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Chlorine in PDB 1q4n: Structural Studies of PHE256TRP of Human Salivary Alpha-Amylase: Implications For the Role of A Conserved Water Molecule and Its Associated Chain in Enzyme Activity

Enzymatic activity of Structural Studies of PHE256TRP of Human Salivary Alpha-Amylase: Implications For the Role of A Conserved Water Molecule and Its Associated Chain in Enzyme Activity

All present enzymatic activity of Structural Studies of PHE256TRP of Human Salivary Alpha-Amylase: Implications For the Role of A Conserved Water Molecule and Its Associated Chain in Enzyme Activity:
3.2.1.1;

Protein crystallography data

The structure of Structural Studies of PHE256TRP of Human Salivary Alpha-Amylase: Implications For the Role of A Conserved Water Molecule and Its Associated Chain in Enzyme Activity, PDB code: 1q4n was solved by N.Ramasubbu, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 41.17 / 2.07
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 51.900, 74.200, 134.820, 90.00, 90.00, 90.00
R / Rfree (%) 15.6 / 20.6

Other elements in 1q4n:

The structure of Structural Studies of PHE256TRP of Human Salivary Alpha-Amylase: Implications For the Role of A Conserved Water Molecule and Its Associated Chain in Enzyme Activity also contains other interesting chemical elements:

Calcium (Ca) 1 atom

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Structural Studies of PHE256TRP of Human Salivary Alpha-Amylase: Implications For the Role of A Conserved Water Molecule and Its Associated Chain in Enzyme Activity (pdb code 1q4n). 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 Structural Studies of PHE256TRP of Human Salivary Alpha-Amylase: Implications For the Role of A Conserved Water Molecule and Its Associated Chain in Enzyme Activity, PDB code: 1q4n:

Chlorine binding site 1 out of 1 in 1q4n

Go back to Chlorine Binding Sites List in 1q4n
Chlorine binding site 1 out of 1 in the Structural Studies of PHE256TRP of Human Salivary Alpha-Amylase: Implications For the Role of A Conserved Water Molecule and Its Associated Chain in Enzyme Activity


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Structural Studies of PHE256TRP of Human Salivary Alpha-Amylase: Implications For the Role of A Conserved Water Molecule and Its Associated Chain in Enzyme Activity within 5.0Å range:
probe atom residue distance (Å) B Occ
X:Cl951

b:23.4
occ:1.00
 O X:HOH524 3.1 19.9 1.0
NH2 X:ARG337 3.2 22.8 1.0
NE X:ARG195 3.2 22.4 1.0
NH2 X:ARG195 3.3 25.3 1.0
ND2 X:ASN298 3.3 25.1 1.0
NH1 X:ARG337 3.4 22.6 1.0
CZ X:ARG195 3.7 25.3 1.0
CZ X:ARG337 3.7 20.7 1.0
CG2 X:THR254 3.9 22.6 1.0
CZ2 X:TRP256 4.1 38.5 1.0
CG X:GLU233 4.2 25.1 1.0
CD X:ARG195 4.4 24.5 1.0
CG X:ASN298 4.4 23.5 1.0
CB X:GLU233 4.4 24.0 1.0
CB X:ASN298 4.6 21.0 1.0
CG X:ARG195 4.7 23.3 1.0
CE2 X:TRP256 4.8 35.2 1.0
CB X:THR254 4.8 21.9 1.0
CZ X:PHE295 4.8 23.1 1.0
OE2 X:GLU233 4.9 29.2 1.0
CD X:GLU233 4.9 26.6 1.0
NE1 X:TRP256 4.9 28.5 1.0
CH2 X:TRP256 4.9 42.1 1.0
CE1 X:HIS299 5.0 19.9 1.0

Reference:

N.Ramasubbu, K.Sundar, C.Ragunath, M.M.Rafi. Structural Studies of A PHE256TRP Mutant of Human Salivary Alpha-Amylase: Implications For the Role of A Conserved Water Molecule in Enzyme Activity Arch.Biochem.Biophys. V. 421 115 2004.
ISSN: ISSN 0003-9861
PubMed: 14678792
DOI: 10.1016/J.ABB.2003.10.007
Page generated: Sat Dec 12 08:46:26 2020

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