Calcium in PDB 5w78: Human Acyloxyacyl Hydrolase (Aoah), Proteolytically Processed

All present enzymatic activity of Human Acyloxyacyl Hydrolase (Aoah), Proteolytically Processed:
3.1.1.77;

The structure of Human Acyloxyacyl Hydrolase (Aoah), Proteolytically Processed, PDB code: 5w78 was solved by A.Gorelik, K.Illes, B.Nagar, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	47.66 / 2.27
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	50.402, 87.356, 146.510, 90.00, 90.00, 90.00
R / Rfree (%)	16.6 / 20.1

The binding sites of Calcium atom in the Human Acyloxyacyl Hydrolase (Aoah), Proteolytically Processed (pdb code 5w78). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the Human Acyloxyacyl Hydrolase (Aoah), Proteolytically Processed, PDB code: 5w78:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in the Human Acyloxyacyl Hydrolase (Aoah), Proteolytically Processed


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Human Acyloxyacyl Hydrolase (Aoah), Proteolytically Processed within 5.0Å range: probe atom residue distance (Å) B Occ B:Ca601 b:43.9 occ:1.00 O B:VAL213 2.3 26.5 1.0 OD2 B:ASP205 2.4 34.0 1.0 O B:HOH780 2.4 35.4 1.0 O B:ASP210 2.5 33.2 1.0 O B:ASN207 2.5 32.0 1.0 OD1 B:ASP205 2.8 27.6 1.0 CG B:ASP205 2.9 32.5 1.0 HA B:ASP208 3.0 39.1 1.0 HB B:VAL213 3.1 28.8 1.0 HA B:GLU211 3.4 50.0 1.0 H B:VAL213 3.4 32.5 1.0 C B:VAL213 3.4 25.8 1.0 C B:ASN207 3.4 28.3 1.0 C B:ASP210 3.5 37.3 1.0 H B:ASP210 3.6 41.9 1.0 CA B:ASP208 3.9 32.6 1.0 CB B:VAL213 3.9 24.0 1.0 H B:ASN207 3.9 35.8 1.0 CA B:VAL213 4.0 25.6 1.0 HB3 B:TYR214 4.0 30.3 1.0 HG12 B:VAL213 4.0 29.8 1.0 N B:ASP208 4.0 30.9 1.0 N B:VAL213 4.0 27.1 1.0 HB3 B:ASN207 4.1 32.2 1.0 CA B:GLU211 4.2 41.6 1.0 N B:GLU211 4.3 38.1 1.0 N B:ASP210 4.3 35.0 1.0 HB3 B:ASP210 4.4 42.9 1.0 CA B:ASN207 4.4 27.4 1.0 CB B:ASP205 4.4 29.8 1.0 CG1 B:VAL213 4.5 24.9 1.0 HA B:TYR214 4.5 29.5 1.0 CA B:ASP210 4.5 33.2 1.0 C B:ASP208 4.5 34.8 1.0 N B:ASN207 4.5 29.8 1.0 N B:TYR214 4.5 24.2 1.0 C B:GLU211 4.6 35.2 1.0 HD2 B:TYR214 4.7 36.2 1.0 HB2 B:ASP205 4.7 35.7 1.0 CB B:ASN207 4.7 26.8 1.0 HG11 B:VAL213 4.8 29.8 1.0 HB3 B:ASP205 4.8 35.7 1.0 CA B:TYR214 4.8 24.6 1.0 H B:ASP208 4.8 37.0 1.0 CB B:TYR214 4.9 25.2 1.0 N B:SER209 4.9 37.2 1.0 HA B:VAL213 4.9 30.7 1.0 H B:SER209 4.9 44.7 1.0 HB3 B:ASP208 4.9 43.5 1.0 CB B:ASP208 5.0 36.2 1.0

Calcium binding site 2 out of 2 in the Human Acyloxyacyl Hydrolase (Aoah), Proteolytically Processed


