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Iodine in PDB 2ha7: Crystal Structure of Mutant S203A of Mouse Acetylcholinesterase Complexed with Butyrylthiocholine

Enzymatic activity of Crystal Structure of Mutant S203A of Mouse Acetylcholinesterase Complexed with Butyrylthiocholine

All present enzymatic activity of Crystal Structure of Mutant S203A of Mouse Acetylcholinesterase Complexed with Butyrylthiocholine:
3.1.1.7;

Protein crystallography data

The structure of Crystal Structure of Mutant S203A of Mouse Acetylcholinesterase Complexed with Butyrylthiocholine, PDB code: 2ha7 was solved by Y.Bourne, Z.Radic, G.Sulzenbacher, E.Kim, P.Taylor, P.Marchot, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 2.66
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 79.325, 111.115, 228.651, 90.00, 90.00, 90.00
R / Rfree (%) 20 / 24.1

Iodine Binding Sites:

The binding sites of Iodine atom in the Crystal Structure of Mutant S203A of Mouse Acetylcholinesterase Complexed with Butyrylthiocholine (pdb code 2ha7). This binding sites where shown within 5.0 Angstroms radius around Iodine atom.
In total 9 binding sites of Iodine where determined in the Crystal Structure of Mutant S203A of Mouse Acetylcholinesterase Complexed with Butyrylthiocholine, PDB code: 2ha7:
Jump to Iodine binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9;

Iodine binding site 1 out of 9 in 2ha7

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Iodine binding site 1 out of 9 in the Crystal Structure of Mutant S203A of Mouse Acetylcholinesterase Complexed with Butyrylthiocholine


Mono view


Stereo pair view

A full contact list of Iodine with other atoms in the I binding site number 1 of Crystal Structure of Mutant S203A of Mouse Acetylcholinesterase Complexed with Butyrylthiocholine within 5.0Å range:
probe atom residue distance (Å) B Occ
A:I900

b:70.7
occ:0.50
 O12 A:BCH910 2.8 92.1 1.0
C20 A:BCH910 3.3 91.6 1.0
N A:PHE295 3.5 46.9 1.0
C18 A:BCH910 3.7 92.4 1.0
CD2 A:PHE338 4.0 44.5 1.0
C19 A:BCH910 4.0 92.1 1.0
CA A:ILE294 4.1 49.4 1.0
CB A:ILE294 4.3 49.6 1.0
C A:ILE294 4.3 48.5 1.0
CA A:PHE295 4.3 45.3 1.0
C21 A:BCH910 4.3 91.4 1.0
CB A:TYR341 4.5 51.4 1.0
CE2 A:PHE338 4.5 43.9 1.0
CE1 A:PHE297 4.5 38.1 1.0
CG2 A:ILE294 4.6 50.3 1.0
N A:ARG296 4.9 44.2 1.0

Iodine binding site 2 out of 9 in 2ha7

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Iodine binding site 2 out of 9 in the Crystal Structure of Mutant S203A of Mouse Acetylcholinesterase Complexed with Butyrylthiocholine


Mono view


Stereo pair view

A full contact list of Iodine with other atoms in the I binding site number 2 of Crystal Structure of Mutant S203A of Mouse Acetylcholinesterase Complexed with Butyrylthiocholine within 5.0Å range:
probe atom residue distance (Å) B Occ
A:I902

b:57.5
occ:0.50
 NE A:ARG245 3.4 52.8 1.0
O A:ALA241 3.8 51.9 1.0
CD A:ARG245 3.8 54.0 1.0
C A:ALA241 3.9 52.0 1.0
CB A:ALA241 4.0 52.6 1.0
CB A:PRO162 4.1 57.1 1.0
N A:GLY242 4.2 53.2 1.0
CB A:ARG245 4.2 53.2 1.0
CA A:GLY242 4.3 54.3 1.0
O A:PRO162 4.4 61.8 1.0
CG A:PRO162 4.5 55.1 1.0
CZ A:ARG245 4.5 53.4 1.0
CA A:ALA241 4.6 51.4 1.0
CD A:PRO162 4.6 55.1 1.0
CG A:ARG245 4.7 53.3 1.0
NH2 A:ARG245 4.7 52.7 1.0

Iodine binding site 3 out of 9 in 2ha7

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Iodine binding site 3 out of 9 in the Crystal Structure of Mutant S203A of Mouse Acetylcholinesterase Complexed with Butyrylthiocholine


