Chlorine in PDB 1kxt: Camelid Vhh Domains in Complex with Porcine Pancreatic Alpha-Amylase

All present enzymatic activity of Camelid Vhh Domains in Complex with Porcine Pancreatic Alpha-Amylase:
3.2.1.1;

The structure of Camelid Vhh Domains in Complex with Porcine Pancreatic Alpha-Amylase, PDB code: 1kxt was solved by A.Desmyter, S.Spinelli, F.Payan, M.Lauwereys, L.Wyns, S.Muyldermans, C.Cambillau, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.95 / 2.00
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	52.780, 286.850, 65.980, 90.00, 93.73, 90.00
R / Rfree (%)	20.3 / 23.6

The structure of Camelid Vhh Domains in Complex with Porcine Pancreatic Alpha-Amylase also contains other interesting chemical elements:

Calcium

(Ca)

3 atoms

The binding sites of Chlorine atom in the Camelid Vhh Domains in Complex with Porcine Pancreatic Alpha-Amylase (pdb code 1kxt). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 3 binding sites of Chlorine where determined in the Camelid Vhh Domains in Complex with Porcine Pancreatic Alpha-Amylase, PDB code: 1kxt:
Jump to Chlorine binding site number: 1; 2; 3;

Chlorine binding site 1 out of 3 in the Camelid Vhh Domains in Complex with Porcine Pancreatic Alpha-Amylase


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Camelid Vhh Domains in Complex with Porcine Pancreatic Alpha-Amylase within 5.0Å range: probe atom residue distance (Å) B Occ A:Cl4002 b:22.5 occ:1.00 NH2 A:ARG195 2.7 14.7 1.0 O A:HOH4159 3.2 19.6 1.0 NH2 A:ARG337 3.3 8.9 1.0 NH1 A:ARG337 3.4 7.0 1.0 CG A:GLU233 3.7 12.8 1.0 CZ A:ARG337 3.8 6.9 1.0 CD A:ARG195 3.9 13.8 1.0 CZ A:ARG195 3.9 15.5 1.0 CG2 A:THR254 4.0 5.8 1.0 ND2 A:ASN298 4.1 7.9 1.0 CZ A:PHE256 4.1 11.6 1.0 NE A:ARG195 4.4 15.6 1.0 CB A:GLU233 4.4 11.9 1.0 CB A:ASN298 4.6 8.5 1.0 CD A:GLU233 4.7 13.3 1.0 CB A:THR254 4.7 7.8 1.0 CE2 A:PHE256 4.8 11.0 1.0 CG A:ARG195 4.8 12.2 1.0 CG A:ASN298 4.8 8.1 1.0 OE1 A:GLU233 4.9 14.0 1.0 CZ A:PHE295 4.9 4.0 1.0 OG1 A:THR254 5.0 8.9 1.0

Chlorine binding site 2 out of 3 in the Camelid Vhh Domains in Complex with Porcine Pancreatic Alpha-Amylase


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Camelid Vhh Domains in Complex with Porcine Pancreatic Alpha-Amylase within 5.0Å range: probe atom residue distance (Å) B Occ C:Cl4004 b:27.3 occ:1.00 NH1 C:ARG337 2.9 17.1 1.0 O C:HOH4293 2.9 32.5 1.0 NH2 C:ARG337 3.2 16.8 1.0 NH2 C:ARG195 3.4 22.4 1.0 CZ C:ARG337 3.5 17.2 1.0 ND2 C:ASN298 3.6 12.2 1.0 CG C:GLU233 3.7 18.5 1.0 CZ C:PHE256 3.8 13.0 1.0 CG2 C:THR254 3.9 13.1 1.0 CD C:ARG195 4.0 18.6 1.0 CZ C:ARG195 4.3 21.6 1.0 CB C:ASN298 4.4 13.3 1.0 CE2 C:PHE256 4.4 12.7 1.0 CB C:GLU233 4.4 17.1 1.0 CG C:ASN298 4.5 13.9 1.0 CZ C:PHE295 4.5 10.0 1.0 NE C:ARG195 4.5 20.6 1.0 CD C:GLU233 4.6 18.9 1.0 CB C:THR254 4.7 13.8 1.0 OE1 C:GLU233 4.7 19.6 1.0 CE1 C:PHE256 4.7 12.3 1.0 NE C:ARG337 4.8 17.6 1.0 CE2 C:PHE295 4.9 9.4 1.0 O C:HOH4056 4.9 26.2 1.0 O C:HOH4006 4.9 14.4 1.0 CG C:ARG195 4.9 17.5 1.0 CE1 C:PHE295 4.9 10.0 1.0

Chlorine binding site 3 out of 3 in the Camelid Vhh Domains in Complex with Porcine Pancreatic Alpha-Amylase


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Camelid Vhh Domains in Complex with Porcine Pancreatic Alpha-Amylase within 5.0Å range: probe atom residue distance (Å) B Occ E:Cl4006 b:21.8 occ:1.00 NH2 E:ARG195 2.9 14.1 1.0 NH1 E:ARG337 3.1 7.4 1.0 O E:HOH4011 3.1 8.6 1.0 NH2 E:ARG337 3.2 7.3 1.0 CZ E:ARG337 3.6 7.2 1.0 CG E:GLU233 3.6 13.1 1.0 CD E:ARG195 3.7 12.2 1.0 ND2 E:ASN298 3.9 11.7 1.0 CZ E:ARG195 4.0 14.9 1.0 CG2 E:THR254 4.2 9.1 1.0 CZ E:PHE256 4.3 4.4 1.0 NE E:ARG195 4.3 15.2 1.0 CB E:GLU233 4.4 13.1 1.0 CD E:GLU233 4.6 13.8 1.0 CG E:ARG195 4.6 11.7 1.0 CB E:ASN298 4.7 10.7 1.0 CG E:ASN298 4.7 10.7 1.0 OE1 E:GLU233 4.8 14.0 1.0 NE E:ARG337 4.9 8.3 1.0 CB E:THR254 4.9 9.0 1.0 CZ E:PHE295 5.0 6.8 1.0 CE2 E:PHE256 5.0 4.1 1.0

A.Desmyter, S.Spinelli, F.Payan, M.Lauwereys, L.Wyns, S.Muyldermans, C.Cambillau. Three Camelid Vhh Domains in Complex with Porcine Pancreatic Alpha-Amylase. Inhibition and Versatility of Binding Topology. J.Biol.Chem. V. 277 23645 2002.
ISSN: ISSN 0021-9258
PubMed: 11960990
DOI: 10.1074/JBC.M202327200