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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 / Rfree (%) 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

Go back to 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

Go back to 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

Go back to 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

Go back to 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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