Calcium in PDB 1mpx: Alpha-Amino Acid Ester Hydrolase Labeled with Selenomethionine

All present enzymatic activity of Alpha-Amino Acid Ester Hydrolase Labeled with Selenomethionine:
3.1.1.43;

The structure of Alpha-Amino Acid Ester Hydrolase Labeled with Selenomethionine, PDB code: 1mpx was solved by T.R.M.Barends, J.J.Polderman-Tijmes, P.A.Jekel, C.M.H.Hensgens, E.J.Devries, D.B.Janssen, B.W.Dijkstra, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	40.00 / 1.90
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	89.772, 126.016, 132.291, 90.00, 91.06, 90.00
R / Rfree (%)	14.9 / 17.8

The binding sites of Calcium atom in the Alpha-Amino Acid Ester Hydrolase Labeled with Selenomethionine (pdb code 1mpx). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 4 binding sites of Calcium where determined in the Alpha-Amino Acid Ester Hydrolase Labeled with Selenomethionine, PDB code: 1mpx:
Jump to Calcium binding site number: 1; 2; 3; 4;

Calcium binding site 1 out of 4 in the Alpha-Amino Acid Ester Hydrolase Labeled with Selenomethionine


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Alpha-Amino Acid Ester Hydrolase Labeled with Selenomethionine within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca638 b:15.3 occ:1.00 OD1 A:ASN328 2.3 13.1 1.0 O A:ASN331 2.3 13.8 1.0 O A:HOH3085 2.3 16.6 1.0 OD2 A:ASP325 2.4 15.8 1.0 O A:HOH3051 2.4 14.7 1.0 OE2 A:GLU322 2.5 16.2 1.0 OE1 A:GLU322 2.5 19.4 1.0 CD A:GLU322 2.9 19.4 1.0 C A:ASN331 3.4 14.0 1.0 CG A:ASN328 3.5 17.4 1.0 CG A:ASP325 3.5 20.0 1.0 CA A:ASN328 4.1 19.1 1.0 CB A:ASP325 4.2 22.8 1.0 CB A:ASN331 4.2 15.4 1.0 CA A:ASN331 4.2 14.6 1.0 N A:ASN331 4.3 14.5 1.0 OH A:TYR318 4.3 14.3 1.0 C A:ASN328 4.3 18.8 1.0 O A:ASN328 4.4 19.8 1.0 O A:HOH3032 4.4 13.5 1.0 CB A:ASN328 4.4 18.1 1.0 O A:HOH3278 4.4 26.2 1.0 ND2 A:ASN328 4.4 14.1 1.0 CG A:GLU322 4.4 16.3 1.0 CB A:PRO387 4.5 17.6 1.0 CE1 A:TYR318 4.5 11.2 1.0 N A:TYR332 4.5 12.9 1.0 OD1 A:ASP325 4.5 17.9 1.0 O A:PRO387 4.7 13.4 1.0 CA A:TYR332 4.7 14.7 1.0 CZ A:TYR318 4.8 15.7 1.0 ND2 A:ASN331 4.9 11.9 1.0 CA A:PRO387 4.9 17.2 1.0 N A:THR329 5.0 21.3 1.0

Calcium binding site 2 out of 4 in the Alpha-Amino Acid Ester Hydrolase Labeled with Selenomethionine


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Alpha-Amino Acid Ester Hydrolase Labeled with Selenomethionine within 5.0Å range: probe atom residue distance (Å) B Occ B:Ca638 b:14.7 occ:1.00 O B:ASN331 2.2 14.2 1.0 OD1 B:ASN328 2.3 16.0 1.0 O B:HOH3021 2.3 11.9 1.0 O B:HOH3032 2.4 13.1 1.0 OD2 B:ASP325 2.4 15.9 1.0 OE2 B:GLU322 2.6 14.4 1.0 OE1 B:GLU322 2.6 17.4 1.0 CD B:GLU322 2.9 15.6 1.0 C B:ASN331 3.4 13.2 1.0 CG B:ASN328 3.5 14.4 1.0 CG B:ASP325 3.5 22.0 1.0 CA B:ASN328 4.1 16.8 1.0 CA B:ASN331 4.1 13.2 1.0 CB B:ASN331 4.1 11.9 1.0 CB B:ASP325 4.1 19.6 1.0 N B:ASN331 4.2 13.9 1.0 C B:ASN328 4.3 14.8 1.0 OH B:TYR318 4.3 16.4 1.0 O B:ASN328 4.3 16.1 1.0 O B:HOH3232 4.3 23.7 1.0 CB B:ASN328 4.4 15.9 1.0 O B:HOH3084 4.4 16.4 1.0 ND2 B:ASN328 4.4 12.9 1.0 CG B:GLU322 4.4 15.7 1.0 CB B:PRO387 4.4 17.6 1.0 N B:TYR332 4.5 13.7 1.0 CE1 B:TYR318 4.5 11.1 1.0 OD1 B:ASP325 4.5 14.6 1.0 O B:PRO387 4.7 12.6 1.0 CA B:TYR332 4.7 12.6 1.0 CA B:PRO387 4.8 15.4 1.0 CZ B:TYR318 4.9 17.6 1.0 ND2 B:ASN331 4.9 16.4 1.0 N B:THR329 5.0 16.3 1.0

