Fluorine in PDB 2tdd: Structures of Thymidylate Synthase with A C-Terminal Deletion: Role of the C-Terminus in Alignment of D/Ump and CH2H4FOLATE

Enzymatic activity of Structures of Thymidylate Synthase with A C-Terminal Deletion: Role of the C-Terminus in Alignment of D/Ump and CH2H4FOLATE

All present enzymatic activity of Structures of Thymidylate Synthase with A C-Terminal Deletion: Role of the C-Terminus in Alignment of D/Ump and CH2H4FOLATE:
2.1.1.45;

Protein crystallography data

The structure of Structures of Thymidylate Synthase with A C-Terminal Deletion: Role of the C-Terminus in Alignment of D/Ump and CH2H4FOLATE, PDB code: 2tdd was solved by K.M.Perry, C.W.Carreras, L.C.Chang, D.V.Santi, R.M.Stroud, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

*Resolution Low / High (Å)*	N/A / 2.70
*Space group*	P 6₁ 2 2
*Cell size a, b, c (Å), α, β, γ (°)*	78.400, 78.400, 242.200, 90.00, 90.00, 120.00
*R / R_free (%)*	19 / n/a

Fluorine Binding Sites:

The binding sites of Fluorine atom in the Structures of Thymidylate Synthase with A C-Terminal Deletion: Role of the C-Terminus in Alignment of D/Ump and CH2H4FOLATE (pdb code 2tdd). 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 Structures of Thymidylate Synthase with A C-Terminal Deletion: Role of the C-Terminus in Alignment of D/Ump and CH2H4FOLATE, PDB code: 2tdd:

Fluorine binding site 1 out of 1 in 2tdd

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Fluorine Binding Sites List in 2tdd

Fluorine binding site 1 out of 1 in the Structures of Thymidylate Synthase with A C-Terminal Deletion: Role of the C-Terminus in Alignment of D/Ump and CH2H4FOLATE

Mono view

Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Structures of Thymidylate Synthase with A C-Terminal Deletion: Role of the C-Terminus in Alignment of D/Ump and CH2H4FOLATE within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
A:F529 b:17.0 occ:1.00	F5	A:UFP529	0.0	17.0	1.0
	C5	A:UFP529	1.3	22.9	1.0
	C6	A:UFP529	2.4	21.4	1.0
	C4	A:UFP529	2.4	25.4	1.0
	N10	A:THF568	2.5	41.5	1.0
	C14	A:THF568	2.9	41.5	1.0
	O4	A:UFP529	2.9	27.3	1.0
	C13	A:THF568	2.9	40.1	1.0
	C9	A:THF568	3.3	40.6	1.0
	N1	A:UFP529	3.6	21.7	1.0
	N3	A:UFP529	3.6	23.8	1.0
	C12	A:THF568	3.7	41.8	1.0
	C15	A:THF568	3.9	41.8	1.0
	C6	A:THF568	4.0	41.3	1.0
	CA	A:GLY225	4.0	13.6	1.0
	C2	A:UFP529	4.1	22.6	1.0
	N5	A:THF568	4.3	40.0	1.0
	CP1	A:THF568	4.5	40.0	1.0
	C11	A:THF568	4.6	42.5	1.0
	N	A:GLY225	4.6	16.1	1.0
	OD2	A:ASP221	4.7	13.7	1.0
	C16	A:THF568	4.7	43.3	1.0
	C1'	A:UFP529	4.7	19.4	1.0
	O	A:LEU224	4.8	16.5	1.0
	O4	A:THF568	4.8	36.3	1.0
	C	A:LEU224	4.9	17.3	1.0
	CB	A:ASP221	5.0	18.9	1.0

Reference:

K.M.Perry, C.W.Carreras, L.C.Chang, D.V.Santi, R.M.Stroud. Structures of Thymidylate Synthase with A C-Terminal Deletion: Role of the C-Terminus in Alignment of 2'-Deoxyuridine 5'-Monophosphate and 5,10-Methylenetetrahydrofolate. Biochemistry V. 32 7116 1993.
ISSN: ISSN 0006-2960
PubMed: 8343503
DOI: 10.1021/BI00079A007

Page generated: Wed Jul 31 16:00:35 2024

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