Mono view


Stereo pair view

A full contact list of Iodine with other atoms in the I binding site number 3 of Crystal Structure of Mutant S203A of Mouse Acetylcholinesterase Complexed with Butyrylthiocholine within 5.0Å range:
probe atom residue distance (Å) B Occ
A:I903

b:71.9
occ:0.50
 NE2 A:GLN291 2.8 61.6 1.0
OG A:SER293 3.3 53.4 1.0
N A:GLN291 3.6 56.7 1.0
CD A:PRO290 3.7 53.9 1.0
CB A:SER293 3.8 53.3 1.0
CG A:PRO290 3.8 55.0 1.0
CG A:ARG296 3.8 43.1 1.0
CB A:GLN291 3.9 57.7 1.0
O A:GLN291 4.0 56.4 1.0
CD A:GLN291 4.0 63.9 1.0
CB A:ARG296 4.1 43.5 1.0
CA A:GLN291 4.2 57.7 1.0
N A:PRO290 4.2 55.0 1.0
CG A:PRO368 4.2 51.5 1.0
CB A:PRO368 4.2 52.1 1.0
O A:HOH933 4.2 48.8 1.0
CD2 A:LEU289 4.3 49.6 1.0
C A:GLN291 4.4 57.2 1.0
CD A:ARG296 4.4 44.0 1.0
CB A:LEU289 4.4 51.5 1.0
CG A:GLN291 4.6 60.4 1.0
C A:PRO290 4.6 57.1 1.0
CB A:PRO290 4.8 57.0 1.0
C A:LEU289 4.8 54.2 1.0
CA A:PRO290 4.8 56.7 1.0
CG A:LEU289 4.8 50.5 1.0
NE A:ARG296 4.9 45.4 1.0
CA A:LEU289 5.0 52.6 1.0
OE1 A:GLN291 5.0 66.2 1.0
CD1 A:LEU289 5.0 48.3 1.0

Iodine binding site 4 out of 9 in 2ha7

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Iodine binding site 4 out of 9 in the Crystal Structure of Mutant S203A of Mouse Acetylcholinesterase Complexed with Butyrylthiocholine


Mono view


Stereo pair view

A full contact list of Iodine with other atoms in the I binding site number 4 of Crystal Structure of Mutant S203A of Mouse Acetylcholinesterase Complexed with Butyrylthiocholine within 5.0Å range:
probe atom residue distance (Å) B Occ
A:I907

b:66.1
occ:0.30
 OD2 A:ASP280 3.5 64.1 1.0
O A:VAL255 3.7 65.5 1.0
NE2 A:HIS284 3.8 54.3 1.0
CA A:VAL255 3.8 61.7 1.0
CG A:ASP280 4.0 60.5 1.0
C A:VAL255 4.0 64.5 1.0
CB A:VAL255 4.1 60.1 1.0
CB A:ASP280 4.2 56.3 1.0
CD2 A:HIS284 4.2 53.0 1.0
CG1 A:VAL255 4.4 57.0 1.0
O A:LEU254 4.4 60.6 1.0
CE1 A:HIS284 4.7 54.9 1.0
OD1 A:ASP280 4.8 61.5 1.0
N A:VAL255 5.0 60.9 1.0

Iodine binding site 5 out of 9 in 2ha7

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Iodine binding site 5 out of 9 in the Crystal Structure of Mutant S203A of Mouse Acetylcholinesterase Complexed with Butyrylthiocholine


Mono view


Stereo pair view

A full contact list of Iodine with other atoms in the I binding site number 5 of Crystal Structure of Mutant S203A of Mouse Acetylcholinesterase Complexed with Butyrylthiocholine within 5.0Å range:
probe atom residue distance (Å) B Occ
B:I904

b:65.6
occ:0.50
 NE B:ARG245 3.4 65.0 1.0
CD B:ARG245 3.7 66.5 1.0
O B:ALA241 3.9 59.9 1.0
C B:ALA241 4.0 59.5 1.0
CB B:PRO162 4.0 63.6 1.0
N B:GLY242 4.1 61.3 1.0
CB B:ARG245 4.1 64.3 1.0
CB B:ALA241 4.1 58.2 1.0
CG B:PRO162 4.2 62.4 1.0
CA B:GLY242 4.3 63.3 1.0
O B:PRO162 4.4 68.2 1.0
CD B:PRO162 4.5 63.0 1.0
CZ B:ARG245 4.6 66.0 1.0
CG B:ARG245 4.6 66.0 1.0
CA B:ALA241 4.7 57.4 1.0
NH1 B:ARG245 4.8 64.3 1.0

Iodine binding site 6 out of 9 in 2ha7

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Iodine binding site 6 out of 9 in the Crystal Structure of Mutant S203A of Mouse Acetylcholinesterase Complexed with Butyrylthiocholine


