Phosphorus in PDB 1agr: Complex of ALF4-Activated Gi-Alpha-1 with RGS4

The structure of Complex of ALF4-Activated Gi-Alpha-1 with RGS4, PDB code: 1agr was solved by J.J.G.Tesmer, S.R.Sprang, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	5.00 / 2.80
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	164.000, 97.200, 110.000, 90.00, 90.00, 90.00
R / Rfree (%)	21.6 / 29.1

The binding sites of Phosphorus atom in the Complex of ALF4-Activated Gi-Alpha-1 with RGS4 (pdb code 1agr). This binding sites where shown within 5.0 Angstroms radius around Phosphorus atom.
In total 4 binding sites of Phosphorus where determined in the Complex of ALF4-Activated Gi-Alpha-1 with RGS4, PDB code: 1agr:
Jump to Phosphorus binding site number: 1; 2; 3; 4;

Phosphorus binding site 1 out of 4 in the Complex of ALF4-Activated Gi-Alpha-1 with RGS4


Mono view


Stereo pair view

A full contact list of Phosphorus with other atoms in the P binding site number 1 of Complex of ALF4-Activated Gi-Alpha-1 with RGS4 within 5.0Å range: probe atom residue distance (Å) B Occ A:P355 b:16.9 occ:1.00 PB A:GDP355 0.0 16.9 1.0 O2B A:GDP355 1.5 2.0 1.0 O3B A:GDP355 1.5 28.5 1.0 O1B A:GDP355 1.5 7.8 1.0 O3A A:GDP355 1.7 11.5 1.0 PA A:GDP355 2.8 19.2 1.0 O1A A:GDP355 3.1 28.3 1.0 AL A:ALF357 3.2 12.3 1.0 F3 A:ALF357 3.2 19.3 1.0 MG A:MG356 3.2 14.3 1.0 O2A A:GDP355 3.4 20.3 1.0 O A:HOH365 3.4 11.6 1.0 F4 A:ALF357 3.6 8.3 1.0 F2 A:ALF357 3.6 2.6 1.0 N A:GLU43 3.7 25.9 1.0 N A:GLY45 3.7 19.4 1.0 F1 A:ALF357 3.8 9.2 1.0 CA A:GLU43 3.9 27.7 1.0 N A:SER44 3.9 23.6 1.0 N A:LYS46 4.0 20.2 1.0 NZ A:LYS46 4.0 15.0 1.0 NH1 A:ARG178 4.0 22.4 1.0 O5' A:GDP355 4.0 7.9 1.0 N A:SER47 4.1 15.2 1.0 O A:HOH364 4.1 15.1 1.0 C A:GLU43 4.1 26.6 1.0 OG A:SER47 4.3 19.6 1.0 CA A:GLY45 4.4 17.8 1.0 C A:GLY45 4.4 21.7 1.0 CE A:LYS46 4.5 19.8 1.0 CB A:LYS46 4.5 13.5 1.0 OG A:SER44 4.5 33.8 1.0 CB A:SER47 4.6 24.8 1.0 CA A:LYS46 4.6 15.0 1.0 C5' A:GDP355 4.7 7.8 1.0 C A:SER44 4.7 23.2 1.0 CZ A:ARG178 4.8 19.8 1.0 CA A:SER44 4.8 22.1 1.0 CG A:LYS46 4.8 2.0 1.0 C A:GLY42 4.9 21.6 1.0 C A:LYS46 4.9 15.8 1.0 NH2 A:ARG178 4.9 11.1 1.0 CA A:SER47 4.9 17.5 1.0 O A:GLU43 5.0 29.2 1.0

Phosphorus binding site 2 out of 4 in the Complex of ALF4-Activated Gi-Alpha-1 with RGS4


Mono view


Stereo pair view

A full contact list of Phosphorus with other atoms in the P binding site number 2 of Complex of ALF4-Activated Gi-Alpha-1 with RGS4 within 5.0Å range: probe atom residue distance (Å) B Occ A:P355 b:19.2 occ:1.00 PA A:GDP355 0.0 19.2 1.0 O2A A:GDP355 1.5 20.3 1.0 O1A A:GDP355 1.5 28.3 1.0 O5' A:GDP355 1.6 7.9 1.0 O3A A:GDP355 1.6 11.5 1.0 C5' A:GDP355 2.6 7.8 1.0 PB A:GDP355 2.8 16.9 1.0 O2B A:GDP355 2.9 2.0 1.0 O3B A:GDP355 3.4 28.5 1.0 O A:HOH365 3.5 11.6 1.0 OG1 A:THR48 3.7 37.4 1.0 NH1 A:ARG178 3.8 22.4 1.0 C4' A:GDP355 3.8 11.3 1.0 O1B A:GDP355 3.9 7.8 1.0 CA A:GLY45 4.0 17.8 1.0 C3' A:GDP355 4.0 15.4 1.0 N A:GLY45 4.1 19.4 1.0 C A:GLY45 4.3 21.7 1.0 CB A:SER47 4.3 24.8 1.0 N A:SER47 4.3 15.2 1.0 C2' A:GDP355 4.4 22.2 1.0 N A:THR48 4.4 19.7 1.0 MG A:MG356 4.6 14.3 1.0 O A:GLY45 4.6 24.1 1.0 CZ A:ARG178 4.6 19.8 1.0 O4' A:GDP355 4.7 18.2 1.0 CA A:GLU43 4.7 27.7 1.0 N A:LYS46 4.7 20.2 1.0 CA A:SER47 4.8 17.5 1.0 C A:GLU43 4.8 26.6 1.0 OG A:SER47 4.8 19.6 1.0 CB A:THR48 4.9 22.1 1.0 F2 A:ALF357 4.9 2.6 1.0 O A:GLU43 5.0 29.2 1.0

