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Chlorine in PDB 1mfv: Probing the Role of A Mobile Loop in Human Slaivary Amylase: Structural Studies on the Loop-Deleted Enzyme

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

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

Protein crystallography data

The structure of Probing the Role of A Mobile Loop in Human Slaivary Amylase: Structural Studies on the Loop-Deleted Enzyme, PDB code: 1mfv 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) 20.00 / 2.00
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 51.681, 73.197, 134.448, 90.00, 90.00, 90.00
R / Rfree (%) 16.7 / 19.5

Other elements in 1mfv:

The structure of Probing the Role of A Mobile Loop in Human Slaivary Amylase: Structural Studies on the Loop-Deleted Enzyme 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 Slaivary Amylase: Structural Studies on the Loop-Deleted Enzyme (pdb code 1mfv). 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 Slaivary Amylase: Structural Studies on the Loop-Deleted Enzyme, PDB code: 1mfv:

Chlorine binding site 1 out of 1 in 1mfv

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


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 Slaivary Amylase: Structural Studies on the Loop-Deleted Enzyme within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl498

b:24.1
occ:1.00
 NH2 A:ARG337 3.1 18.1 1.0
NE A:ARG195 3.1 23.0 1.0
O A:HOH651 3.2 25.3 1.0
NH2 A:ARG195 3.3 21.3 1.0
NH1 A:ARG337 3.3 16.3 1.0
ND2 A:ASN298 3.4 20.1 1.0
CZ A:ARG195 3.6 24.1 1.0
CZ A:ARG337 3.6 21.0 1.0
CG2 A:THR254 3.9 19.8 1.0
CG A:GLU233 4.0 24.1 1.0
CZ A:PHE256 4.1 23.2 1.0
CD A:ARG195 4.2 24.2 1.0
CB A:GLU233 4.3 23.2 1.0
CG A:ASN298 4.4 19.8 1.0
CB A:ASN298 4.4 20.5 1.0
CG A:ARG195 4.5 24.3 1.0
CE1 A:PHE256 4.7 22.9 1.0
O A:HOH641 4.9 24.1 1.0
CE1 A:HIS299 4.9 23.6 1.0
CB A:THR254 4.9 22.0 1.0
CD A:GLU233 4.9 25.3 1.0
NH1 A:ARG195 5.0 23.6 1.0
NE A:ARG337 5.0 19.7 1.0
CZ A:PHE295 5.0 18.3 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 Dec 12 08:42:42 2020

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