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Fluorine in PDB 4axx: The Catalytically Active Fully Closed Conformation of Human Phosphoglycerate Kinase in Complex with Adp 3-Phosphoglycerate and Beryllium Trifluoride

Enzymatic activity of The Catalytically Active Fully Closed Conformation of Human Phosphoglycerate Kinase in Complex with Adp 3-Phosphoglycerate and Beryllium Trifluoride

All present enzymatic activity of The Catalytically Active Fully Closed Conformation of Human Phosphoglycerate Kinase in Complex with Adp 3-Phosphoglycerate and Beryllium Trifluoride:
2.7.2.3;

Protein crystallography data

The structure of The Catalytically Active Fully Closed Conformation of Human Phosphoglycerate Kinase in Complex with Adp 3-Phosphoglycerate and Beryllium Trifluoride, PDB code: 4axx was solved by M.W.Bowler, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 1.74
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 38.820, 90.800, 108.540, 90.00, 90.00, 90.00
R / Rfree (%) 16.976 / 20.65

Other elements in 4axx:

The structure of The Catalytically Active Fully Closed Conformation of Human Phosphoglycerate Kinase in Complex with Adp 3-Phosphoglycerate and Beryllium Trifluoride also contains other interesting chemical elements:

Magnesium (Mg) 1 atom
Chlorine (Cl) 1 atom

Fluorine Binding Sites:

The binding sites of Fluorine atom in the The Catalytically Active Fully Closed Conformation of Human Phosphoglycerate Kinase in Complex with Adp 3-Phosphoglycerate and Beryllium Trifluoride (pdb code 4axx). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 3 binding sites of Fluorine where determined in the The Catalytically Active Fully Closed Conformation of Human Phosphoglycerate Kinase in Complex with Adp 3-Phosphoglycerate and Beryllium Trifluoride, PDB code: 4axx:
Jump to Fluorine binding site number: 1; 2; 3;

Fluorine binding site 1 out of 3 in 4axx

Go back to Fluorine Binding Sites List in 4axx
Fluorine binding site 1 out of 3 in the The Catalytically Active Fully Closed Conformation of Human Phosphoglycerate Kinase in Complex with Adp 3-Phosphoglycerate and Beryllium Trifluoride


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of The Catalytically Active Fully Closed Conformation of Human Phosphoglycerate Kinase in Complex with Adp 3-Phosphoglycerate and Beryllium Trifluoride within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F1422

b:16.2
occ:1.00
F1 A:BEF1422 0.0 16.2 1.0
BE A:BEF1422 1.8 15.7 1.0
MG A:MG1418 2.1 15.4 1.0
NZ A:LYS216 2.5 15.4 1.0
O A:HOH2388 2.7 16.6 1.0
O2A A:ADP1420 2.8 14.0 1.0
O2 A:3PG1421 2.9 13.2 1.0
O3B A:ADP1420 2.9 12.7 1.0
F2 A:BEF1422 3.0 17.5 1.0
O A:HOH2236 3.0 19.9 1.0
F3 A:BEF1422 3.0 15.7 1.0
O1 A:3PG1421 3.1 13.0 1.0
O1B A:ADP1420 3.1 14.2 1.0
PB A:ADP1420 3.3 13.9 1.0
C1 A:3PG1421 3.3 12.0 1.0
CE A:LYS216 3.4 16.4 1.0
CD A:LYS216 3.6 15.6 1.0
PA A:ADP1420 3.8 14.0 1.0
O3A A:ADP1420 4.0 14.4 1.0
OD2 A:ASP375 4.0 15.0 1.0
O1A A:ADP1420 4.3 15.9 1.0
O A:HOH2196 4.4 14.5 1.0
NZ A:LYS220 4.4 23.2 1.0
O2B A:ADP1420 4.7 14.6 1.0
O A:HOH2418 4.7 16.2 1.0
O A:HOH2051 4.8 17.2 1.0
C2 A:3PG1421 4.8 11.7 1.0
N A:GLY374 4.8 11.9 1.0
O4P A:3PG1421 4.8 12.0 1.0
CG A:LYS216 4.8 15.7 1.0

Fluorine binding site 2 out of 3 in 4axx

Go back to Fluorine Binding Sites List in 4axx
Fluorine binding site 2 out of 3 in the The Catalytically Active Fully Closed Conformation of Human Phosphoglycerate Kinase in Complex with Adp 3-Phosphoglycerate and Beryllium Trifluoride


