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Calcium in PDB 1z32: Structure-Function Relationships in Human Salivary Alpha-Amylase: Role of Aromatic Residues

Enzymatic activity of Structure-Function Relationships in Human Salivary Alpha-Amylase: Role of Aromatic Residues

All present enzymatic activity of Structure-Function Relationships in Human Salivary Alpha-Amylase: Role of Aromatic Residues:
3.2.1.1;

Protein crystallography data

The structure of Structure-Function Relationships in Human Salivary Alpha-Amylase: Role of Aromatic Residues, PDB code: 1z32 was solved by N.Ramasubbu, C.Ragunath, K.Sundar, P.J.Mishra, G.Gyemant, L.Kandra, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 19.84 / 1.60
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 51.657, 73.513, 134.362, 90.00, 90.00, 90.00
R / Rfree (%) 17.1 / 19.2

Other elements in 1z32:

The structure of Structure-Function Relationships in Human Salivary Alpha-Amylase: Role of Aromatic Residues also contains other interesting chemical elements:

Chlorine (Cl) 1 atom

Calcium Binding Sites:

The binding sites of Calcium atom in the Structure-Function Relationships in Human Salivary Alpha-Amylase: Role of Aromatic Residues (pdb code 1z32). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total only one binding site of Calcium was determined in the Structure-Function Relationships in Human Salivary Alpha-Amylase: Role of Aromatic Residues, PDB code: 1z32:

Calcium binding site 1 out of 1 in 1z32

Go back to Calcium Binding Sites List in 1z32
Calcium binding site 1 out of 1 in the Structure-Function Relationships in Human Salivary Alpha-Amylase: Role of Aromatic Residues


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Structure-Function Relationships in Human Salivary Alpha-Amylase: Role of Aromatic Residues within 5.0Å range:
probe atom residue distance (Å) B Occ
X:Ca497

b:18.5
occ:1.00
 O X:ARG158 2.4 19.3 1.0
OD1 X:ASN100 2.4 17.6 1.0
O X:HIS201 2.4 17.1 1.0
O X:HOH638 2.5 16.7 1.0
O X:HOH650 2.5 18.6 1.0
OD2 X:ASP167 2.5 18.4 1.0
O X:HOH658 2.6 20.7 1.0
OD1 X:ASP167 2.6 18.2 1.0
CG X:ASP167 2.9 19.5 1.0
C X:ARG158 3.4 20.1 1.0
CG X:ASN100 3.5 16.8 1.0
C X:HIS201 3.6 17.2 1.0
ND2 X:ASN100 4.0 17.3 1.0
CA X:ARG158 4.1 19.9 1.0
CB X:HIS201 4.3 17.6 1.0
O X:ASN100 4.4 17.4 1.0
CB X:ASP167 4.4 19.4 1.0
N X:ASP159 4.5 20.6 1.0
CA X:HIS201 4.5 17.4 1.0
ND2 X:ASN137 4.5 21.8 1.0
N X:MET202 4.5 17.4 1.0
O X:HOH715 4.6 26.2 1.0
O X:CYS160 4.6 20.8 1.0
CG X:MET202 4.7 17.3 1.0
CA X:MET202 4.7 17.6 1.0
O X:VAL157 4.7 20.1 1.0
CB X:ASN100 4.8 17.1 1.0
CA X:ASP159 4.8 21.1 1.0
O X:LEU168 4.8 19.5 1.0
O X:HOH652 4.9 18.3 1.0
CB X:ARG158 5.0 19.8 1.0

Reference:

N.Ramasubbu, C.Ragunath, K.Sundar, P.J.Mishra, G.Gyemant, L.Kandra. Structure-Function Relationships in Human Salivary Alpha-Amylase: Role of Aromatic Residues To Be Published.
Page generated: Sat Dec 12 03:29:38 2020

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