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Chlorine in PDB 1kbb: 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: 1kbb 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 (°) 52.920, 74.770, 136.940, 90.00, 90.00, 90.00
R / Rfree (%) 17.2 / 19.4

Other elements in 1kbb:

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:

Calcium (Ca) 1 atom

Chlorine Binding Sites:

The binding sites of Chlorine 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 1kbb). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine 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: 1kbb:

Chlorine binding site 1 out of 1 in 1kbb

Go back to Chlorine Binding Sites List in 1kbb
Chlorine 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 Chlorine with other atoms in the Cl 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:Cl498

b:16.4
occ:1.00
 NE A:ARG195 3.1 13.5 1.0
NH2 A:ARG337 3.2 14.0 1.0
O A:HOH538 3.3 14.4 1.0
NH1 A:ARG337 3.4 11.7 1.0
NH2 A:ARG195 3.4 9.8 1.0
ND2 A:ASN298 3.5 17.4 1.0
CZ A:ARG195 3.7 12.6 1.0
CZ A:ARG337 3.7 14.2 1.0
CG2 A:THR254 4.0 13.9 1.0
CZ A:PHE256 4.0 14.2 1.0
CD A:ARG195 4.2 13.5 1.0
CB A:ASN298 4.4 14.2 1.0
CG A:ASN298 4.5 16.4 1.0
CB A:ALA233 4.6 27.2 1.0
CE2 A:PHE256 4.6 15.1 1.0
CZ A:PHE295 4.7 14.5 1.0
CB A:THR254 4.7 15.5 1.0
CE1 A:PHE295 4.9 13.8 1.0
CE1 A:HIS299 4.9 17.2 1.0
CE1 A:PHE256 4.9 14.9 1.0
CG A:ARG195 4.9 14.7 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 08:39:50 2020

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