Fluorine in PDB 1dvr: Structure of A Mutant Adenylate Kinase Ligated with An Atp-Analogue Showing Domain Closure Over Atp

Enzymatic activity of Structure of A Mutant Adenylate Kinase Ligated with An Atp-Analogue Showing Domain Closure Over Atp

All present enzymatic activity of Structure of A Mutant Adenylate Kinase Ligated with An Atp-Analogue Showing Domain Closure Over Atp:
2.7.4.3;

Protein crystallography data

The structure of Structure of A Mutant Adenylate Kinase Ligated with An Atp-Analogue Showing Domain Closure Over Atp, PDB code: 1dvr was solved by G.J.Schlauderer, G.E.Schulz, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

*Resolution Low / High (Å)*	10.00 / 2.36
*Space group*	P 2₁ 2₁ 2₁
*Cell size a, b, c (Å), α, β, γ (°)*	47.800, 73.400, 118.800, 90.00, 90.00, 90.00
*R / R_free (%)*	19.1 / n/a

Fluorine Binding Sites:

The binding sites of Fluorine atom in the Structure of A Mutant Adenylate Kinase Ligated with An Atp-Analogue Showing Domain Closure Over Atp (pdb code 1dvr). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 4 binding sites of Fluorine where determined in the Structure of A Mutant Adenylate Kinase Ligated with An Atp-Analogue Showing Domain Closure Over Atp, PDB code: 1dvr:
Jump to Fluorine binding site number: 1; 2; 3; 4;

Fluorine binding site 1 out of 4 in 1dvr

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Fluorine Binding Sites List in 1dvr

Fluorine binding site 1 out of 4 in the Structure of A Mutant Adenylate Kinase Ligated with An Atp-Analogue Showing Domain Closure Over Atp

Mono view

Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Structure of A Mutant Adenylate Kinase Ligated with An Atp-Analogue Showing Domain Closure Over Atp within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
A:F230 b:24.9 occ:1.00	F1B	A:ATF230	0.0	24.9	1.0
	C3B	A:ATF230	1.4	15.3	1.0
	F2B	A:ATF230	1.9	13.2	1.0
	PB	A:ATF230	2.6	8.4	1.0
	PG	A:ATF230	2.6	15.7	1.0
	O	A:HOH249	2.7	36.8	1.0
	O3A	A:ATF230	2.7	13.5	1.0
	NZ	B:LYS55	3.0	21.1	1.0
	O1G	A:ATF230	3.0	24.1	1.0
	O2G	A:ATF230	3.0	10.2	1.0
	O	B:HOH231	3.1	26.4	1.0
	O1A	A:ATF230	3.3	14.6	1.0
	PA	A:ATF230	3.4	11.3	1.0
	O1B	A:ATF230	3.4	8.5	1.0
	NH1	A:ARG132	3.6	9.9	1.0
	O2B	A:ATF230	3.8	3.7	1.0
	O3G	A:ATF230	4.0	18.6	1.0
	N	A:GLY18	4.0	10.7	1.0
	O2A	A:ATF230	4.1	22.6	1.0
	CA	A:GLY18	4.3	13.0	1.0
	CE	B:LYS55	4.5	19.0	1.0
	O	B:HOH273	4.6	41.6	1.0
	O5'	A:ATF230	4.7	14.0	1.0
	CZ	A:ARG132	4.8	2.6	1.0

Fluorine binding site 2 out of 4 in 1dvr

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Fluorine Binding Sites List in 1dvr

Fluorine binding site 2 out of 4 in the Structure of A Mutant Adenylate Kinase Ligated with An Atp-Analogue Showing Domain Closure Over Atp

Mono view

Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of Structure of A Mutant Adenylate Kinase Ligated with An Atp-Analogue Showing Domain Closure Over Atp within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
A:F230 b:13.2 occ:1.00	F2B	A:ATF230	0.0	13.2	1.0
	C3B	A:ATF230	1.4	15.3	1.0
	F1B	A:ATF230	1.9	24.9	1.0
	PG	A:ATF230	2.6	15.7	1.0
	O1G	A:ATF230	2.6	24.1	1.0
	PB	A:ATF230	2.6	8.4	1.0
	O	A:HOH249	3.0	36.8	1.0
	O3A	A:ATF230	3.1	13.5	1.0
	O2B	A:ATF230	3.1	3.7	1.0
	N	A:GLY18	3.3	10.7	1.0
	O3G	A:ATF230	3.5	18.6	1.0
	CE	A:LYS17	3.5	14.0	1.0
	CB	A:LYS17	3.6	13.0	1.0
	O2G	A:ATF230	3.7	10.2	1.0
	O1B	A:ATF230	3.9	8.5	1.0
	NZ	A:LYS17	3.9	17.9	1.0
	CA	A:GLY18	4.0	13.0	1.0
	C	A:LYS17	4.1	11.8	1.0
	CA	A:LYS17	4.1	11.5	1.0
	N	A:LYS17	4.2	9.3	1.0
	PA	A:ATF230	4.3	11.3	1.0
	NZ	B:LYS55	4.4	21.1	1.0
	CG	A:LYS17	4.5	5.0	1.0
	CD	A:LYS17	4.6	13.1	1.0
	O2A	A:ATF230	4.8	22.6	1.0
	O1A	A:ATF230	4.8	14.6	1.0
	O	B:HOH231	4.8	26.4	1.0

