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Chlorine in PDB 1hx0: Structure of Pig Pancreatic Alpha-Amylase Complexed with the "Truncate" Acarbose Molecule (Pseudotrisaccharide)

Enzymatic activity of Structure of Pig Pancreatic Alpha-Amylase Complexed with the "Truncate" Acarbose Molecule (Pseudotrisaccharide)

All present enzymatic activity of Structure of Pig Pancreatic Alpha-Amylase Complexed with the "Truncate" Acarbose Molecule (Pseudotrisaccharide):
3.2.1.1;

Protein crystallography data

The structure of Structure of Pig Pancreatic Alpha-Amylase Complexed with the "Truncate" Acarbose Molecule (Pseudotrisaccharide), PDB code: 1hx0 was solved by M.Qian, F.Payan, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 35.00 / 1.38
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 69.280, 113.550, 117.160, 90.00, 90.00, 90.00
R / Rfree (%) 10.8 / 13

Other elements in 1hx0:

The structure of Structure of Pig Pancreatic Alpha-Amylase Complexed with the "Truncate" Acarbose Molecule (Pseudotrisaccharide) also contains other interesting chemical elements:

Calcium (Ca) 1 atom

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Structure of Pig Pancreatic Alpha-Amylase Complexed with the "Truncate" Acarbose Molecule (Pseudotrisaccharide) (pdb code 1hx0). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 4 binding sites of Chlorine where determined in the Structure of Pig Pancreatic Alpha-Amylase Complexed with the "Truncate" Acarbose Molecule (Pseudotrisaccharide), PDB code: 1hx0:
Jump to Chlorine binding site number: 1; 2; 3; 4;

Chlorine binding site 1 out of 4 in 1hx0

Go back to Chlorine Binding Sites List in 1hx0
Chlorine binding site 1 out of 4 in the Structure of Pig Pancreatic Alpha-Amylase Complexed with the "Truncate" Acarbose Molecule (Pseudotrisaccharide)


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Structure of Pig Pancreatic Alpha-Amylase Complexed with the "Truncate" Acarbose Molecule (Pseudotrisaccharide) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl498

b:16.1
occ:1.00
 NH1 A:ARG337 3.2 14.5 1.0
O A:HOH6021 3.2 15.4 1.0
NE A:ARG195 3.2 16.0 1.0
NH2 A:ARG337 3.3 14.8 1.0
ND2 A:ASN298 3.3 15.1 1.0
NH2 A:ARG195 3.3 16.2 1.0
CZ A:ARG337 3.7 14.7 1.0
CZ A:ARG195 3.8 14.4 1.0
CG2 A:THR254 3.8 14.2 1.0
CG A:GLU233 4.1 15.7 1.0
CZ A:PHE256 4.1 13.8 1.0
CD A:ARG195 4.3 18.2 1.0
CG A:ASN298 4.4 12.8 1.0
CB A:ASN298 4.4 13.1 1.0
CB A:GLU233 4.4 14.2 1.0
CE2 A:PHE256 4.6 13.9 1.0
CZ A:PHE295 4.8 15.0 1.0
CG A:ARG195 4.8 19.8 1.0
O A:HOH6042 4.8 16.9 1.0
CD A:GLU233 4.9 17.7 1.0
CB A:THR254 4.9 13.2 1.0
OE1 A:GLU233 5.0 19.6 1.0
CE1 A:PHE256 5.0 15.2 1.0

Chlorine binding site 2 out of 4 in 1hx0

Go back to Chlorine Binding Sites List in 1hx0
Chlorine binding site 2 out of 4 in the Structure of Pig Pancreatic Alpha-Amylase Complexed with the "Truncate" Acarbose Molecule (Pseudotrisaccharide)


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Structure of Pig Pancreatic Alpha-Amylase Complexed with the "Truncate" Acarbose Molecule (Pseudotrisaccharide) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl499

b:22.1
occ:1.00
 N A:GLY205 3.2 15.7 1.0
O A:HOH6346 3.3 37.3 1.0
O A:HOH6179 3.4 35.8 0.6
CD A:PRO204 3.7 15.8 1.0
N A:PRO204 3.8 14.0 1.0
CB A:TRP203 3.9 15.1 1.0
CA A:GLY205 3.9 16.7 1.0
CE3 A:TRP203 4.1 18.2 1.0
O A:HOH6571 4.1 51.3 1.0
CB A:PRO204 4.1 16.2 1.0
C A:PRO204 4.2 14.5 1.0
C A:TRP203 4.2 13.8 1.0
CA A:PRO204 4.2 14.1 1.0
CG A:PRO204 4.3 16.7 1.0
CA A:TRP203 4.4 14.4 1.0
O A:HOH6882 4.6 44.5 0.5
CG A:TRP203 4.6 15.5 1.0
CD2 A:TRP203 4.7 16.1 1.0
O A:HOH6179 4.7 22.2 0.5
O A:HOH6255 4.8 26.6 1.0
O A:TRP203 4.9 14.4 1.0
C A:GLY205 5.0 16.3 1.0

