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Fluorine in PDB 1c5i: Hydrogen Bonding and Catalysis: An Unexpected Explanation For How A Single Amino Acid Substitution Can Change the pH Optimum of A Glycosidase

Enzymatic activity of Hydrogen Bonding and Catalysis: An Unexpected Explanation For How A Single Amino Acid Substitution Can Change the pH Optimum of A Glycosidase

All present enzymatic activity of Hydrogen Bonding and Catalysis: An Unexpected Explanation For How A Single Amino Acid Substitution Can Change the pH Optimum of A Glycosidase:
3.2.1.8;

Protein crystallography data

The structure of Hydrogen Bonding and Catalysis: An Unexpected Explanation For How A Single Amino Acid Substitution Can Change the pH Optimum of A Glycosidase, PDB code: 1c5i was solved by M.D.Joshi, G.Sidhu, I.Pot, G.D.Brayer, S.G.Withers, L.P.Mcintosh, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 10.00 / 1.80
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 43.830, 52.740, 78.800, 90.00, 90.00, 90.00
R / Rfree (%) 19.3 / n/a

Fluorine Binding Sites:

The binding sites of Fluorine atom in the Hydrogen Bonding and Catalysis: An Unexpected Explanation For How A Single Amino Acid Substitution Can Change the pH Optimum of A Glycosidase (pdb code 1c5i). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total only one binding site of Fluorine was determined in the Hydrogen Bonding and Catalysis: An Unexpected Explanation For How A Single Amino Acid Substitution Can Change the pH Optimum of A Glycosidase, PDB code: 1c5i:

Fluorine binding site 1 out of 1 in 1c5i

Go back to Fluorine Binding Sites List in 1c5i
Fluorine binding site 1 out of 1 in the Hydrogen Bonding and Catalysis: An Unexpected Explanation For How A Single Amino Acid Substitution Can Change the pH Optimum of A Glycosidase


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Hydrogen Bonding and Catalysis: An Unexpected Explanation For How A Single Amino Acid Substitution Can Change the pH Optimum of A Glycosidase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F502

b:18.5
occ:1.00
 F2 A:DFX502 0.0 18.5 1.0
C2 A:DFX502 1.4 20.4 1.0
C3 A:DFX502 2.4 22.4 1.0
C1 A:DFX502 2.4 19.5 1.0
OE1 A:GLU78 2.7 13.0 1.0
OE2 A:GLU78 2.9 12.2 1.0
O3 A:DFX502 2.9 20.4 1.0
NE A:ARG112 3.0 32.8 1.0
CD A:GLU78 3.1 12.1 1.0
CZ A:PHE125 3.2 4.9 1.0
NE2 A:GLN127 3.4 12.5 1.0
CE1 A:PHE125 3.4 7.1 1.0
O5 A:DFX502 3.7 19.6 1.0
NH2 A:ARG112 3.8 37.5 1.0
C4 A:DFX502 3.8 22.9 1.0
CG A:ARG112 3.8 19.6 1.0
CZ A:ARG112 3.8 35.1 1.0
CD A:ARG112 3.9 26.0 1.0
C5 A:DFX502 4.1 21.5 1.0
O A:HOH525 4.2 26.3 1.0
CD A:GLN127 4.3 13.1 1.0
CG A:GLU78 4.5 9.7 1.0
CE2 A:PHE125 4.5 5.3 1.0
O4 A:DFX502 4.6 24.1 1.0
O A:PRO116 4.7 10.4 1.0
OH A:TYR80 4.7 7.9 1.0
CB A:ARG112 4.7 17.1 1.0
CD1 A:PHE125 4.8 5.3 1.0
CG A:GLN127 4.8 9.8 1.0
CH2 A:TRP71 4.9 8.2 1.0
CB A:GLU78 4.9 7.2 1.0
CZ2 A:TRP71 4.9 7.3 1.0

Reference:

M.D.Joshi, G.Sidhu, I.Pot, G.D.Brayer, S.G.Withers, L.P.Mcintosh. Hydrogen Bonding and Catalysis: A Novel Explanation For How A Single Amino Acid Substitution Can Change the pH Optimum of A Glycosidase. J.Mol.Biol. V. 299 255 2000.
ISSN: ISSN 0022-2836
PubMed: 10860737
DOI: 10.1006/JMBI.2000.3722
Page generated: Mon Jul 14 10:29:05 2025

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