Calcium binding site 3 out of 4 in the Alpha-Amino Acid Ester Hydrolase Labeled with Selenomethionine


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 3 of Alpha-Amino Acid Ester Hydrolase Labeled with Selenomethionine within 5.0Å range: probe atom residue distance (Å) B Occ C:Ca638 b:19.8 occ:1.00 O C:ASN331 2.3 16.6 1.0 OD1 C:ASN328 2.3 20.1 1.0 O C:HOH3064 2.4 18.6 1.0 O C:HOH3019 2.4 15.7 1.0 OD2 C:ASP325 2.4 21.0 1.0 OE2 C:GLU322 2.6 23.8 1.0 OE1 C:GLU322 2.7 27.6 1.0 CD C:GLU322 3.0 25.8 1.0 C C:ASN331 3.4 17.7 1.0 CG C:ASN328 3.5 22.8 1.0 CG C:ASP325 3.6 23.1 1.0 CA C:ASN328 4.0 23.0 1.0 CB C:ASN331 4.1 18.8 1.0 CA C:ASN331 4.2 19.1 1.0 C C:ASN328 4.2 20.0 1.0 CB C:ASP325 4.2 23.4 1.0 O C:ASN328 4.2 20.5 1.0 N C:ASN331 4.3 20.8 1.0 O C:HOH3249 4.3 28.7 1.0 OH C:TYR318 4.4 24.2 1.0 CB C:ASN328 4.4 22.6 1.0 CB C:PRO387 4.4 19.8 1.0 N C:TYR332 4.5 18.9 1.0 O C:HOH3031 4.5 16.4 1.0 ND2 C:ASN328 4.5 18.6 1.0 CE1 C:TYR318 4.5 19.4 1.0 CG C:GLU322 4.5 20.5 1.0 OD1 C:ASP325 4.5 20.8 1.0 O C:PRO387 4.7 18.7 1.0 CA C:TYR332 4.7 16.2 1.0 CA C:PRO387 4.8 19.8 1.0 N C:THR329 4.9 18.9 1.0 CZ C:TYR318 4.9 22.9 1.0 ND2 C:ASN331 4.9 17.7 1.0

Calcium binding site 4 out of 4 in the Alpha-Amino Acid Ester Hydrolase Labeled with Selenomethionine


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 4 of Alpha-Amino Acid Ester Hydrolase Labeled with Selenomethionine within 5.0Å range: probe atom residue distance (Å) B Occ D:Ca638 b:21.1 occ:1.00 O D:ASN331 2.2 21.1 1.0 OD1 D:ASN328 2.3 22.3 1.0 O D:HOH3092 2.4 20.2 1.0 OD2 D:ASP325 2.4 20.5 1.0 O D:HOH3052 2.4 17.9 1.0 OE2 D:GLU322 2.5 21.3 1.0 OE1 D:GLU322 2.6 25.6 1.0 CD D:GLU322 2.9 24.7 1.0 C D:ASN331 3.4 23.2 1.0 CG D:ASN328 3.5 25.9 1.0 CG D:ASP325 3.5 23.9 1.0 CA D:ASN328 4.1 26.3 1.0 CB D:ASN331 4.1 23.0 1.0 CA D:ASN331 4.1 21.0 1.0 CB D:ASP325 4.1 24.0 1.0 O D:HOH3199 4.2 26.6 1.0 C D:ASN328 4.2 23.2 1.0 N D:ASN331 4.3 22.5 1.0 O D:ASN328 4.3 27.1 1.0 OH D:TYR318 4.3 21.0 1.0 CB D:ASN328 4.4 24.3 1.0 O D:HOH3083 4.5 19.6 1.0 CG D:GLU322 4.5 23.7 1.0 CE1 D:TYR318 4.5 19.9 1.0 ND2 D:ASN328 4.5 20.7 1.0 N D:TYR332 4.5 21.1 1.0 OD1 D:ASP325 4.5 17.1 1.0 CB D:PRO387 4.6 17.5 1.0 CA D:TYR332 4.7 20.0 1.0 O D:PRO387 4.8 19.1 1.0 ND2 D:ASN331 4.9 18.0 1.0 CZ D:TYR318 4.9 21.1 1.0 N D:THR329 4.9 24.2 1.0 CA D:PRO387 5.0 18.9 1.0

T.R.Barends, J.J.Polderman-Tijmes, P.A.Jekel, C.M.Hensgens, E.J.De Vries, D.B.Janssen, B.W.Dijkstra. The Sequence and Crystal Structure of the Alpha-Amino Acid Ester Hydrolase From Xanthomonas Citri Define A New Family of Beta-Lactam Antibiotic Acylases. J.Biol.Chem. V. 278 23076 2003.
ISSN: ISSN 0021-9258
PubMed: 12684501
DOI: 10.1074/JBC.M302246200