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Calcium in PDB 1kbk: Mechanistic Analyses of Catalysis in Human Pancreatic Alpha-Amylase: Detailed Kinetic and Structural Studies of Mutants of Three Conserved Carboxylic Acids

Enzymatic activity of Mechanistic Analyses of Catalysis in Human Pancreatic Alpha-Amylase: Detailed Kinetic and Structural Studies of Mutants of Three Conserved Carboxylic Acids

All present enzymatic activity of Mechanistic Analyses of Catalysis in Human Pancreatic Alpha-Amylase: Detailed Kinetic and Structural Studies of Mutants of Three Conserved Carboxylic Acids:
3.2.1.1;

Protein crystallography data

The structure of Mechanistic Analyses of Catalysis in Human Pancreatic Alpha-Amylase: Detailed Kinetic and Structural Studies of Mutants of Three Conserved Carboxylic Acids, PDB code: 1kbk was solved by E.H.Rydberg, C.Li, R.Maurus, C.M.Overall, G.D.Brayer, S.G.Withers, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 10.00 / 1.90
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 52.880, 69.520, 131.600, 90.00, 90.00, 90.00
R / Rfree (%) 17.1 / 17.7

Other elements in 1kbk:

The structure of Mechanistic Analyses of Catalysis in Human Pancreatic Alpha-Amylase: Detailed Kinetic and Structural Studies of Mutants of Three Conserved Carboxylic Acids also contains other interesting chemical elements:

Chlorine (Cl) 1 atom

Calcium Binding Sites:

The binding sites of Calcium atom in the Mechanistic Analyses of Catalysis in Human Pancreatic Alpha-Amylase: Detailed Kinetic and Structural Studies of Mutants of Three Conserved Carboxylic Acids (pdb code 1kbk). 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 Mechanistic Analyses of Catalysis in Human Pancreatic Alpha-Amylase: Detailed Kinetic and Structural Studies of Mutants of Three Conserved Carboxylic Acids, PDB code: 1kbk:

Calcium binding site 1 out of 1 in 1kbk

Go back to Calcium Binding Sites List in 1kbk
Calcium binding site 1 out of 1 in the Mechanistic Analyses of Catalysis in Human Pancreatic Alpha-Amylase: Detailed Kinetic and Structural Studies of Mutants of Three Conserved Carboxylic Acids


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Mechanistic Analyses of Catalysis in Human Pancreatic Alpha-Amylase: Detailed Kinetic and Structural Studies of Mutants of Three Conserved Carboxylic Acids within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca497

b:12.0
occ:1.00
O A:ARG158 2.4 13.9 1.0
O A:HIS201 2.4 10.7 1.0
OD1 A:ASN100 2.5 12.4 1.0
OD1 A:ASP167 2.6 12.2 1.0
OD2 A:ASP167 2.6 14.5 1.0
O A:HOH539 2.6 16.8 1.0
O A:HOH534 2.7 14.5 1.0
CG A:ASP167 2.9 12.9 1.0
C A:ARG158 3.5 15.2 1.0
CG A:ASN100 3.6 13.2 1.0
C A:HIS201 3.6 11.3 1.0
ND2 A:ASN100 4.0 10.5 1.0
CA A:ARG158 4.1 14.7 1.0
CB A:HIS201 4.2 12.3 1.0
CB A:ASP167 4.4 10.4 1.0
O A:ASN100 4.4 10.6 1.0
CA A:HIS201 4.5 11.4 1.0
O A:CYS160 4.5 14.4 1.0
N A:ASP159 4.5 14.9 1.0
N A:MET202 4.6 11.5 1.0
ND2 A:ASN137 4.6 16.5 1.0
O A:HOH562 4.6 17.7 1.0
CA A:MET202 4.7 11.4 1.0
O A:VAL157 4.8 17.5 1.0
CG A:MET202 4.8 12.3 1.0
CA A:ASP159 4.8 14.7 1.0
CB A:ASN100 4.9 10.8 1.0
O A:LEU168 4.9 13.4 1.0
O A:HOH506 4.9 12.0 1.0

Reference:

E.H.Rydberg, C.Li, R.Maurus, C.M.Overall, G.D.Brayer, S.G.Withers. Mechanistic Analyses of Catalysis in Human Pancreatic Alpha-Amylase: Detailed Kinetic and Structural Studies of Mutants of Three Conserved Carboxylic Acids. Biochemistry V. 41 4492 2002.
ISSN: ISSN 0006-2960
PubMed: 11914097
DOI: 10.1021/BI011821Z
Page generated: Sat Dec 12 03:03:36 2020

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