Fluorine binding site 3 out of 4 in 1dvr

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Fluorine Binding Sites List in 1dvr

Fluorine binding site 3 out of 4 in the Structure of A Mutant Adenylate Kinase Ligated with An Atp-Analogue Showing Domain Closure Over Atp

Mono view

Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 3 of Structure of A Mutant Adenylate Kinase Ligated with An Atp-Analogue Showing Domain Closure Over Atp within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
B:F230 b:36.4 occ:1.00	F1B	B:ATF230	0.0	36.4	1.0
	C3B	B:ATF230	1.4	30.2	1.0
	F2B	B:ATF230	1.8	33.3	1.0
	PG	B:ATF230	2.5	30.6	1.0
	O1G	B:ATF230	2.6	29.6	1.0
	PB	B:ATF230	2.7	16.1	1.0
	O3A	B:ATF230	3.0	7.1	1.0
	NZ	A:LYS55	3.2	37.8	1.0
	O2G	B:ATF230	3.5	34.1	1.0
	O1B	B:ATF230	3.6	25.6	1.0
	O3G	B:ATF230	3.7	34.1	1.0
	O2B	B:ATF230	3.8	16.6	1.0
	PA	B:ATF230	3.8	8.4	1.0
	O1A	B:ATF230	3.8	13.7	1.0
	NH1	B:ARG132	4.0	10.9	1.0
	N	B:GLY18	4.2	14.8	1.0
	CA	B:GLY18	4.4	15.9	1.0
	O2A	B:ATF230	4.6	4.9	1.0
	CE	A:LYS55	4.6	36.1	1.0
	CE	B:LYS17	4.9	2.5	1.0
	NZ	B:LYS17	4.9	15.3	1.0

Fluorine binding site 4 out of 4 in 1dvr

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Fluorine Binding Sites List in 1dvr

Fluorine binding site 4 out of 4 in the Structure of A Mutant Adenylate Kinase Ligated with An Atp-Analogue Showing Domain Closure Over Atp

Mono view

Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 4 of Structure of A Mutant Adenylate Kinase Ligated with An Atp-Analogue Showing Domain Closure Over Atp within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
B:F230 b:33.3 occ:1.00	F2B	B:ATF230	0.0	33.3	1.0
	C3B	B:ATF230	1.4	30.2	1.0
	F1B	B:ATF230	1.8	36.4	1.0
	PB	B:ATF230	2.4	16.1	1.0
	PG	B:ATF230	2.7	30.6	1.0
	O2B	B:ATF230	2.7	16.6	1.0
	O1G	B:ATF230	2.9	29.6	1.0
	O3G	B:ATF230	3.1	34.1	1.0
	O3A	B:ATF230	3.1	7.1	1.0
	CE	B:LYS17	3.2	2.5	1.0
	NZ	B:LYS17	3.3	15.3	1.0
	CB	B:LYS17	3.7	14.9	1.0
	O1B	B:ATF230	3.7	25.6	1.0
	N	B:GLY18	3.8	14.8	1.0
	O2G	B:ATF230	4.1	34.1	1.0
	CD	B:LYS17	4.3	11.1	1.0
	CG	B:LYS17	4.3	5.0	1.0
	N	B:LYS17	4.3	8.3	1.0
	CA	B:LYS17	4.4	11.7	1.0
	C	B:LYS17	4.5	11.1	1.0
	CA	B:GLY18	4.5	15.9	1.0
	PA	B:ATF230	4.5	8.4	1.0
	NE2	A:GLN59	4.6	73.1	1.0
	NZ	A:LYS55	4.7	37.8	1.0
	O1A	B:ATF230	5.0	13.7	1.0

Reference:

G.J.Schlauderer, K.Proba, G.E.Schulz. Structure of A Mutant Adenylate Kinase Ligated with An Atp-Analogue Showing Domain Closure Over Atp. J.Mol.Biol. V. 256 223 1996.
ISSN: ISSN 0022-2836
PubMed: 8594191
DOI: 10.1006/JMBI.1996.0080

Page generated: Wed Jul 31 11:06:08 2024

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