Fluorine in PDB 4c6l: Crystal Structure of the Dihydroorotase Domain of Human Cad Bound to the Inhibitor Fluoroorotate at pH 6.0

Enzymatic activity of Crystal Structure of the Dihydroorotase Domain of Human Cad Bound to the Inhibitor Fluoroorotate at pH 6.0

All present enzymatic activity of Crystal Structure of the Dihydroorotase Domain of Human Cad Bound to the Inhibitor Fluoroorotate at pH 6.0:
3.5.2.3;

Protein crystallography data

The structure of Crystal Structure of the Dihydroorotase Domain of Human Cad Bound to the Inhibitor Fluoroorotate at pH 6.0, PDB code: 4c6l was solved by S.Ramon-Maiques, N.Lallous, A.Grande-Garcia, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

*Resolution Low / High (Å)*	44.381 / 1.55
*Space group*	C 2 2 2₁
*Cell size a, b, c (Å), α, β, γ (°)*	81.960, 158.370, 61.260, 90.00, 90.00, 90.00
*R / R_free (%)*	12.37 / 15.87

Other elements in 4c6l:

The structure of Crystal Structure of the Dihydroorotase Domain of Human Cad Bound to the Inhibitor Fluoroorotate at pH 6.0 also contains other interesting chemical elements:

Zinc

(Zn)

2 atoms

Fluorine Binding Sites:

The binding sites of Fluorine atom in the Crystal Structure of the Dihydroorotase Domain of Human Cad Bound to the Inhibitor Fluoroorotate at pH 6.0 (pdb code 4c6l). 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 Crystal Structure of the Dihydroorotase Domain of Human Cad Bound to the Inhibitor Fluoroorotate at pH 6.0, PDB code: 4c6l:

Fluorine binding site 1 out of 1 in 4c6l

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Fluorine Binding Sites List in 4c6l

Fluorine binding site 1 out of 1 in the Crystal Structure of the Dihydroorotase Domain of Human Cad Bound to the Inhibitor Fluoroorotate at pH 6.0

Mono view

Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Crystal Structure of the Dihydroorotase Domain of Human Cad Bound to the Inhibitor Fluoroorotate at pH 6.0 within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
A:F2826 b:13.6 occ:1.00	F5	A:FOT2826	0.0	13.6	1.0
	C5	A:FOT2826	1.3	11.3	1.0
	C4	A:FOT2826	2.4	10.7	1.0
	C6	A:FOT2826	2.4	11.4	1.0
	HD22	A:ASN1505	2.7	14.7	1.0
	O6	A:FOT2826	2.8	12.7	1.0
	O42	A:FOT2826	2.8	13.6	1.0
	HE1	A:TYR1558	2.9	13.7	1.0
	O	A:HOH2143	2.9	27.8	1.0
	HD21	A:ASN1505	3.0	14.7	1.0
	C41	A:FOT2826	3.0	12.0	1.0
	HE1	A:HIS1473	3.0	12.1	1.0
	ND2	A:ASN1505	3.1	12.2	1.0
	O	A:HOH2093	3.4	25.3	1.0
	CE1	A:HIS1473	3.4	10.0	1.0
	CE1	A:TYR1558	3.6	11.4	1.0
	N1	A:FOT2826	3.7	11.4	1.0
	N3	A:FOT2826	3.7	11.2	1.0
	OQ2	A:KCX1556	3.7	11.9	1.0
	O	A:HOH2071	3.8	12.1	1.0
	NE2	A:HIS1473	3.9	10.0	1.0
	ZN	A:ZN2824	4.1	10.4	0.9
	OH	A:TYR1558	4.1	12.8	1.0
	HH	A:TYR1558	4.2	15.4	1.0
	CG	A:ASN1505	4.2	11.5	1.0
	O41	A:FOT2826	4.2	13.8	1.0
	C2	A:FOT2826	4.2	11.5	1.0
	CZ	A:TYR1558	4.3	11.9	1.0
	ND1	A:HIS1473	4.3	9.8	1.0
	ZN	A:ZN2823	4.3	12.9	1.0
	HN1	A:FOT2826	4.4	13.7	1.0
	HN3	A:FOT2826	4.4	13.5	1.0
	HD1	A:TYR1558	4.5	14.1	1.0
	CD1	A:TYR1558	4.5	11.8	1.0
	CX	A:KCX1556	4.5	10.7	1.0
	HD1	A:HIS1473	4.6	11.8	1.0
	O	A:HOH2009	4.7	40.8	1.0
	OQ1	A:KCX1556	4.7	10.9	1.0
	HH12	A:ARG1475	4.8	14.2	1.0
	OD1	A:ASN1505	4.8	12.2	1.0
	CD2	A:HIS1473	4.9	10.8	1.0
	O	A:HOH2385	4.9	46.4	1.0
	HB3	A:ASN1505	5.0	13.0	1.0

Reference:

A.Grande-Garcia, N.Lallous, C.Diaz-Tejada, S.Ramon-Maiques. Structure, Functional Characterization and Evolution of the Dihydroorotase Domain of Human Cad. Structure V. 22 185 2014.
ISSN: ISSN 0969-2126
PubMed: 24332717
DOI: 10.1016/J.STR.2013.10.016

Page generated: Thu Aug 1 00:40:40 2024

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