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Chlorine in PDB 1bsi: Human Pancreatic Alpha-Amylase From Pichia Pastoris, Glycosylated Protein

Enzymatic activity of Human Pancreatic Alpha-Amylase From Pichia Pastoris, Glycosylated Protein

All present enzymatic activity of Human Pancreatic Alpha-Amylase From Pichia Pastoris, Glycosylated Protein:
3.2.1.1;

Protein crystallography data

The structure of Human Pancreatic Alpha-Amylase From Pichia Pastoris, Glycosylated Protein, PDB code: 1bsi was solved by E.H.Rydberg, G.Sidhu, H.C.Vo, J.Hewitt, H.C.F.Cote, Y.Wang, S.Numao, R.T.A.Macgillivray, C.M.Overall, G.D.Brayer, S.G.Withers, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 10.00 / 2.00
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 52.910, 68.900, 131.770, 90.00, 90.00, 90.00
R / Rfree (%) 18.4 / n/a

Other elements in 1bsi:

The structure of Human Pancreatic Alpha-Amylase From Pichia Pastoris, Glycosylated Protein also contains other interesting chemical elements:

Calcium (Ca) 1 atom

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Human Pancreatic Alpha-Amylase From Pichia Pastoris, Glycosylated Protein (pdb code 1bsi). 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 Human Pancreatic Alpha-Amylase From Pichia Pastoris, Glycosylated Protein, PDB code: 1bsi:

Chlorine binding site 1 out of 1 in 1bsi

Go back to Chlorine Binding Sites List in 1bsi
Chlorine binding site 1 out of 1 in the Human Pancreatic Alpha-Amylase From Pichia Pastoris, Glycosylated Protein


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Human Pancreatic Alpha-Amylase From Pichia Pastoris, Glycosylated Protein within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl499

b:15.4
occ:1.00
 NH2 A:ARG337 3.1 7.3 1.0
NE A:ARG195 3.2 9.1 1.0
NH2 A:ARG195 3.3 9.2 1.0
ND2 A:ASN298 3.4 7.3 1.0
O A:HOH507 3.4 10.4 1.0
NH1 A:ARG337 3.4 8.2 1.0
CZ A:ARG337 3.7 9.5 1.0
CZ A:ARG195 3.7 8.2 1.0
CG2 A:THR254 3.8 8.0 1.0
CZ A:PHE256 4.1 6.9 1.0
CG A:GLU233 4.2 10.2 1.0
CD A:ARG195 4.4 8.0 1.0
CG A:ASN298 4.4 8.9 1.0
CB A:ASN298 4.4 7.1 1.0
CB A:GLU233 4.6 8.1 1.0
CZ A:PHE295 4.6 11.9 1.0
CE1 A:PHE256 4.7 6.6 1.0
CB A:THR254 4.7 10.1 1.0
CE1 A:PHE295 4.8 11.0 1.0
O A:HOH539 4.8 13.4 1.0
CG A:ARG195 4.9 7.1 1.0
CD A:GLU233 4.9 11.3 1.0
CE2 A:PHE256 5.0 7.3 1.0
OE2 A:GLU233 5.0 12.4 1.0

Reference:

E.H.Rydberg, G.Sidhu, H.C.Vo, J.Hewitt, H.C.Cote, Y.Wang, S.Numao, R.T.Macgillivray, C.M.Overall, G.D.Brayer, S.G.Withers. Cloning, Mutagenesis, and Structural Analysis of Human Pancreatic Alpha-Amylase Expressed in Pichia Pastoris. Protein Sci. V. 8 635 1999.
ISSN: ISSN 0961-8368
PubMed: 10091666
Page generated: Fri Jul 19 21:04:46 2024

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