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Human Acyloxyacyl Hydrolase (Aoah), Proteolytically Processed within 5.0Å range: probe atom residue distance (Å) B Occ B:Ca602 b:20.4 occ:1.00 O B:ILE233 2.2 19.9 1.0 OD1 B:ASN229 2.3 24.7 1.0 OE2 B:GLU245 2.3 24.2 1.0 OD2 B:ASP227 2.3 24.5 1.0 OD2 B:ASP223 2.3 25.5 1.0 OD1 B:ASN231 2.5 24.1 1.0 H B:ILE233 3.3 28.4 1.0 CG B:ASN231 3.3 20.1 1.0 HD21 B:ASN231 3.3 26.9 1.0 C B:ILE233 3.4 20.9 1.0 CG B:ASN229 3.4 22.3 1.0 HB B:ILE233 3.4 22.2 1.0 CG B:ASP223 3.5 25.2 1.0 CD B:GLU245 3.5 31.3 1.0 CG B:ASP227 3.5 23.0 1.0 H B:ASN229 3.6 28.9 1.0 HD21 B:ASN229 3.6 30.1 1.0 H B:ASN231 3.6 24.0 1.0 ND2 B:ASN231 3.6 22.4 1.0 HA B:ASP227 3.7 31.4 1.0 ND2 B:ASN229 3.9 25.1 1.0 N B:ILE233 3.9 23.7 1.0 HB2 B:ASP223 4.0 29.3 1.0 CA B:ILE233 4.0 21.7 1.0 HB3 B:ASP223 4.0 29.3 1.0 CB B:ASP223 4.1 24.4 1.0 CB B:ILE233 4.2 18.5 1.0 HB3 B:TRP234 4.2 30.2 1.0 OE1 B:GLU245 4.2 34.4 1.0 HB2 B:GLU245 4.2 36.1 1.0 H B:SER228 4.2 25.5 1.0 HB3 B:PRO219 4.3 33.7 1.0 OD1 B:ASP227 4.3 26.3 1.0 CA B:ASP227 4.4 26.2 1.0 N B:ASN231 4.4 20.0 1.0 N B:ASN229 4.4 24.1 1.0 HA B:TRP234 4.4 32.8 1.0 H B:CYS230 4.4 27.8 1.0 CB B:ASP227 4.4 23.4 1.0 HD22 B:ASN231 4.4 26.9 1.0 N B:TRP234 4.5 20.5 1.0 OD1 B:ASP223 4.5 23.9 1.0 CB B:ASN231 4.5 20.1 1.0 N B:SER228 4.6 21.2 1.0 H B:GLY232 4.6 26.7 1.0 HG22 B:ILE233 4.6 29.0 1.0 CG B:GLU245 4.6 35.4 1.0 C B:ASP227 4.6 23.5 1.0 CB B:ASN229 4.7 27.4 1.0 HG2 B:GLU245 4.7 42.5 1.0 HB2 B:ASP227 4.7 28.1 1.0 N B:CYS230 4.7 23.2 1.0 HD22 B:ASN229 4.7 30.1 1.0 N B:GLY232 4.8 22.2 1.0 CA B:TRP234 4.8 27.4 1.0 HB3 B:ASN231 4.8 24.1 1.0 CA B:ASN231 4.8 18.3 1.0 CA B:ASN229 4.9 22.4 1.0 C B:ASN229 4.9 23.2 1.0 HG B:SER228 4.9 28.6 1.0 C B:ASN231 4.9 19.4 1.0 CB B:GLU245 4.9 30.1 1.0 CB B:TRP234 4.9 25.1 1.0 HA B:ILE233 4.9 26.1 1.0 CG2 B:ILE233 5.0 24.2 1.0

A.Gorelik, K.Illes, B.Nagar. Crystal Structure of the Mammalian Lipopolysaccharide Detoxifier. Proc. Natl. Acad. Sci. V. 115 E896 2018U.S.A..
ISSN: ESSN 1091-6490
PubMed: 29343645
DOI: 10.1073/PNAS.1719834115