Chlorine in PDB 5td4: Starch Binding Sites on the Human Pancreatic Alpha Amylase D300N Variant Complexed with An Octaose Substrate.

Enzymatic activity of Starch Binding Sites on the Human Pancreatic Alpha Amylase D300N Variant Complexed with An Octaose Substrate.

All present enzymatic activity of Starch Binding Sites on the Human Pancreatic Alpha Amylase D300N Variant Complexed with An Octaose Substrate.:
3.2.1.1;

Protein crystallography data

The structure of Starch Binding Sites on the Human Pancreatic Alpha Amylase D300N Variant Complexed with An Octaose Substrate., PDB code: 5td4 was solved by S.Caner, G.D.Brayer, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 38.48 / 2.30
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 52.210, 73.640, 135.380, 90.00, 90.00, 90.00
R / Rfree (%) 15.1 / 18.9

Other elements in 5td4:

The structure of Starch Binding Sites on the Human Pancreatic Alpha Amylase D300N Variant Complexed with An Octaose Substrate. also contains other interesting chemical elements:

Calcium (Ca) 1 atom

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Starch Binding Sites on the Human Pancreatic Alpha Amylase D300N Variant Complexed with An Octaose Substrate. (pdb code 5td4). 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 Starch Binding Sites on the Human Pancreatic Alpha Amylase D300N Variant Complexed with An Octaose Substrate., PDB code: 5td4:

Chlorine binding site 1 out of 1 in 5td4

Go back to Chlorine Binding Sites List in 5td4
Chlorine binding site 1 out of 1 in the Starch Binding Sites on the Human Pancreatic Alpha Amylase D300N Variant Complexed with An Octaose Substrate.


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Starch Binding Sites on the Human Pancreatic Alpha Amylase D300N Variant Complexed with An Octaose Substrate. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl501

b:19.9
occ:1.00
 NE A:ARG195 3.0 15.1 1.0
O A:HOH738 3.0 17.3 1.0
NH2 A:ARG337 3.3 12.8 1.0
NH2 A:ARG195 3.3 18.8 1.0
NH1 A:ARG337 3.3 14.8 1.0
ND2 A:ASN298 3.5 17.2 1.0
CZ A:ARG195 3.6 18.9 1.0
CZ A:ARG337 3.7 16.2 1.0
CG2 A:THR254 3.8 15.6 1.0
CD A:ARG195 4.1 18.4 1.0
CG A:GLU233 4.1 17.9 1.0
CZ A:PHE256 4.1 18.4 1.0
CB A:ASN298 4.5 16.9 1.0
CG A:ASN298 4.5 17.9 1.0
CB A:GLU233 4.5 17.1 1.0
O A:HOH648 4.6 26.3 1.0
CB A:THR254 4.7 15.1 1.0
OE2 A:GLU233 4.7 21.1 1.0
CE1 A:PHE256 4.7 18.0 1.0
CZ A:PHE295 4.8 16.6 1.0
CD A:GLU233 4.8 16.0 1.0
CG A:ARG195 4.9 16.5 1.0
NH1 A:ARG195 4.9 14.1 1.0
CE2 A:PHE256 5.0 22.1 1.0

Reference:

X.Zhang, S.Caner, E.Kwan, C.Li, G.D.Brayer, S.G.Withers. Evaluation of the Significance of Starch Surface Binding Sites on Human Pancreatic Alpha-Amylase. Biochemistry V. 55 6000 2016.
ISSN: ISSN 0006-2960
PubMed: 27756128
DOI: 10.1021/ACS.BIOCHEM.6B00992
Page generated: Sat Dec 12 12:28:10 2020

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