Mono view


Stereo pair view

A full contact list of Iodine with other atoms in the I binding site number 6 of Crystal Structure of Mutant S203A of Mouse Acetylcholinesterase Complexed with Butyrylthiocholine within 5.0Å range:
probe atom residue distance (Å) B Occ
B:I905

b:75.5
occ:0.50
 OG B:SER293 3.1 65.4 1.0
CB B:SER293 3.7 65.8 1.0
NE2 B:GLN291 3.8 74.2 1.0
CD B:PRO290 3.8 67.6 1.0
N B:GLN291 3.8 72.2 1.0
CB B:GLN291 3.9 72.7 1.0
O B:GLN291 3.9 71.8 1.0
CG B:PRO290 3.9 68.7 1.0
CG B:ARG296 3.9 56.5 1.0
CD2 B:LEU289 4.0 61.4 1.0
CB B:ARG296 4.1 56.0 1.0
CA B:GLN291 4.2 73.6 1.0
CB B:PRO368 4.2 64.3 1.0
O B:HOH937 4.2 51.6 1.0
CG B:PRO368 4.3 62.5 1.0
CB B:LEU289 4.3 65.7 1.0
CD B:ARG296 4.4 56.6 1.0
C B:GLN291 4.4 73.2 1.0
N B:PRO290 4.4 69.6 1.0
CG B:LEU289 4.6 63.2 1.0
CD B:GLN291 4.7 76.3 1.0
NE B:ARG296 4.8 59.0 1.0
C B:PRO290 4.9 73.2 1.0
CD1 B:LEU289 4.9 62.5 1.0
CG B:GLN291 4.9 75.5 1.0
C B:LEU289 4.9 69.4 1.0

Iodine binding site 7 out of 9 in 2ha7

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Iodine binding site 7 out of 9 in the Crystal Structure of Mutant S203A of Mouse Acetylcholinesterase Complexed with Butyrylthiocholine


Mono view


Stereo pair view

A full contact list of Iodine with other atoms in the I binding site number 7 of Crystal Structure of Mutant S203A of Mouse Acetylcholinesterase Complexed with Butyrylthiocholine within 5.0Å range:
probe atom residue distance (Å) B Occ
B:I906

b:62.0
occ:0.30
 NZ B:LYS332 3.6 69.5 1.0
CA B:GLY444 3.8 57.4 1.0
C B:GLY444 4.2 55.9 1.0
CD B:ARG433 4.2 62.5 1.0
CB B:ARG433 4.2 60.7 1.0
CG2 B:VAL445 4.2 52.0 1.0
N B:VAL445 4.5 54.0 1.0
CE B:LYS332 4.7 67.7 1.0
O B:GLY444 4.7 56.8 1.0
CG B:ARG433 4.9 61.6 1.0
OD1 B:ASP333 5.0 57.8 1.0

Iodine binding site 8 out of 9 in 2ha7

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Iodine binding site 8 out of 9 in the Crystal Structure of Mutant S203A of Mouse Acetylcholinesterase Complexed with Butyrylthiocholine


Mono view


Stereo pair view

A full contact list of Iodine with other atoms in the I binding site number 8 of Crystal Structure of Mutant S203A of Mouse Acetylcholinesterase Complexed with Butyrylthiocholine within 5.0Å range:
probe atom residue distance (Å) B Occ
B:I908

b:43.7
occ:0.50
 O B:HOH966 3.0 42.3 1.0
NZ B:LYS53 3.6 46.3 1.0
CE B:LYS53 3.8 47.9 1.0
CB B:TRP56 4.1 54.8 1.0
CD1 B:LEU60 4.2 55.3 1.0
CG B:TRP56 4.8 54.3 1.0
CD2 B:LEU60 4.8 52.0 1.0

Iodine binding site 9 out of 9 in 2ha7

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Iodine binding site 9 out of 9 in the Crystal Structure of Mutant S203A of Mouse Acetylcholinesterase Complexed with Butyrylthiocholine


Mono view


Stereo pair view

A full contact list of Iodine with other atoms in the I binding site number 9 of Crystal Structure of Mutant S203A of Mouse Acetylcholinesterase Complexed with Butyrylthiocholine within 5.0Å range:
probe atom residue distance (Å) B Occ
B:I909

b:65.5
occ:0.30
 N B:PHE295 3.2 57.1 1.0
CD2 B:PHE338 3.8 55.3 1.0
CA B:ILE294 4.0 61.8 1.0
CA B:PHE295 4.0 54.8 1.0
C B:ILE294 4.1 59.1 1.0
CB B:ILE294 4.2 62.5 1.0
CE2 B:PHE338 4.5 54.7 1.0
CB B:TYR341 4.5 63.8 1.0
CE1 B:PHE297 4.5 50.6 1.0
N B:ARG296 4.6 54.8 1.0
CG2 B:ILE294 4.7 64.7 1.0
CG B:PHE338 4.9 56.5 1.0
C B:PHE295 4.9 54.6 1.0
CB B:PHE338 4.9 57.9 1.0

Reference:

Y.Bourne, Z.Radic, G.Sulzenbacher, E.Kim, P.Taylor, P.Marchot. Substrate and Product Trafficking Through the Active Center Gorge of Acetylcholinesterase Analyzed By Crystallography and Equilibrium Binding J.Biol.Chem. V. 281 29256 2006.
ISSN: ISSN 0021-9258
PubMed: 16837465
DOI: 10.1074/JBC.M603018200
Page generated: Sun Aug 11 13:56:00 2024

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