Phosphorus binding site 3 out of 4 in the Complex of ALF4-Activated Gi-Alpha-1 with RGS4


Mono view


Stereo pair view

A full contact list of Phosphorus with other atoms in the P binding site number 3 of Complex of ALF4-Activated Gi-Alpha-1 with RGS4 within 5.0Å range: probe atom residue distance (Å) B Occ D:P355 b:27.5 occ:1.00 PB D:GDP355 0.0 27.5 1.0 O3B D:GDP355 1.5 31.5 1.0 O2B D:GDP355 1.5 17.7 1.0 O1B D:GDP355 1.5 17.7 1.0 O3A D:GDP355 1.7 19.4 1.0 PA D:GDP355 2.8 21.4 1.0 F3 D:ALF357 3.1 21.1 1.0 AL D:ALF357 3.1 28.8 1.0 O1A D:GDP355 3.2 27.2 1.0 MG D:MG356 3.2 15.2 1.0 O2A D:GDP355 3.4 30.6 1.0 O D:HOH366 3.5 14.5 1.0 F2 D:ALF357 3.6 14.2 1.0 F4 D:ALF357 3.6 18.6 1.0 N D:GLU43 3.7 23.5 1.0 N D:GLY45 3.8 19.9 1.0 F1 D:ALF357 3.8 22.4 1.0 CA D:GLU43 3.9 28.3 1.0 N D:SER44 3.9 32.5 1.0 N D:LYS46 3.9 16.3 1.0 NZ D:LYS46 4.0 32.9 1.0 O D:HOH365 4.0 18.9 1.0 N D:SER47 4.0 24.9 1.0 O5' D:GDP355 4.1 25.3 1.0 NH1 D:ARG178 4.1 15.3 1.0 C D:GLU43 4.1 31.1 1.0 OG D:SER47 4.3 24.1 1.0 C D:GLY45 4.3 19.5 1.0 CA D:GLY45 4.4 20.7 1.0 CB D:LYS46 4.4 6.4 1.0 CE D:LYS46 4.4 34.7 1.0 OG D:SER44 4.5 41.2 1.0 CA D:LYS46 4.6 16.5 1.0 CB D:SER47 4.6 32.6 1.0 C5' D:GDP355 4.7 23.2 1.0 CG D:LYS46 4.7 18.4 1.0 C D:SER44 4.8 20.8 1.0 CZ D:ARG178 4.8 18.1 1.0 CA D:SER44 4.8 25.3 1.0 C D:LYS46 4.8 21.3 1.0 C D:GLY42 4.8 20.2 1.0 NH2 D:ARG178 4.9 11.8 1.0 O D:GLU43 4.9 30.1 1.0 CA D:SER47 4.9 26.7 1.0

Phosphorus binding site 4 out of 4 in the Complex of ALF4-Activated Gi-Alpha-1 with RGS4


Mono view


Stereo pair view

A full contact list of Phosphorus with other atoms in the P binding site number 4 of Complex of ALF4-Activated Gi-Alpha-1 with RGS4 within 5.0Å range: probe atom residue distance (Å) B Occ D:P355 b:21.4 occ:1.00 PA D:GDP355 0.0 21.4 1.0 O1A D:GDP355 1.5 27.2 1.0 O2A D:GDP355 1.5 30.6 1.0 O5' D:GDP355 1.6 25.3 1.0 O3A D:GDP355 1.6 19.4 1.0 C5' D:GDP355 2.6 23.2 1.0 PB D:GDP355 2.8 27.5 1.0 O2B D:GDP355 2.9 17.7 1.0 O3B D:GDP355 3.5 31.5 1.0 O D:HOH366 3.5 14.5 1.0 OG1 D:THR48 3.7 39.6 1.0 NH1 D:ARG178 3.8 15.3 1.0 C4' D:GDP355 3.8 23.4 1.0 O1B D:GDP355 3.9 17.7 1.0 CA D:GLY45 4.0 20.7 1.0 C3' D:GDP355 4.0 17.4 1.0 N D:GLY45 4.1 19.9 1.0 CB D:SER47 4.2 32.6 1.0 C D:GLY45 4.2 19.5 1.0 N D:SER47 4.3 24.9 1.0 N D:THR48 4.4 26.5 1.0 C2' D:GDP355 4.4 28.1 1.0 MG D:MG356 4.5 15.2 1.0 O D:GLY45 4.6 17.2 1.0 CZ D:ARG178 4.7 18.1 1.0 N D:LYS46 4.7 16.3 1.0 CA D:SER47 4.7 26.7 1.0 O4' D:GDP355 4.7 33.7 1.0 CA D:GLU43 4.7 28.3 1.0 OG D:SER47 4.8 24.1 1.0 C D:GLU43 4.8 31.1 1.0 F2 D:ALF357 4.8 14.2 1.0 CB D:THR48 4.8 27.1 1.0 O D:GLU43 4.9 30.1 1.0 C D:SER47 4.9 28.4 1.0 C8 D:GDP355 5.0 39.6 1.0 CD D:ARG178 5.0 10.0 1.0

J.J.Tesmer, D.M.Berman, A.G.Gilman, S.R.Sprang. Structure of RGS4 Bound to ALF4--Activated G(I ALPHA1): Stabilization of the Transition State For Gtp Hydrolysis. Cell(Cambridge,Mass.) V. 89 251 1997.
ISSN: ISSN 0092-8674
PubMed: 9108480
DOI: 10.1016/S0092-8674(00)80204-4