Fluorine in PDB 8pbk: Mutant R1722W of the Dihydroorotase Domain of Human Cad Protein Bound to the Inhibitor Fluoorotate

Enzymatic activity of Mutant R1722W of the Dihydroorotase Domain of Human Cad Protein Bound to the Inhibitor Fluoorotate

All present enzymatic activity of Mutant R1722W of the Dihydroorotase Domain of Human Cad Protein Bound to the Inhibitor Fluoorotate:
2.1.3.2; 3.5.2.3; 6.3.5.5;

Protein crystallography data

The structure of Mutant R1722W of the Dihydroorotase Domain of Human Cad Protein Bound to the Inhibitor Fluoorotate, PDB code: 8pbk was solved by F.Del Cano-Ochoa, S.Ramon-Maiques, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 44.36 / 1.69
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 82.158, 158.123, 61.939, 90, 90, 90
R / Rfree (%) 13.9 / 18.3

Other elements in 8pbk:

The structure of Mutant R1722W of the Dihydroorotase Domain of Human Cad Protein Bound to the Inhibitor Fluoorotate also contains other interesting chemical elements:

Zinc (Zn) 2 atoms

Fluorine Binding Sites:

The binding sites of Fluorine atom in the Mutant R1722W of the Dihydroorotase Domain of Human Cad Protein Bound to the Inhibitor Fluoorotate (pdb code 8pbk). 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 Mutant R1722W of the Dihydroorotase Domain of Human Cad Protein Bound to the Inhibitor Fluoorotate, PDB code: 8pbk:

Fluorine binding site 1 out of 1 in 8pbk

Go back to Fluorine Binding Sites List in 8pbk
Fluorine binding site 1 out of 1 in the Mutant R1722W of the Dihydroorotase Domain of Human Cad Protein Bound to the Inhibitor Fluoorotate


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Mutant R1722W of the Dihydroorotase Domain of Human Cad Protein Bound to the Inhibitor Fluoorotate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F1901

b:18.7
occ:1.00
 F5 A:FOT1901 0.0 18.7 1.0
C5 A:FOT1901 1.3 16.1 1.0
C4 A:FOT1901 2.4 16.4 1.0
C6 A:FOT1901 2.4 15.5 1.0
HD21 A:ASN1505 2.6 18.9 1.0
O6 A:FOT1901 2.8 16.6 1.0
O41 A:FOT1901 2.8 15.9 1.0
HE1 A:TYR1558 2.9 16.8 1.0
HD22 A:ASN1505 2.9 18.9 1.0
O A:HOH2190 3.0 32.6 1.0
C41 A:FOT1901 3.0 16.6 1.0
ND2 A:ASN1505 3.0 15.8 1.0
HE1 A:HIS1473 3.1 16.3 1.0
O A:HOH2049 3.4 25.9 1.0
HH A:TYR1558 3.5 18.8 1.0
CE1 A:HIS1473 3.5 13.6 1.0
N1 A:FOT1901 3.6 15.9 1.0
N3 A:FOT1901 3.6 16.6 1.0
CE1 A:TYR1558 3.7 14.0 1.0
O A:HOH2047 3.7 14.2 1.0
OQ1 A:KCX1556 3.8 12.9 1.0
NE2 A:HIS1473 3.8 14.5 1.0
ZN A:ZN1907 4.0 15.1 1.0
O1 A:FMT1903 4.1 46.4 1.0
OH A:TYR1558 4.2 15.7 1.0
C2 A:FOT1901 4.2 16.0 1.0
CG A:ASN1505 4.2 15.9 1.0
O42 A:FOT1901 4.2 16.8 1.0
HN3 A:FOT1901 4.3 20.0 1.0
HN1 A:FOT1901 4.3 19.1 1.0
CZ A:TYR1558 4.3 14.6 1.0
ZN A:ZN1906 4.3 15.7 1.0
C A:FMT1903 4.3 45.9 1.0
ND1 A:HIS1473 4.4 13.1 1.0
CX A:KCX1556 4.5 13.0 1.0
HD1 A:TYR1558 4.5 16.2 1.0
CD1 A:TYR1558 4.5 13.5 1.0
O2 A:FMT1903 4.6 45.2 1.0
HO2 A:FMT1903 4.7 54.2 1.0
OQ2 A:KCX1556 4.7 14.6 1.0
HD1 A:HIS1473 4.7 15.8 1.0
H A:FMT1903 4.7 55.1 1.0
HH12 A:ARG1475 4.8 18.9 1.0
OD1 A:ASN1505 4.8 16.2 1.0
CD2 A:HIS1473 4.9 15.3 1.0

Reference:

F.Del Cano-Ochoa, B.G.Ng, A.Rubio-Del-Campo, S.Mahajan, M.P.Wilson, M.Vilar, D.Rymen, P.Sanchez-Pintos, J.Kenny, M.Ley Martos, T.Campos, S.B.Wortmann, H.H.Freeze, S.Ramon-Maiques. Beyond Genetics: Deciphering the Impact of Missense Variants in Cad Deficiency. J Inherit Metab Dis 2023.
ISSN: ISSN 1573-2665
PubMed: 37540500
DOI: 10.1002/JIMD.12667
Page generated: Fri Aug 2 21:57:19 2024

Last articles

Zn in 9JYW
Zn in 9IR4
Zn in 9IR3
Zn in 9GMX
Zn in 9GMW
Zn in 9JEJ
Zn in 9ERF
Zn in 9ERE
Zn in 9EGV
Zn in 9EGW
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy