Phosphorus in PDB 1aj7: Immunoglobulin 48G7 Germline Fab Antibody Complexed with Hapten 5-(Para-Nitrophenyl Phosphonate)-Pentanoic Acid. Affinity Maturation of An Esterolytic Antibody

The structure of Immunoglobulin 48G7 Germline Fab Antibody Complexed with Hapten 5-(Para-Nitrophenyl Phosphonate)-Pentanoic Acid. Affinity Maturation of An Esterolytic Antibody, PDB code: 1aj7 was solved by G.J.Wedemayer, L.H.Wang, P.A.Patten, P.G.Schultz, R.C.Stevens, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 2.10
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	46.100, 60.900, 73.100, 90.00, 104.80, 90.00
R / Rfree (%)	21.7 / 25.8

The binding sites of Phosphorus atom in the Immunoglobulin 48G7 Germline Fab Antibody Complexed with Hapten 5-(Para-Nitrophenyl Phosphonate)-Pentanoic Acid. Affinity Maturation of An Esterolytic Antibody (pdb code 1aj7). 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 Immunoglobulin 48G7 Germline Fab Antibody Complexed with Hapten 5-(Para-Nitrophenyl Phosphonate)-Pentanoic Acid. Affinity Maturation of An Esterolytic Antibody, PDB code: 1aj7:

Phosphorus binding site 1 out of 1 in the Immunoglobulin 48G7 Germline Fab Antibody Complexed with Hapten 5-(Para-Nitrophenyl Phosphonate)-Pentanoic Acid. Affinity Maturation of An Esterolytic Antibody


Mono view


Stereo pair view

A full contact list of Phosphorus with other atoms in the P binding site number 1 of Immunoglobulin 48G7 Germline Fab Antibody Complexed with Hapten 5-(Para-Nitrophenyl Phosphonate)-Pentanoic Acid. Affinity Maturation of An Esterolytic Antibody within 5.0Å range: probe atom residue distance (Å) B Occ H:P217 b:30.1 occ:1.00 P H:NPE217 0.0 30.1 1.0 O2P H:NPE217 1.4 29.4 1.0 O1P H:NPE217 1.4 30.0 1.0 O3P H:NPE217 1.5 34.9 1.0 C7 H:NPE217 1.8 31.7 1.0 H72 H:NPE217 2.4 0.0 0.0 H71 H:NPE217 2.4 0.0 0.0 C4 H:NPE217 2.5 40.5 1.0 C8 H:NPE217 2.7 30.4 1.0 H82 H:NPE217 2.8 0.0 0.0 HH21 L:ARG96 2.9 0.0 0.0 H81 H:NPE217 2.9 0.0 0.0 HE2 H:HIS35 3.1 0.0 0.0 C5 H:NPE217 3.3 42.2 1.0 H H:TYR99 3.4 0.0 0.0 H3 H:NPE217 3.4 0.0 0.0 HE L:ARG96 3.4 0.0 0.0 H5 H:NPE217 3.4 0.0 0.0 C3 H:NPE217 3.4 42.4 1.0 NE2 H:HIS35 3.7 10.8 1.0 NH2 L:ARG96 3.8 6.5 1.0 CE1 H:HIS35 4.0 9.3 1.0 C9 H:NPE217 4.1 30.2 1.0 NE L:ARG96 4.2 6.5 1.0 N H:TYR99 4.2 36.2 1.0 CD2 H:TYR33 4.3 25.5 1.0 H91 H:NPE217 4.4 0.0 0.0 H101 H:NPE217 4.4 0.0 0.0 HH22 L:ARG96 4.4 0.0 0.0 CZ L:ARG96 4.5 6.4 1.0 C6 H:NPE217 4.6 44.3 1.0 CD1 H:TYR98 4.6 52.0 1.0 CE1 H:TYR98 4.6 54.0 1.0 C2 H:NPE217 4.6 44.8 1.0 CA H:TYR99 4.7 36.3 1.0 H92 H:NPE217 4.8 0.0 0.0 CE2 H:TYR33 4.8 23.9 1.0 CB L:TYR91 4.9 5.3 1.0 C10 H:NPE217 4.9 27.3 1.0 CD2 H:HIS35 5.0 9.8 1.0

G.J.Wedemayer, P.A.Patten, L.H.Wang, P.G.Schultz, R.C.Stevens. Structural Insights Into the Evolution of An Antibody Combining Site. Science V. 276 1665 1997.
ISSN: ISSN 0036-8075
PubMed: 9180069
DOI: 10.1126/SCIENCE.276.5319.1665