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Chlorine in PDB 2anv: Crystal Structure of P22 Lysozyme Mutant L86M

Enzymatic activity of Crystal Structure of P22 Lysozyme Mutant L86M

All present enzymatic activity of Crystal Structure of P22 Lysozyme Mutant L86M:
3.2.1.17;

Protein crystallography data

The structure of Crystal Structure of P22 Lysozyme Mutant L86M, PDB code: 2anv 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 (%) 12.2 / 15.1

Other elements in 2anv:

The structure of Crystal Structure of P22 Lysozyme Mutant L86M also contains other interesting chemical elements:

Magnesium (Mg) 1 atom
Samarium (Sm) 3 atoms
Iodine (I) 6 atoms

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of P22 Lysozyme Mutant L86M (pdb code 2anv). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 3 binding sites of Chlorine where determined in the Crystal Structure of P22 Lysozyme Mutant L86M, PDB code: 2anv:
Jump to Chlorine binding site number: 1; 2; 3;

Chlorine binding site 1 out of 3 in 2anv

Go back to Chlorine Binding Sites List in 2anv
Chlorine binding site 1 out of 3 in the Crystal Structure of P22 Lysozyme Mutant L86M


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure of P22 Lysozyme Mutant L86M within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl2991

b:28.1
occ:0.50
CL A:CL2991 0.0 28.1 0.5
CL A:CL2991 2.2 28.2 0.5
N A:ASP41 3.1 13.5 1.0
NZ A:LYS55 3.4 28.7 1.0
CA A:VAL40 3.9 12.9 1.0
OD1 A:ASP41 3.9 35.3 1.0
C A:VAL40 3.9 13.8 1.0
CD2 A:LEU59 4.0 12.9 1.0
CA A:ASP41 4.0 15.0 1.0
O A:HOH3224 4.3 25.4 1.0
CG1 A:VAL40 4.3 16.6 1.0
O A:LYS39 4.4 11.4 0.5
O A:LYS39 4.4 11.3 0.5
CE A:LYS55 4.4 27.6 1.0
CG A:ASP41 4.6 23.8 1.0
CD A:LYS55 4.6 17.6 1.0
CB A:VAL40 4.7 13.8 1.0
N A:VAL40 4.8 12.9 1.0
CB A:ASP41 4.9 21.2 1.0
C A:LYS39 5.0 12.2 0.5
C A:LYS39 5.0 13.3 0.5

Chlorine binding site 2 out of 3 in 2anv

Go back to Chlorine Binding Sites List in 2anv
Chlorine binding site 2 out of 3 in the Crystal Structure of P22 Lysozyme Mutant L86M


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Crystal Structure of P22 Lysozyme Mutant L86M within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl2991

b:28.2
occ:0.50
CL A:CL2991 0.0 28.2 0.5
CL A:CL2991 2.2 28.1 0.5
O A:HOH3224 2.7 25.4 1.0
O A:LYS39 2.8 11.4 0.5
O A:LYS39 2.9 11.3 0.5
CD2 A:LEU59 3.5 12.9 1.0
O A:HOH3967 3.7 45.5 1.0
C A:LYS39 3.7 12.2 0.5
C A:LYS39 3.8 13.3 0.5
CA A:VAL40 3.8 12.9 1.0
N A:ASP41 4.1 13.5 1.0
N A:VAL40 4.2 12.9 1.0
NE2 A:HIS36 4.4 12.2 1.0
C A:VAL40 4.4 13.8 1.0
CE1 A:HIS36 4.6 12.1 1.0
CB A:VAL40 4.8 13.8 1.0
O A:HOH3173 4.9 20.2 1.0
CA A:LYS39 4.9 13.8 0.5
CG2 A:VAL40 4.9 13.4 1.0
CG A:LEU59 5.0 10.0 1.0
CG1 A:VAL40 5.0 16.6 1.0

Chlorine binding site 3 out of 3 in 2anv

Go back to Chlorine Binding Sites List in 2anv
Chlorine binding site 3 out of 3 in the Crystal Structure of P22 Lysozyme Mutant L86M


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Crystal Structure of P22 Lysozyme Mutant L86M within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl2993

b:19.5
occ:0.33
O B:HOH3506 2.8 37.2 1.0
CB B:LYS55 3.6 10.4 0.7
N B:THR52 3.6 12.8 1.0
CG B:LYS55 3.8 12.0 0.7
CA B:ILE51 3.9 13.5 1.0
OG1 B:THR52 4.0 14.6 1.0
CB B:ILE51 4.0 13.1 1.0
O B:HOH3914 4.1 79.3 1.0
CG2 B:THR52 4.2 19.6 1.0
CG2 B:ILE51 4.2 15.9 1.0
C B:ILE51 4.3 13.2 1.0
CE B:LYS55 4.5 28.0 0.7
CB B:THR52 4.5 14.4 1.0
O B:THR50 4.7 22.8 1.0
CA B:THR52 4.7 13.5 1.0
CD B:LYS55 4.7 19.2 0.7

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: Thu Jul 10 21:11:04 2025

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