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Chlorine in PDB 6z8l: Alpha-Amylase in Complex with Probe Fragments

Enzymatic activity of Alpha-Amylase in Complex with Probe Fragments

All present enzymatic activity of Alpha-Amylase in Complex with Probe Fragments:
3.2.1.1;

Protein crystallography data

The structure of Alpha-Amylase in Complex with Probe Fragments, PDB code: 6z8l was solved by S.Adam, J.Koehnke, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 48.43 / 1.40
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 51.873, 73.729, 135.207, 90.00, 90.00, 90.00
R / Rfree (%) 14.2 / 15.4

Other elements in 6z8l:

The structure of Alpha-Amylase in Complex with Probe Fragments also contains other interesting chemical elements:

Calcium (Ca) 1 atom

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Alpha-Amylase in Complex with Probe Fragments (pdb code 6z8l). 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 Alpha-Amylase in Complex with Probe Fragments, PDB code: 6z8l:

Chlorine binding site 1 out of 1 in 6z8l

Go back to Chlorine Binding Sites List in 6z8l
Chlorine binding site 1 out of 1 in the Alpha-Amylase in Complex with Probe Fragments


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Alpha-Amylase in Complex with Probe Fragments within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl907

b:16.1
occ:1.00
HH22 A:ARG337 2.4 21.6 1.0
HE A:ARG195 2.5 21.6 1.0
HD22 A:ASN298 2.5 21.1 1.0
HH21 A:ARG195 2.5 20.4 1.0
HH12 A:ARG337 2.5 19.5 1.0
HG21 A:THR254 3.0 17.8 1.0
HG3 A:GLU233 3.1 20.9 1.0
NH2 A:ARG337 3.2 18.0 1.0
NE A:ARG195 3.3 17.9 1.0
O A:HOH1281 3.3 17.6 1.0
NH2 A:ARG195 3.3 17.0 1.0
NH1 A:ARG337 3.3 16.2 1.0
ND2 A:ASN298 3.3 17.6 1.0
HZ A:PHE256 3.4 20.1 1.0
HD21 A:ASN298 3.7 21.1 1.0
CZ A:ARG337 3.7 16.4 1.0
HB2 A:GLU233 3.7 20.1 1.0
CZ A:ARG195 3.7 16.5 1.0
HG22 A:THR254 3.8 17.8 1.0
CG2 A:THR254 3.8 14.8 1.0
HH21 A:ARG337 3.9 21.6 1.0
HB2 A:ASN298 3.9 17.8 1.0
HH22 A:ARG195 4.0 20.4 1.0
HH11 A:ARG337 4.0 19.5 1.0
CG A:GLU233 4.0 17.4 1.0
HG3 A:ARG195 4.1 23.8 1.0
CZ A:PHE256 4.1 16.8 1.0
HG23 A:THR254 4.3 17.8 1.0
HB3 A:ASN298 4.3 17.8 1.0
CB A:GLU233 4.3 16.7 1.0
CG A:ASN298 4.4 16.4 1.0
HE1 A:PHE256 4.4 18.5 1.0
CB A:ASN298 4.4 14.8 1.0
HE1 A:HIS299 4.4 23.4 1.0
CD A:ARG195 4.4 19.9 1.0
CG A:ARG195 4.6 19.9 1.0
HA A:GLU233 4.6 18.9 1.0
HG2 A:GLU233 4.6 20.9 1.0
HE22 A:GLN41 4.6 18.6 1.0
HG2 A:ARG195 4.6 23.8 1.0
CE1 A:PHE256 4.7 15.4 1.0
HD2 A:ARG195 4.7 24.0 1.0
HZ A:PHE295 4.7 17.2 1.0
HB A:THR254 4.7 18.2 1.0
CD A:GLU233 4.8 19.1 1.0
CZ A:PHE295 4.8 14.3 1.0
CB A:THR254 4.9 15.1 1.0
OE2 A:GLU233 4.9 19.7 1.0
O A:HOH1082 4.9 20.0 1.0

Reference:

A.Axer, R.P.Jumde, S.Adam, A.Faust, M.Schafers, M.Fobker, J.Koehnke, A.K.H.Hirsch, R.Gilmour. Enhancing Glycan Stability Via Site-Selective Fluorination: Modulating Substrate Orientation By Molecular Design Chem Sci 2020.
ISSN: ESSN 2041-6539
DOI: 10.1039/D0SC04297H
Page generated: Mon Jul 29 17:58:20 2024

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