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Samarium in PDB 2anx: Crystal Structure of Bacteriophage P22 Lysozyme Mutant L87M

Enzymatic activity of Crystal Structure of Bacteriophage P22 Lysozyme Mutant L87M

All present enzymatic activity of Crystal Structure of Bacteriophage P22 Lysozyme Mutant L87M:
3.2.1.17;

Protein crystallography data

The structure of Crystal Structure of Bacteriophage P22 Lysozyme Mutant L87M, PDB code: 2anx was solved by B.H.Mooers, B.W.Matthews, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 42.00 / 1.04
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 134.013, 50.415, 46.587, 90.00, 103.80, 90.00
R / Rfree (%) 11.7 / 15

Other elements in 2anx:

The structure of Crystal Structure of Bacteriophage P22 Lysozyme Mutant L87M also contains other interesting chemical elements:

Magnesium (Mg) 1 atom
Iodine (I) 9 atoms

Samarium Binding Sites:

The binding sites of Samarium atom in the Crystal Structure of Bacteriophage P22 Lysozyme Mutant L87M (pdb code 2anx). This binding sites where shown within 5.0 Angstroms radius around Samarium atom.
In total 3 binding sites of Samarium where determined in the Crystal Structure of Bacteriophage P22 Lysozyme Mutant L87M, PDB code: 2anx:
Jump to Samarium binding site number: 1; 2; 3;

Samarium binding site 1 out of 3 in 2anx

Go back to Samarium Binding Sites List in 2anx
Samarium binding site 1 out of 3 in the Crystal Structure of Bacteriophage P22 Lysozyme Mutant L87M


Mono view


Stereo pair view

A full contact list of Samarium with other atoms in the Sm binding site number 1 of Crystal Structure of Bacteriophage P22 Lysozyme Mutant L87M within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Sm2802

b:10.9
occ:0.33
O A:HOH4209 2.3 22.1 0.5
OE1 A:GLU58 2.3 21.2 1.0
OE1 A:GLU54 2.4 16.1 1.0
OE2 A:GLU58 2.6 25.5 1.0
CD A:GLU58 2.8 22.0 1.0
CD A:GLU54 3.4 14.4 1.0
CG A:GLU54 4.0 13.1 1.0
CG A:GLU58 4.3 18.5 1.0
OE2 A:GLU54 4.4 16.7 1.0
O A:HOH4683 4.4 49.5 1.0
N B:MET1 4.5 22.4 1.0
O A:HOH3129 4.7 20.9 0.5
O A:HOH2945 4.8 29.4 1.0
O A:HOH3257 4.9 32.7 1.0
O A:HOH3129 4.9 12.2 0.5

Samarium binding site 2 out of 3 in 2anx

Go back to Samarium Binding Sites List in 2anx
Samarium binding site 2 out of 3 in the Crystal Structure of Bacteriophage P22 Lysozyme Mutant L87M


Mono view


Stereo pair view

A full contact list of Samarium with other atoms in the Sm binding site number 2 of Crystal Structure of Bacteriophage P22 Lysozyme Mutant L87M within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Sm2801

b:10.8
occ:0.51
OE1 B:GLN65 2.2 24.8 1.0
O B:HOH3152 2.3 22.1 1.0
O B:HOH3726 2.5 17.6 0.5
O B:HOH3151 2.8 24.5 1.0
O B:HOH3150 2.8 15.9 1.0
CD B:GLN65 3.3 26.7 1.0
CG B:GLN65 4.1 20.3 1.0
NE2 B:GLN65 4.2 23.8 1.0
CB B:GLN65 4.2 18.1 1.0
O B:HOH3791 4.5 34.7 1.0
OD1 B:ASP69 4.5 18.7 1.0
O B:HOH3548 4.6 22.6 1.0
OD2 B:ASP69 4.6 19.3 1.0
O B:HOH4210 4.9 41.9 1.0

Samarium binding site 3 out of 3 in 2anx

Go back to Samarium Binding Sites List in 2anx
Samarium binding site 3 out of 3 in the Crystal Structure of Bacteriophage P22 Lysozyme Mutant L87M


Mono view


Stereo pair view

A full contact list of Samarium with other atoms in the Sm binding site number 3 of Crystal Structure of Bacteriophage P22 Lysozyme Mutant L87M within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Sm2803

b:7.1
occ:0.92
OD1 B:ASP131 2.2 10.3 1.0
O B:HOH3321 2.3 11.1 1.0
O B:HOH3132 2.3 11.9 1.0
OD1 B:ASP129 2.3 10.2 1.0
OD2 B:ASP129 2.5 9.8 1.0
CG B:ASP129 2.8 9.0 1.0
CG B:ASP131 3.3 10.0 1.0
OD2 B:ASP131 3.7 12.7 1.0
CB B:ASP129 4.3 9.6 1.0
O B:HOH3233 4.3 15.9 0.5
N B:ILE132 4.4 9.0 1.0
O B:HOH2982 4.4 15.7 1.0
N B:ASP131 4.4 9.5 1.0
C B:ASP131 4.5 8.9 1.0
CB B:ASP131 4.5 10.4 1.0
CA B:ILE132 4.7 8.9 1.0
CA B:ASP131 4.7 9.7 1.0
CD B:PRO130 4.9 11.8 1.0
O B:ASP131 4.9 9.5 1.0
CB B:ILE132 4.9 10.0 1.0
CA B:ASP129 5.0 10.3 1.0

Reference:

B.H.Mooers, B.W.Matthews. Extension to 2268 Atoms of Direct Methods in the Ab Initio Determination of the Unknown Structure of Bacteriophage P22 Lysozyme. Acta Crystallogr.,Sect.D V. 62 165 2006.
ISSN: ISSN 0907-4449
PubMed: 16421448
DOI: 10.1107/S0907444905037212
Page generated: Wed Dec 16 02:09:51 2020

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