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Chlorine in PDB 1pif: Pig Alpha-Amylase

Enzymatic activity of Pig Alpha-Amylase

All present enzymatic activity of Pig Alpha-Amylase:
3.2.1.1;

Protein crystallography data

The structure of Pig Alpha-Amylase, PDB code: 1pif was solved by M.Machius, L.Vertesy, R.Huber, G.Wiegand, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 7.00 / 2.30
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 70.700, 114.900, 118.900, 90.00, 90.00, 90.00
R / Rfree (%) 17.1 / 20.8

Other elements in 1pif:

The structure of Pig Alpha-Amylase also contains other interesting chemical elements:

Calcium (Ca) 1 atom

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Pig Alpha-Amylase (pdb code 1pif). 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 Pig Alpha-Amylase, PDB code: 1pif:

Chlorine binding site 1 out of 1 in 1pif

Go back to Chlorine Binding Sites List in 1pif
Chlorine binding site 1 out of 1 in the Pig Alpha-Amylase


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Pig Alpha-Amylase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl600

b:30.9
occ:1.00
NH1 A:ARG195 3.0 22.4 1.0
NH2 A:ARG337 3.1 21.9 1.0
NH1 A:ARG337 3.3 25.4 1.0
ND2 A:ASN298 3.4 19.7 1.0
O A:HOH1093 3.5 25.1 1.0
CZ A:ARG337 3.7 23.7 1.0
CG2 A:THR254 3.8 21.5 1.0
CD A:ARG195 3.9 24.1 1.0
CG A:GLU233 4.0 26.2 1.0
CZ A:ARG195 4.1 25.2 1.0
CZ A:PHE256 4.2 20.9 1.0
CB A:GLU233 4.3 24.2 1.0
CG A:ASN298 4.4 21.4 1.0
NE A:ARG195 4.4 26.5 1.0
CB A:ASN298 4.4 19.9 1.0
CE1 A:PHE256 4.7 20.0 1.0
CD A:GLU233 4.7 32.2 1.0
CB A:THR254 4.8 23.6 1.0
CZ A:PHE295 4.8 19.4 1.0
OE2 A:GLU233 4.8 39.3 1.0
CG A:ARG195 4.8 24.5 1.0
O A:HOH1017 4.9 32.8 1.0
CE1 A:PHE295 4.9 18.9 1.0

Reference:

M.Machius, L.Vertesy, R.Huber, G.Wiegand. Carbohydrate and Protein-Based Inhibitors of Porcine Pancreatic Alpha-Amylase: Structure Analysis and Comparison of Their Binding Characteristics. J.Mol.Biol. V. 260 409 1996.
ISSN: ISSN 0022-2836
PubMed: 8757803
DOI: 10.1006/JMBI.1996.0410
Page generated: Sat Jul 20 01:13:19 2024

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