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Chlorine in PDB 1mfu: Probing the Role of A Mobile Loop in Human Salivary Amylase: Structural Studies on the Loop-Deleted Mutant

Enzymatic activity of Probing the Role of A Mobile Loop in Human Salivary Amylase: Structural Studies on the Loop-Deleted Mutant

All present enzymatic activity of Probing the Role of A Mobile Loop in Human Salivary Amylase: Structural Studies on the Loop-Deleted Mutant:
3.2.1.1;

Protein crystallography data

The structure of Probing the Role of A Mobile Loop in Human Salivary Amylase: Structural Studies on the Loop-Deleted Mutant, PDB code: 1mfu was solved by N.Ramasubbu, C.Ragunath, P.J.Mishra, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 26.54 / 2.00
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 52.074, 73.815, 135.787, 90.00, 90.00, 90.00
R / Rfree (%) 16 / 20.1

Other elements in 1mfu:

The structure of Probing the Role of A Mobile Loop in Human Salivary Amylase: Structural Studies on the Loop-Deleted Mutant also contains other interesting chemical elements:

Calcium (Ca) 1 atom

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Probing the Role of A Mobile Loop in Human Salivary Amylase: Structural Studies on the Loop-Deleted Mutant (pdb code 1mfu). 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 Probing the Role of A Mobile Loop in Human Salivary Amylase: Structural Studies on the Loop-Deleted Mutant, PDB code: 1mfu:

Chlorine binding site 1 out of 1 in 1mfu

Go back to Chlorine Binding Sites List in 1mfu
Chlorine binding site 1 out of 1 in the Probing the Role of A Mobile Loop in Human Salivary Amylase: Structural Studies on the Loop-Deleted Mutant


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Probing the Role of A Mobile Loop in Human Salivary Amylase: Structural Studies on the Loop-Deleted Mutant within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl493

b:19.5
occ:1.00
 NH2 A:ARG332 3.1 16.6 1.0
NE A:ARG195 3.2 18.4 1.0
O A:HOH701 3.3 14.9 1.0
NH1 A:ARG332 3.3 14.5 1.0
NH2 A:ARG195 3.3 17.7 1.0
ND2 A:ASN298 3.5 17.6 1.0
CZ A:ARG332 3.6 17.2 1.0
CZ A:ARG195 3.7 17.6 1.0
CG2 A:THR254 3.9 16.9 1.0
CG A:GLU233 4.0 19.4 1.0
CZ A:PHE256 4.0 19.8 1.0
CB A:GLU233 4.3 18.9 1.0
CD A:ARG195 4.4 17.9 1.0
CB A:ASN298 4.4 16.1 1.0
CG A:ASN298 4.5 16.5 1.0
CG A:ARG195 4.6 18.8 1.0
CE1 A:PHE256 4.6 17.1 1.0
O A:HOH732 4.8 18.8 1.0
CZ A:PHE295 4.8 16.8 1.0
CD A:GLU233 4.9 19.6 1.0
CB A:THR254 4.9 17.9 1.0
NE A:ARG332 5.0 14.1 1.0
NH1 A:ARG195 5.0 17.8 1.0

Reference:

N.Ramasubbu, C.Ragunath, P.J.Mishra. Probing the Role of A Mobile Loop in Substrate Binding and Enzyme Activity of Human Salivary Amylase. J.Mol.Biol. V. 325 1061 2003.
ISSN: ISSN 0022-2836
PubMed: 12527308
DOI: 10.1016/S0022-2836(02)01326-8
Page generated: Sat Jul 20 00:08:40 2024

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