.0 OE1 A:GLU172 2.5 22.2 1.0 CD A:GLU172 2.8 18.2 1.0 O A:HOH422 3.7 50.6 1.0 CG A:GLU172 4.3 12.8 1.0 NH1 A:ARG169 4.3 32.1 1.0 CD A:ARG169 5.0 18.2 1.0

Cadmium binding site 3 out of 6 in the Esterase ALINE4 Mutant-S13A


Mono view


Stereo pair view

A full contact list of Cadmium with other atoms in the Cd binding site number 3 of Esterase ALINE4 Mutant-S13A within 5.0Å range: probe atom residue distance (Å) B Occ A:Cd203 b:20.8 occ:0.70 O A:HOH390 2.2 32.6 1.0 O A:HOH409 2.3 26.6 1.0 OE2 A:GLU31 2.3 22.4 1.0 O A:HOH366 2.3 28.1 1.0 OE1 A:GLU31 2.4 17.1 1.0 O A:HOH449 2.5 29.0 1.0 CD A:GLU31 2.7 21.2 1.0 CG A:GLU31 4.2 19.9 1.0 O A:HOH365 4.2 24.9 1.0 O A:HOH388 4.3 23.5 1.0 O A:ILE43 4.7 13.4 1.0 N A:ILE43 4.7 11.3 1.0 CG A:ARG42 4.9 19.9 1.0 CB A:GLU31 4.9 16.8 1.0 CA A:ARG42 4.9 12.6 1.0

Cadmium binding site 4 out of 6 in the Esterase ALINE4 Mutant-S13A


Mono view


Stereo pair view

A full contact list of Cadmium with other atoms in the Cd binding site number 4 of Esterase ALINE4 Mutant-S13A within 5.0Å range: probe atom residue distance (Å) B Occ A:Cd204 b:16.4 occ:0.52 ND1 A:HIS163 2.2 38.4 1.0 CE1 A:HIS165 2.3 43.5 1.0 NE2 A:HIS165 2.7 39.7 1.0 CE1 A:HIS163 3.1 46.0 1.0 CG A:HIS163 3.4 39.6 1.0 ND1 A:HIS165 3.5 42.6 1.0 O A:HOH302 3.7 19.1 1.0 CB A:HIS163 3.7 36.5 1.0 CD2 A:HIS165 4.0 38.7 1.0 CG A:HIS165 4.3 35.4 1.0 NE2 A:HIS163 4.3 52.1 1.0 CD2 A:HIS163 4.4 41.8 1.0 CA A:HIS163 4.5 30.0 1.0

Cadmium binding site 5 out of 6 in the Esterase ALINE4 Mutant-S13A


Mono view


Stereo pair view

A full contact list of Cadmium with other atoms in the Cd binding site number 5 of Esterase ALINE4 Mutant-S13A within 5.0Å range: probe atom residue distance (Å) B Occ A:Cd205 b:26.8 occ:0.74 O A:HOH369 2.2 34.8 1.0 OD1 A:ASN180 2.5 18.6 1.0 CG A:ASN180 3.2 17.9 1.0 ND2 A:ASN180 3.6 16.9 1.0 CB A:ASN180 4.3 12.2 1.0 CA A:ASN180 4.8 11.0 1.0

Cadmium binding site 6 out of 6 in the Esterase ALINE4 Mutant-S13A


Mono view


Stereo pair view

A full contact list of Cadmium with other atoms in the Cd binding site number 6 of Esterase ALINE4 Mutant-S13A within 5.0Å range: probe atom residue distance (Å) B Occ A:Cd206 b:38.2 occ:0.54 OE2 A:GLU24 2.5 20.7 1.0 CD A:GLU24 3.4 18.9 1.0 CG A:GLU24 3.6 15.9 1.0 O A:HOH304 3.7 24.1 1.0 O A:HOH313 4.1 39.0 1.0 NZ A:LYS29 4.5 19.1 1.0 OE1 A:GLU24 4.6 21.1 1.0 O A:HOH432 4.8 43.7 1.0

Z.Li, L.Li, Y.Huo, Z.Chen, Y.Zhao, J.Huang, S.Jian, Z.Rong, D.Wu, J.Gan, X.Hu, J.Li, X.W.Xu. Structure-Guided Protein Engineering Increases Enzymatic Activities of the Sgnh Family Esterases. Biotechnol Biofuels V. 13 107 2020.
ISSN: ESSN 1754-6834
PubMed: 32549911
DOI: 10.1186/S13068-020-01742-8