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Xenon in PDB 1l1g: The Structure of Porcine Pancreatic Elastase Complexed with Xenon and Bromide, Cryoprotected with Glycerol

Enzymatic activity of The Structure of Porcine Pancreatic Elastase Complexed with Xenon and Bromide, Cryoprotected with Glycerol

All present enzymatic activity of The Structure of Porcine Pancreatic Elastase Complexed with Xenon and Bromide, Cryoprotected with Glycerol:
3.4.21.36;

Protein crystallography data

The structure of The Structure of Porcine Pancreatic Elastase Complexed with Xenon and Bromide, Cryoprotected with Glycerol, PDB code: 1l1g was solved by S.Panjikar, P.A.Tucker, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 35.00 / 1.50
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 50.280, 57.700, 74.110, 90.00, 90.00, 90.00
R / Rfree (%) 17.3 / 21.5

Other elements in 1l1g:

The structure of The Structure of Porcine Pancreatic Elastase Complexed with Xenon and Bromide, Cryoprotected with Glycerol also contains other interesting chemical elements:

Bromine (Br) 8 atoms
Sodium (Na) 1 atom

Xenon Binding Sites:

The binding sites of Xenon atom in the The Structure of Porcine Pancreatic Elastase Complexed with Xenon and Bromide, Cryoprotected with Glycerol (pdb code 1l1g). This binding sites where shown within 5.0 Angstroms radius around Xenon atom.
In total only one binding site of Xenon was determined in the The Structure of Porcine Pancreatic Elastase Complexed with Xenon and Bromide, Cryoprotected with Glycerol, PDB code: 1l1g:

Xenon binding site 1 out of 1 in 1l1g

Go back to Xenon Binding Sites List in 1l1g
Xenon binding site 1 out of 1 in the The Structure of Porcine Pancreatic Elastase Complexed with Xenon and Bromide, Cryoprotected with Glycerol


Mono view


Stereo pair view

A full contact list of Xenon with other atoms in the Xe binding site number 1 of The Structure of Porcine Pancreatic Elastase Complexed with Xenon and Bromide, Cryoprotected with Glycerol within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Xe261

b:15.9
occ:0.83
 OG A:SER188 3.5 15.4 1.0
O A:CYS184 3.6 11.2 1.0
C A:CYS184 3.8 9.4 1.0
CG2 A:THR206 4.1 7.8 1.0
CA A:PHE208 4.1 7.2 1.0
CG1 A:VAL209 4.1 10.7 1.0
O2 A:SO4251 4.2 12.6 0.5
N A:GLN185 4.2 9.7 1.0
N A:VAL209 4.2 9.6 1.0
CG2 A:VAL209 4.2 9.6 1.0
O A:HOH346 4.2 15.6 1.0
C A:PHE208 4.3 8.5 1.0
CA A:CYS184 4.3 10.8 1.0
N A:CYS184 4.4 9.2 1.0
O A:SER207 4.4 11.0 1.0
CA A:GLN185 4.4 9.3 1.0
N A:PHE208 4.5 8.8 1.0
N A:SER188 4.5 9.3 1.0
C A:SER207 4.6 8.8 1.0
CB A:VAL209 4.7 12.1 1.0
O A:HOH397 4.7 20.8 1.0
CB A:SER188 4.7 10.7 1.0
CA A:SER188 4.7 9.4 1.0
C A:GLY183 4.8 9.0 1.0
O A:PHE208 4.9 9.4 1.0
O4 A:SO4251 4.9 53.7 0.5

Reference:

S.Panjikar, P.A.Tucker. Xenon Derivatization of Halide-Soaked Protein Crystals. Acta Crystallogr.,Sect.D V. 58 1413 2002.
ISSN: ISSN 0907-4449
PubMed: 12198297
DOI: 10.1107/S0907444902011010
Page generated: Tue Aug 19 17:43:45 2025

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