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of The Catalytically Active Fully Closed Conformation of Human Phosphoglycerate Kinase in Complex with Adp 3-Phosphoglycerate and Beryllium Trifluoride within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F1422

b:17.5
occ:1.00
F2 A:BEF1422 0.0 17.5 1.0
BE A:BEF1422 1.8 15.7 1.0
O2 A:3PG1421 2.7 13.2 1.0
O1B A:ADP1420 2.7 14.2 1.0
O A:HOH2196 2.7 14.5 1.0
NZ A:LYS220 2.8 23.2 1.0
N A:GLY397 2.9 11.2 1.0
F3 A:BEF1422 2.9 15.7 1.0
F1 A:BEF1422 3.0 16.2 1.0
CE A:LYS220 3.3 23.8 1.0
O A:HOH2193 3.6 11.7 1.0
CA A:GLY397 3.7 11.7 1.0
CA A:GLY396 3.7 11.1 1.0
C A:GLY396 3.8 10.7 1.0
C1 A:3PG1421 3.9 12.0 1.0
PB A:ADP1420 4.1 13.9 1.0
NZ A:LYS216 4.2 15.4 1.0
N A:GLY396 4.3 11.1 1.0
CD A:LYS216 4.4 15.6 1.0
O A:HOH2198 4.4 27.7 1.0
OD1 A:ASN337 4.5 14.4 1.0
O1 A:3PG1421 4.5 13.0 1.0
O3B A:ADP1420 4.5 12.7 1.0
ND2 A:ASN337 4.6 12.4 1.0
MG A:MG1418 4.6 15.4 1.0
O1A A:ADP1420 4.7 15.9 1.0
CD A:LYS220 4.8 22.8 1.0
O3A A:ADP1420 4.8 14.4 1.0
O2A A:ADP1420 4.8 14.0 1.0
O A:GLY396 4.9 11.1 1.0
CE A:LYS216 4.9 16.4 1.0
O4P A:3PG1421 4.9 12.0 1.0
CG A:ASN337 5.0 11.9 1.0
PA A:ADP1420 5.0 14.0 1.0
NE2 A:HIS170 5.0 11.7 1.0
C A:GLY397 5.0 12.0 1.0

Fluorine binding site 3 out of 3 in 4axx

Go back to Fluorine Binding Sites List in 4axx
Fluorine binding site 3 out of 3 in the The Catalytically Active Fully Closed Conformation of Human Phosphoglycerate Kinase in Complex with Adp 3-Phosphoglycerate and Beryllium Trifluoride


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 3 of The Catalytically Active Fully Closed Conformation of Human Phosphoglycerate Kinase in Complex with Adp 3-Phosphoglycerate and Beryllium Trifluoride within 5.0Å range:
probe atom residue distance (Å) B Occ
A:F1422

b:15.7
occ:1.00
F3 A:BEF1422 0.0 15.7 1.0
BE A:BEF1422 1.8 15.7 1.0
O2 A:3PG1421 2.7 13.2 1.0
NH2 A:ARG39 2.8 11.3 1.0
N A:GLY374 2.9 11.9 1.0
F2 A:BEF1422 2.9 17.5 1.0
F1 A:BEF1422 3.0 16.2 1.0
O1B A:ADP1420 3.0 14.2 1.0
C1 A:3PG1421 3.1 12.0 1.0
O1 A:3PG1421 3.1 13.0 1.0
O3B A:ADP1420 3.3 12.7 1.0
CA A:GLY373 3.4 11.3 1.0
O A:HOH2193 3.5 11.7 1.0
O A:HOH2388 3.5 16.6 1.0
PB A:ADP1420 3.6 13.9 1.0
C A:GLY373 3.6 11.5 1.0
N A:GLY396 3.6 11.1 1.0
CZ A:ARG39 3.8 11.5 1.0
CA A:GLY396 3.8 11.1 1.0
CA A:GLY374 3.9 12.7 1.0
MG A:MG1418 4.0 15.4 1.0
NH1 A:ARG39 4.1 11.8 1.0
O2B A:ADP1420 4.3 14.6 1.0
C2 A:3PG1421 4.3 11.7 1.0
N A:GLY397 4.6 11.2 1.0
C A:GLY395 4.6 10.9 1.0
N A:GLY373 4.7 11.5 1.0
C A:GLY396 4.8 10.7 1.0
O A:THR394 4.8 12.2 1.0
N A:ASP375 4.8 13.3 1.0
O A:GLY373 4.8 12.5 1.0
NE A:ARG39 4.9 11.6 1.0
OD1 A:ASN337 4.9 14.4 1.0
C A:GLY374 5.0 13.5 1.0
O A:HOH2196 5.0 14.5 1.0

Reference:

M.W.Bowler, M.J.Cliff, G.M.Blackburn, J.P.Waltho. Catalytic Activity in the Transitions State Analogue Stabilised Conformation of A Phosphoryl Transfer Enzyme To Be Published.
Page generated: Sun Dec 13 11:58:57 2020

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