Atomistry » Fluorine » PDB 1bwf-1dvy » 1dvr
Atomistry »
  Fluorine »
    PDB 1bwf-1dvy »
      1dvr »

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: Mon Jul 14 10:33:50 2025

Last articles

Mg in 4QW1
Mg in 4QW0
Mg in 4QVY
Mg in 4QW3
Mg in 4QVW
Mg in 4QVQ
Mg in 4QVV
Mg in 4QVP
Mg in 4QVM
Mg in 4QVN
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy