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Chlorine in PDB 1mwr: Structure of Semet Penicillin Binding Protein 2A From Methicillin Resistant Staphylococcus Aureus Strain 27R (Trigonal Form) at 2.45 A Resolution.

Protein crystallography data

The structure of Structure of Semet Penicillin Binding Protein 2A From Methicillin Resistant Staphylococcus Aureus Strain 27R (Trigonal Form) at 2.45 A Resolution., PDB code: 1mwr was solved by D.C.Lim, N.C.J.Strynadka, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 24.89 / 2.45
Space group P 31 2 1
Cell size a, b, c (Å), α, β, γ (°) 141.060, 141.060, 146.671, 90.00, 90.00, 120.00
R / Rfree (%) 27 / 32.4

Other elements in 1mwr:

The structure of Structure of Semet Penicillin Binding Protein 2A From Methicillin Resistant Staphylococcus Aureus Strain 27R (Trigonal Form) at 2.45 A Resolution. also contains other interesting chemical elements:

Cadmium (Cd) 4 atoms

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Structure of Semet Penicillin Binding Protein 2A From Methicillin Resistant Staphylococcus Aureus Strain 27R (Trigonal Form) at 2.45 A Resolution. (pdb code 1mwr). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 4 binding sites of Chlorine where determined in the Structure of Semet Penicillin Binding Protein 2A From Methicillin Resistant Staphylococcus Aureus Strain 27R (Trigonal Form) at 2.45 A Resolution., PDB code: 1mwr:
Jump to Chlorine binding site number: 1; 2; 3; 4;

Chlorine binding site 1 out of 4 in 1mwr

Go back to Chlorine Binding Sites List in 1mwr
Chlorine binding site 1 out of 4 in the Structure of Semet Penicillin Binding Protein 2A From Methicillin Resistant Staphylococcus Aureus Strain 27R (Trigonal Form) at 2.45 A Resolution.


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Structure of Semet Penicillin Binding Protein 2A From Methicillin Resistant Staphylococcus Aureus Strain 27R (Trigonal Form) at 2.45 A Resolution. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl1205

b:16.4
occ:1.00
CD A:CD1202 2.6 17.4 1.0
CD A:GLN137 3.3 19.7 1.0
NE2 A:GLN137 3.3 17.6 1.0
NE2 A:GLN140 3.4 18.8 1.0
O A:GLY135 3.7 10.4 1.0
OE1 A:GLN137 3.7 18.3 1.0
CG A:GLN137 3.7 20.5 1.0
NE2 A:HIS311 3.8 12.1 1.0
CG B:GLN207 3.8 26.4 1.0
CB A:ALA310 3.9 11.8 1.0
OD1 B:ASP209 3.9 2.4 1.0
CD2 A:HIS311 4.2 7.4 1.0
CB B:GLN207 4.3 23.7 1.0
CD A:GLN140 4.4 17.2 1.0
OE1 A:GLN140 4.5 17.0 1.0
OD2 B:ASP209 4.7 5.7 1.0
CE1 A:HIS311 4.7 7.1 1.0
CB A:GLN137 4.7 19.8 1.0
CG B:ASP209 4.8 9.1 1.0
OG1 B:THR210 4.8 19.7 1.0
C A:GLY135 4.9 14.4 1.0
CD B:GLN207 4.9 27.5 1.0

Chlorine binding site 2 out of 4 in 1mwr

Go back to Chlorine Binding Sites List in 1mwr
Chlorine binding site 2 out of 4 in the Structure of Semet Penicillin Binding Protein 2A From Methicillin Resistant Staphylococcus Aureus Strain 27R (Trigonal Form) at 2.45 A Resolution.


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 2 of Structure of Semet Penicillin Binding Protein 2A From Methicillin Resistant Staphylococcus Aureus Strain 27R (Trigonal Form) at 2.45 A Resolution. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl1207

b:15.7
occ:1.00
OE1 A:GLU145 2.1 1.7 1.0
OG1 A:THR300 3.0 7.7 1.0
CD A:GLU145 3.1 3.4 1.0
CG2 A:VAL302 3.7 15.6 1.0
CG1 A:ILE309 3.8 18.8 1.0
CG A:GLU145 3.8 17.0 1.0
CD1 A:ILE309 3.8 16.7 1.0
OE2 A:GLU145 3.9 1.7 1.0
CB A:GLU145 4.1 15.8 1.0
CB A:THR300 4.1 9.7 1.0
ND1 A:HIS143 4.2 22.8 1.0
OE1 B:GLU145 4.2 17.4 1.0
CG2 A:THR300 4.2 10.2 1.0
CB A:HIS143 4.2 17.3 1.0
CG A:HIS143 4.7 20.0 1.0

Chlorine binding site 3 out of 4 in 1mwr

Go back to Chlorine Binding Sites List in 1mwr
Chlorine binding site 3 out of 4 in the Structure of Semet Penicillin Binding Protein 2A From Methicillin Resistant Staphylococcus Aureus Strain 27R (Trigonal Form) at 2.45 A Resolution.


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 3 of Structure of Semet Penicillin Binding Protein 2A From Methicillin Resistant Staphylococcus Aureus Strain 27R (Trigonal Form) at 2.45 A Resolution. within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl1206

b:24.5
occ:1.00
CD A:CD1203 2.5 21.4 1.0
NE2 B:HIS311 3.4 22.6 1.0
NE2 B:GLN140 3.4 14.8 1.0
NE2 B:GLN137 3.5 31.0 1.0
O B:GLY135 3.6 15.5 1.0
CD B:GLN137 3.7 29.4 1.0
CB B:ALA310 3.8 22.5 1.0
CD2 B:HIS311 3.8 20.2 1.0
OE1 B:GLN137 3.9 29.7 1.0
OD1 A:ASP209 3.9 26.0 1.0
CG A:GLN207 4.0 38.9 1.0
CB A:GLN207 4.3 36.1 1.0
CD B:GLN140 4.3 16.0 1.0
OE1 B:GLN140 4.3 17.6 1.0
CE1 B:HIS311 4.5 21.6 1.0
CG B:GLN137 4.6 27.1 1.0
OD2 A:ASP209 4.8 24.6 1.0
CG A:ASP209 4.8 26.4 1.0
CD A:GLN207 4.8 42.0 1.0
C B:GLY135 4.9 16.7 1.0
CA B:ALA310 4.9 22.6 1.0
OG1 A:THR210 4.9 28.1 1.0

Chlorine binding site 4 out of 4 in 1mwr

Go back to Chlorine Binding Sites List in 1mwr
Chlorine binding site 4 out of 4 in the Structure of Semet Penicillin Binding Protein 2A From Methicillin Resistant Staphylococcus Aureus Strain 27R (Trigonal Form) at 2.45 A Resolution.


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 4 of Structure of Semet Penicillin Binding Protein 2A From Methicillin Resistant Staphylococcus Aureus Strain 27R (Trigonal Form) at 2.45 A Resolution. within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl1208

b:10.4
occ:1.00
CD B:CD1201 2.4 20.0 1.0
NH2 B:ARG298 2.9 18.5 1.0
OE2 B:GLU145 3.0 12.1 1.0
OG1 B:THR300 3.6 17.5 1.0
CG B:GLU145 3.6 14.3 1.0
CD B:GLU145 3.6 16.4 1.0
ND1 B:HIS143 3.9 18.0 1.0
CZ B:ARG298 4.0 24.3 1.0
CB B:HIS143 4.0 15.5 1.0
CG2 B:VAL302 4.1 14.1 1.0
NE B:ARG298 4.2 25.3 1.0
CG1 B:ILE309 4.3 23.3 1.0
CG B:HIS143 4.3 17.3 1.0
CD1 B:ILE309 4.3 17.4 1.0
OE1 B:GLU145 4.7 17.4 1.0
CB B:THR300 4.9 19.1 1.0
CG A:GLU145 4.9 17.0 1.0
CE1 B:HIS143 4.9 17.4 1.0
OE2 A:GLU145 5.0 1.7 1.0

Reference:

D.Lim, N.C.Strynadka. Structural Basis For the Beta Lactam Resistance of PBP2A From Methicillin-Resistant Staphylococcus Aureus. Nat.Struct.Biol. V. 9 870 2002.
ISSN: ISSN 1072-8368
PubMed: 12389036
Page generated: Thu Jul 10 18:16:10 2025

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