Calcium in PDB 2taa: Structure and Possible Catalytic Residues of Taka-Amylase A

All present enzymatic activity of Structure and Possible Catalytic Residues of Taka-Amylase A:
3.2.1.1;

The structure of Structure and Possible Catalytic Residues of Taka-Amylase A, PDB code: 2taa was solved by M.Kusunoki, Y.Matsuura, N.Tanaka, M.Kakudo, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	N/A / 3.00
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	91.900, 133.300, 94.300, 90.00, 102.70, 90.00
R / Rfree (%)	n/a / n/a

The binding sites of Calcium atom in the Structure and Possible Catalytic Residues of Taka-Amylase A (pdb code 2taa). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 3 binding sites of Calcium where determined in the Structure and Possible Catalytic Residues of Taka-Amylase A, PDB code: 2taa:
Jump to Calcium binding site number: 1; 2; 3;

Calcium binding site 1 out of 3 in the Structure and Possible Catalytic Residues of Taka-Amylase A


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Structure and Possible Catalytic Residues of Taka-Amylase A within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca479 b:0.0 occ:1.00 OD1 A:ASN121 2.1 0.0 1.0 CG A:ASN121 2.9 0.0 1.0 OD2 A:ASP175 3.0 0.0 1.0 OD1 A:ASP175 3.1 0.0 1.0 CG A:ASP175 3.3 0.0 1.0 O A:GLU162 3.5 0.0 1.0 ND2 A:ASN121 3.6 0.0 1.0 OD2 A:ASP177 3.8 0.0 1.0 O A:LEU176 3.9 0.0 1.0 CB A:ASN121 4.0 0.0 1.0 C A:GLU162 4.1 0.0 1.0 O A:HIS210 4.5 0.0 1.0 N A:ASP163 4.6 0.0 1.0 CB A:ASP177 4.6 0.0 1.0 O A:VAL211 4.6 0.0 1.0 CG A:ASP177 4.6 0.0 1.0 CA A:ASP163 4.7 0.0 1.0 CA A:ASN121 4.7 0.0 1.0 O A:ASP163 4.8 0.0 1.0 CA A:GLU162 4.9 0.0 1.0 CB A:ASP175 4.9 0.0 1.0 O A:ASN121 4.9 0.0 1.0

Calcium binding site 2 out of 3 in the Structure and Possible Catalytic Residues of Taka-Amylase A


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Structure and Possible Catalytic Residues of Taka-Amylase A within 5.0Å range: probe atom residue distance (Å) B Occ B:Ca479 b:0.0 occ:1.00 OD1 B:ASN121 2.1 0.0 1.0 CG B:ASN121 2.9 0.0 1.0 OD2 B:ASP175 3.0 0.0 1.0 OD1 B:ASP175 3.1 0.0 1.0 CG B:ASP175 3.3 0.0 1.0 O B:GLU162 3.5 0.0 1.0 ND2 B:ASN121 3.6 0.0 1.0 OD2 B:ASP177 3.8 0.0 1.0 O B:LEU176 3.9 0.0 1.0 CB B:ASN121 4.0 0.0 1.0 C B:GLU162 4.1 0.0 1.0 O B:HIS210 4.5 0.0 1.0 N B:ASP163 4.6 0.0 1.0 CB B:ASP177 4.6 0.0 1.0 O B:VAL211 4.6 0.0 1.0 CG B:ASP177 4.6 0.0 1.0 CA B:ASP163 4.7 0.0 1.0 CA B:ASN121 4.7 0.0 1.0 O B:ASP163 4.8 0.0 1.0 CA B:GLU162 4.9 0.0 1.0 CB B:ASP175 4.9 0.0 1.0 O B:ASN121 4.9 0.0 1.0

Calcium binding site 3 out of 3 in the Structure and Possible Catalytic Residues of Taka-Amylase A


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 3 of Structure and Possible Catalytic Residues of Taka-Amylase A within 5.0Å range: probe atom residue distance (Å) B Occ C:Ca479 b:0.0 occ:1.00 OD1 C:ASN121 2.1 0.0 1.0 CG C:ASN121 2.9 0.0 1.0 OD2 C:ASP175 3.0 0.0 1.0 OD1 C:ASP175 3.1 0.0 1.0 CG C:ASP175 3.3 0.0 1.0 O C:GLU162 3.5 0.0 1.0 ND2 C:ASN121 3.6 0.0 1.0 OD2 C:ASP177 3.8 0.0 1.0 O C:LEU176 3.9 0.0 1.0 CB C:ASN121 4.0 0.0 1.0 C C:GLU162 4.1 0.0 1.0 O C:HIS210 4.5 0.0 1.0 N C:ASP163 4.6 0.0 1.0 CB C:ASP177 4.6 0.0 1.0 O C:VAL211 4.6 0.0 1.0 CG C:ASP177 4.6 0.0 1.0 CA C:ASP163 4.7 0.0 1.0 CA C:ASN121 4.7 0.0 1.0 O C:ASP163 4.8 0.0 1.0 CA C:GLU162 4.9 0.0 1.0 CB C:ASP175 4.9 0.0 1.0 O C:ASN121 4.9 0.0 1.0

Y.Matsuura, M.Kusunoki, W.Harada, M.Kakudo. Structure and Possible Catalytic Residues of Taka-Amylase A J.Biochem.(Tokyo) V. 95 697 1984.
ISSN: ISSN 0021-924X
PubMed: 6609921