Chlorine binding site 3 out of 4 in 1hx0

Go back to Chlorine Binding Sites List in 1hx0
Chlorine binding site 3 out of 4 in the Structure of Pig Pancreatic Alpha-Amylase Complexed with the "Truncate" Acarbose Molecule (Pseudotrisaccharide)


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Structure of Pig Pancreatic Alpha-Amylase Complexed with the "Truncate" Acarbose Molecule (Pseudotrisaccharide) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl501

b:17.9
occ:0.30
 ND2 A:ASN137 2.7 19.1 0.5
O A:HOH6720 2.7 20.6 1.0
CG A:GLU171 2.9 25.9 0.7
OD1 A:ASN137 3.1 14.3 0.5
CD A:GLU171 3.2 34.3 0.7
N A:GLU171 3.2 17.4 1.0
OE2 A:GLU171 3.2 45.9 0.7
CE A:LYS140 3.3 34.1 0.5
CB A:GLU171 3.3 22.0 0.7
NZ A:LYS140 3.3 41.1 0.5
C A:ALA169 3.4 15.5 1.0
CA A:ALA169 3.4 16.1 1.0
CB A:GLU171 3.4 22.8 0.3
N A:LEU170 3.4 16.3 1.0
CD A:LYS140 3.5 33.7 0.5
O A:HOH6204 3.7 18.9 1.0
CG A:ASN137 3.7 16.3 0.5
O A:HOH6273 3.7 29.9 1.0
CB A:ALA169 3.8 18.6 1.0
OD1 A:ASN137 3.8 16.1 0.5
CA A:GLU171 3.9 19.4 1.0
CD A:LYS140 3.9 24.9 0.5
OE1 A:GLU171 4.0 50.0 0.7
O A:ALA169 4.0 17.1 1.0
CG A:ASN137 4.0 17.0 0.5
CE A:LYS140 4.1 27.4 0.5
C A:LEU170 4.2 16.6 1.0
CA A:LEU170 4.3 16.6 1.0
ND2 A:ASN137 4.3 20.6 0.5
OE1 A:GLU171 4.5 39.3 0.3
O A:LEU168 4.6 15.7 1.0
NZ A:LYS140 4.6 28.6 0.5
N A:ALA169 4.7 15.7 1.0
O A:HOH6436 4.7 34.5 1.0
CG A:GLU171 4.7 27.9 0.3
OD1 A:ASP206 4.8 18.4 1.0
N A:LYS172 4.9 17.5 1.0
C A:GLU171 4.9 17.9 1.0
CB A:LEU170 5.0 20.3 1.0

Chlorine binding site 4 out of 4 in 1hx0

Go back to Chlorine Binding Sites List in 1hx0
Chlorine binding site 4 out of 4 in the Structure of Pig Pancreatic Alpha-Amylase Complexed with the "Truncate" Acarbose Molecule (Pseudotrisaccharide)


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 4 of Structure of Pig Pancreatic Alpha-Amylase Complexed with the "Truncate" Acarbose Molecule (Pseudotrisaccharide) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl502

b:25.9
occ:1.00
 O A:HOH6309 2.7 36.4 1.0
N A:GLY225 3.2 18.0 1.0
ND2 A:ASN216 3.3 23.4 1.0
O A:HOH6055 3.7 17.7 1.0
CB A:ASN216 3.8 15.4 1.0
CA A:ALA224 3.8 17.7 1.0
C A:ALA224 4.0 16.6 1.0
CG A:ASN216 4.0 17.9 1.0
CB A:ALA224 4.1 21.6 1.0
CA A:GLY225 4.1 18.5 1.0
CG2 A:THR219 4.1 19.4 1.0
O A:LEU217 4.8 16.0 1.0

Reference:

M.Qian, V.Nahoum, J.Bonicel, H.Bischoff, B.Henrissat, F.Payan. Enzyme-Catalyzed Condensation Reaction in A Mammalian Alpha-Amylase. High-Resolution Structural Analysis of An Enzyme-Inhibitor Complex Biochemistry V. 40 7700 2001.
ISSN: ISSN 0006-2960
PubMed: 11412124
DOI: 10.1021/BI0102050
Page generated: Sat Dec 12 08:37:23 2020

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