Calcium in PDB 1cxl: Complex Between A Covalent Intermediate and Bacillus Circulans Strain 251 Cgtase E257Q

All present enzymatic activity of Complex Between A Covalent Intermediate and Bacillus Circulans Strain 251 Cgtase E257Q:
2.4.1.19;

The structure of Complex Between A Covalent Intermediate and Bacillus Circulans Strain 251 Cgtase E257Q, PDB code: 1cxl was solved by J.C.M.Uitdehaag, B.W.Dijkstra, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	8.00 / 1.81
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	117.071, 109.281, 65.335, 90.00, 90.00, 90.00
R / Rfree (%)	n/a / n/a

The structure of Complex Between A Covalent Intermediate and Bacillus Circulans Strain 251 Cgtase E257Q also contains other interesting chemical elements:

Fluorine

(F)

2 atoms

The binding sites of Calcium atom in the Complex Between A Covalent Intermediate and Bacillus Circulans Strain 251 Cgtase E257Q (pdb code 1cxl). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the Complex Between A Covalent Intermediate and Bacillus Circulans Strain 251 Cgtase E257Q, PDB code: 1cxl:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in the Complex Between A Covalent Intermediate and Bacillus Circulans Strain 251 Cgtase E257Q


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Complex Between A Covalent Intermediate and Bacillus Circulans Strain 251 Cgtase E257Q within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca688 b:18.7 occ:1.00 OD1 A:ASN33 2.3 23.3 1.0 OD2 A:ASP53 2.3 20.5 1.0 OD1 A:ASP27 2.3 20.9 1.0 O A:GLY51 2.5 13.8 1.0 OD1 A:ASN32 2.5 16.9 1.0 O A:HOH969 2.5 18.8 1.0 O A:ASN29 2.5 17.7 1.0 CG A:ASP27 3.2 20.2 1.0 C A:ASN29 3.4 18.7 1.0 CG A:ASP53 3.4 19.2 1.0 CG A:ASN33 3.5 29.2 1.0 C A:GLY51 3.5 16.2 1.0 CG A:ASN32 3.7 27.3 1.0 CB A:ASP53 3.8 14.7 1.0 OD2 A:ASP27 3.9 22.2 1.0 CA A:GLY51 4.0 13.7 1.0 N A:ASN33 4.1 17.4 1.0 N A:PRO30 4.1 18.2 1.0 CA A:PRO30 4.1 18.7 1.0 N A:ASN29 4.1 14.6 1.0 CB A:ASP27 4.2 16.5 1.0 CA A:ASN29 4.3 14.3 1.0 O A:ALA111 4.3 16.5 1.0 ND2 A:ASN33 4.3 14.9 1.0 ND2 A:ASN32 4.3 14.9 1.0 CA A:ASN33 4.3 17.8 1.0 C A:ASN32 4.4 20.7 1.0 OD1 A:ASP53 4.4 17.3 1.0 CA A:ASP27 4.4 15.6 1.0 CB A:ASN33 4.5 19.3 1.0 C A:PRO30 4.6 22.0 1.0 N A:ASN32 4.6 18.6 1.0 CB A:ASN29 4.7 17.2 1.0 N A:GLY52 4.7 13.6 1.0 C A:GLY52 4.7 17.2 1.0 N A:ASP53 4.8 13.7 1.0 C A:ASP27 4.8 18.7 1.0 CA A:ASN32 4.8 17.0 1.0 CB A:ASN32 4.8 16.9 1.0 O A:ASN32 4.8 20.6 1.0 O A:HOH741 4.8 15.0 1.0 O A:PRO30 4.9 21.0 1.0 N A:GLY28 4.9 16.7 1.0 O A:GLY52 4.9 15.9 1.0 CA A:ASP53 5.0 13.6 1.0

Calcium binding site 2 out of 2 in the Complex Between A Covalent Intermediate and Bacillus Circulans Strain 251 Cgtase E257Q


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Complex Between A Covalent Intermediate and Bacillus Circulans Strain 251 Cgtase E257Q within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca689 b:12.3 occ:1.00 O A:HOH1004 2.3 13.0 1.0 O A:HOH959 2.4 10.9 1.0 OD1 A:ASN139 2.4 9.7 1.0 O A:HIS233 2.4 10.9 1.0 O A:HOH941 2.4 10.2 1.0 OD2 A:ASP199 2.5 12.3 1.0 O A:ILE190 2.5 13.1 1.0 OD1 A:ASP199 2.5 14.1 1.0 CG A:ASP199 2.8 14.5 1.0 CG A:ASN139 3.5 13.4 1.0 C A:HIS233 3.6 12.7 1.0 C A:ILE190 3.6 13.3 1.0 ND2 A:ASN139 4.0 12.6 1.0 O A:ASN139 4.3 15.5 1.0 CA A:ILE190 4.3 8.6 1.0 CB A:ASP199 4.3 12.9 1.0 CB A:HIS233 4.5 10.1 1.0 N A:MET234 4.5 8.9 1.0 O A:LYS192 4.5 16.9 1.0 CA A:MET234 4.5 8.0 1.0 O A:GLY189 4.5 13.4 1.0 CG A:MET234 4.6 10.0 1.0 CA A:HIS233 4.6 9.0 1.0 ND1 A:HIS176 4.6 17.6 1.0 O A:HOH756 4.7 10.6 1.0 O A:LEU200 4.8 12.9 1.0 N A:TYR191 4.8 11.3 1.0 CB A:ASN139 4.8 8.9 1.0 CG2 A:ILE190 4.8 10.7 1.0 CE1 A:HIS176 4.9 17.8 1.0

J.C.Uitdehaag, R.Mosi, K.H.Kalk, B.A.Van Der Veen, L.Dijkhuizen, S.G.Withers, B.W.Dijkstra. X-Ray Structures Along the Reaction Pathway of Cyclodextrin Glycosyltransferase Elucidate Catalysis in the Alpha-Amylase Family. Nat.Struct.Biol. V. 6 432 1999.
ISSN: ISSN 1072-8368
PubMed: 10331869
DOI: 10.1038/8235