Phosphorus in PDB 1a0q: 29G11 Complexed with Phenyl [1-(1-N-Succinylamino)Pentyl] Phosphonate

Protein crystallography data

The structure of 29G11 Complexed with Phenyl [1-(1-N-Succinylamino)Pentyl] Phosphonate, PDB code: 1a0q was solved by J.L.Buchbinder, R.C.Stephenson, T.S.Scanlan, R.J.Fletterick, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 50.00 / 2.30
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 36.780, 82.610, 132.340, 90.00, 90.00, 90.00
R / Rfree (%) 20.3 / 27.5

Phosphorus Binding Sites:

The binding sites of Phosphorus atom in the 29G11 Complexed with Phenyl [1-(1-N-Succinylamino)Pentyl] Phosphonate (pdb code 1a0q). 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 29G11 Complexed with Phenyl [1-(1-N-Succinylamino)Pentyl] Phosphonate, PDB code: 1a0q:

Phosphorus binding site 1 out of 1 in 1a0q

Go back to Phosphorus Binding Sites List in 1a0q
Phosphorus binding site 1 out of 1 in the 29G11 Complexed with Phenyl [1-(1-N-Succinylamino)Pentyl] Phosphonate


Mono view


Stereo pair view

A full contact list of Phosphorus with other atoms in the P binding site number 1 of 29G11 Complexed with Phenyl [1-(1-N-Succinylamino)Pentyl] Phosphonate within 5.0Å range:
probe atom residue distance (Å) B Occ
H:P214

b:31.9
occ:1.00
P H:HEP214 0.0 31.9 1.0
O1P H:HEP214 1.5 29.4 1.0
O2P H:HEP214 1.5 35.6 1.0
O3P H:HEP214 1.6 35.0 1.0
C1 H:HEP214 1.7 37.7 1.0
N1 H:HEP214 2.7 45.6 1.0
C2 H:HEP214 2.7 28.6 1.0
C11 H:HEP214 2.7 34.8 1.0
C6 H:HEP214 3.4 29.9 1.0
C12 H:HEP214 3.7 50.7 1.0
C10 H:HEP214 3.7 28.7 1.0
NE L:ARG96 3.8 36.1 1.0
NH2 L:ARG96 3.8 33.1 1.0
N H:TYR96 3.8 35.6 1.0
CE1 H:HIS35 4.0 20.8 1.0
C3 H:HEP214 4.0 26.6 1.0
O4 H:HEP214 4.0 46.8 1.0
NZ H:LYS93 4.3 37.8 1.0
NE2 H:HIS35 4.3 17.4 1.0
CZ L:ARG96 4.3 30.1 1.0
CA H:GLY95 4.4 25.6 1.0
O H:TYR96 4.4 50.8 1.0
CE H:LYS93 4.5 32.2 1.0
C H:GLY95 4.6 31.7 1.0
CA H:TYR96 4.7 42.8 1.0
ND1 H:HIS35 4.7 22.6 1.0
C7 H:HEP214 4.7 23.2 1.0
C H:TYR96 4.8 48.8 1.0
CB H:TYR96 4.8 46.1 1.0
C14 H:HEP214 4.9 53.6 1.0
CD L:ARG96 4.9 32.6 1.0
C9 H:HEP214 4.9 21.2 1.0

Reference:

J.L.Buchbinder, R.C.Stephenson, T.S.Scanlan, R.J.Fletterick. A Comparison of the Crystallographic Structures of Two Catalytic Antibodies with Esterase Activity. J.Mol.Biol. V. 282 1033 1998.
ISSN: ISSN 0022-2836
PubMed: 9753552
DOI: 10.1006/JMBI.1998.2025
Page generated: Fri Sep 25 11:56:45 2020

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