Atomistry » Chlorine » PDB 1hba-1i3k » 1hx0
Atomistry »
  Chlorine »
    PDB 1hba-1i3k »
      1hx0 »

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: Fri Jul 19 22:35:29 2024

Last articles

Zn in 9J0N
Zn in 9J0O
Zn in 9J0P
Zn in 9FJX
Zn in 9EKB
Zn in 9C0F
Zn in 9CAH
Zn in 9CH0
Zn in 9CH3
Zn in 9CH1
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy