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Chlorine in PDB 3ij7: Directed 'in Situ' Elongation As A Strategy to Characterize the Covalent Glycosyl-Enzyme Catalytic Intermediate of Human Pancreatic A-Amylase

Enzymatic activity of Directed 'in Situ' Elongation As A Strategy to Characterize the Covalent Glycosyl-Enzyme Catalytic Intermediate of Human Pancreatic A-Amylase

All present enzymatic activity of Directed 'in Situ' Elongation As A Strategy to Characterize the Covalent Glycosyl-Enzyme Catalytic Intermediate of Human Pancreatic A-Amylase:
3.2.1.1;

Protein crystallography data

The structure of Directed 'in Situ' Elongation As A Strategy to Characterize the Covalent Glycosyl-Enzyme Catalytic Intermediate of Human Pancreatic A-Amylase, PDB code: 3ij7 was solved by C.Li, R.Zhang, S.G.Withers, G.D.Brayer, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 28.43 / 2.00
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 52.140, 67.820, 129.920, 90.00, 90.00, 90.00
R / Rfree (%) 19.3 / 22.9

Other elements in 3ij7:

The structure of Directed 'in Situ' Elongation As A Strategy to Characterize the Covalent Glycosyl-Enzyme Catalytic Intermediate of Human Pancreatic A-Amylase also contains other interesting chemical elements:

Fluorine (F) 2 atoms
Calcium (Ca) 1 atom

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Directed 'in Situ' Elongation As A Strategy to Characterize the Covalent Glycosyl-Enzyme Catalytic Intermediate of Human Pancreatic A-Amylase (pdb code 3ij7). 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 Directed 'in Situ' Elongation As A Strategy to Characterize the Covalent Glycosyl-Enzyme Catalytic Intermediate of Human Pancreatic A-Amylase, PDB code: 3ij7:

Chlorine binding site 1 out of 1 in 3ij7

Go back to Chlorine Binding Sites List in 3ij7
Chlorine binding site 1 out of 1 in the Directed 'in Situ' Elongation As A Strategy to Characterize the Covalent Glycosyl-Enzyme Catalytic Intermediate of Human Pancreatic A-Amylase


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Directed 'in Situ' Elongation As A Strategy to Characterize the Covalent Glycosyl-Enzyme Catalytic Intermediate of Human Pancreatic A-Amylase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl498

b:18.2
occ:1.00
 NH2 A:ARG337 3.1 12.8 1.0
NH2 A:ARG195 3.1 15.9 1.0
NE A:ARG195 3.2 16.7 1.0
NH1 A:ARG337 3.3 14.9 1.0
O A:HOH515 3.3 14.4 1.0
ND2 A:ASN298 3.3 11.6 1.0
CZ A:ARG195 3.6 14.8 1.0
CZ A:ARG337 3.6 13.3 1.0
CG2 A:THR254 3.8 14.9 1.0
CZ A:PHE256 3.9 10.8 1.0
CG A:GLU233 4.1 19.9 1.0
CG A:ASN298 4.3 14.1 1.0
CB A:ASN298 4.3 13.0 1.0
CD A:ARG195 4.4 16.4 1.0
CZ A:PHE295 4.5 16.3 1.0
CE1 A:PHE256 4.5 13.0 1.0
CB A:THR254 4.6 15.8 1.0
O A:HOH549 4.7 18.3 1.0
CB A:GLU233 4.7 18.1 1.0
CE1 A:PHE295 4.8 17.6 1.0
CD A:GLU233 4.8 20.8 1.0
CE2 A:PHE256 4.8 13.0 1.0
OE2 A:GLU233 4.8 22.2 1.0
CG A:ARG195 4.8 17.1 1.0
NH1 A:ARG195 4.9 13.3 1.0
NE A:ARG337 4.9 15.5 1.0
CE2 A:PHE295 5.0 15.9 1.0

Reference:

R.Zhang, C.Li, L.K.Williams, B.P.Rempel, G.D.Brayer, S.G.Withers. Directed "in Situ" Inhibitor Elongation As A Strategy to Structurally Characterize the Covalent Glycosyl-Enzyme Intermediate of Human Pancreatic Alpha-Amylase Biochemistry V. 48 10752 2009.
ISSN: ISSN 0006-2960
PubMed: 19803533
DOI: 10.1021/BI901400P
Page generated: Fri Jul 11 06:23:12 2025

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