Phosphorus in PDB 1a8a: Rat Annexin V Complexed with Glycerophosphoserine

The structure of Rat Annexin V Complexed with Glycerophosphoserine, PDB code: 1a8a was solved by M.A.Swairjo, N.O.Concha, M.A.Kaetzel, J.R.Dedman, B.A.Seaton, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	10.00 / 1.90
Space group	H 3
Cell size a, b, c (Å), α, β, γ (°)	157.270, 157.270, 37.450, 90.00, 90.00, 120.00
R / Rfree (%)	20.1 / n/a

The binding sites of Phosphorus atom in the Rat Annexin V Complexed with Glycerophosphoserine (pdb code 1a8a). This binding sites where shown within 5.0 Angstroms radius around Phosphorus atom.
In total only one binding site of Phosphorus was determined in the Rat Annexin V Complexed with Glycerophosphoserine, PDB code: 1a8a:

Phosphorus binding site 1 out of 1 in the Rat Annexin V Complexed with Glycerophosphoserine


Mono view


Stereo pair view

A full contact list of Phosphorus with other atoms in the P binding site number 1 of Rat Annexin V Complexed with Glycerophosphoserine within 5.0Å range: probe atom residue distance (Å) B Occ A:P997 b:14.9 occ:0.84 P A:GSE997 0.0 14.9 0.8 O13 A:GSE997 1.4 14.9 0.8 O14 A:GSE997 1.5 14.9 0.8 O11 A:GSE997 1.5 14.9 0.8 O12 A:GSE997 1.6 14.9 0.8 C11 A:GSE997 2.6 18.2 0.8 C1 A:GSE997 2.7 29.5 0.8 CA A:CA407 3.7 10.0 1.0 C2 A:GSE997 3.9 29.5 0.8 O21 A:GSE997 3.9 29.5 0.8 O A:HOH510 3.9 30.7 1.0 N A:GLY186 3.9 11.5 1.0 C12 A:GSE997 4.0 18.2 0.8 CA A:GLY186 4.0 11.8 1.0 N A:GSE997 4.0 18.2 0.8 OE1 A:GLU226 4.1 20.3 1.0 OE2 A:GLU226 4.2 24.3 1.0 O A:GLY186 4.2 17.0 1.0 O31 A:GSE997 4.3 29.5 0.8 C A:GLY186 4.3 10.8 1.0 CD A:GLU226 4.3 25.4 1.0 C3 A:GSE997 4.6 29.5 0.8 OG1 A:THR187 4.6 11.5 1.0 O A:GLU226 4.7 24.1 1.0 C13 A:GSE997 4.8 18.2 0.8 O A:HOH512 4.9 15.2 1.0 O A:ARG225 4.9 21.8 1.0 CA A:GLU226 5.0 18.0 1.0

M.A.Swairjo, N.O.Concha, M.A.Kaetzel, J.R.Dedman, B.A.Seaton. Ca(2+)-Bridging Mechanism and Phospholipid Head Group Recognition in the Membrane-Binding Protein Annexin V. Nat.Struct.Biol. V. 2 968 1995.
ISSN: ISSN 1072-8368
PubMed: 7583670
DOI: 10.1038/NSB1195-968