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Chlorine in PDB 1vqq: Structure of Penicillin Binding Protein 2A From Methicillin Resistant Staphylococcus Aureus Strain 27R at 1.80 A Resolution.

Protein crystallography data

The structure of Structure of Penicillin Binding Protein 2A From Methicillin Resistant Staphylococcus Aureus Strain 27R at 1.80 A Resolution., PDB code: 1vqq was solved by D.Lim, N.C.J.Strynadka, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 24.92 / 1.80
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 80.869, 100.608, 186.235, 90.00, 90.00, 90.00
R / Rfree (%) 23.7 / 27.4

Other elements in 1vqq:

The structure of Structure of Penicillin Binding Protein 2A From Methicillin Resistant Staphylococcus Aureus Strain 27R at 1.80 A Resolution. also contains other interesting chemical elements:

Cadmium (Cd) 7 atoms

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Structure of Penicillin Binding Protein 2A From Methicillin Resistant Staphylococcus Aureus Strain 27R at 1.80 A Resolution. (pdb code 1vqq). 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 Penicillin Binding Protein 2A From Methicillin Resistant Staphylococcus Aureus Strain 27R at 1.80 A Resolution., PDB code: 1vqq:
Jump to Chlorine binding site number: 1; 2; 3; 4;

Chlorine binding site 1 out of 4 in 1vqq

Go back to Chlorine Binding Sites List in 1vqq
Chlorine binding site 1 out of 4 in the Structure of Penicillin Binding Protein 2A From Methicillin Resistant Staphylococcus Aureus Strain 27R at 1.80 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 Penicillin Binding Protein 2A From Methicillin Resistant Staphylococcus Aureus Strain 27R at 1.80 A Resolution. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl1009

b:27.6
occ:1.00
CD B:CD1001 2.5 25.3 1.0
OG1 A:THR300 3.1 21.4 1.0
CG A:GLU145 3.6 28.1 1.0
OE1 A:GLU145 3.6 24.5 1.0
O A:HOH1133 3.6 20.0 1.0
OE2 B:GLU145 3.8 23.2 1.0
CD1 A:ILE309 3.9 29.7 1.0
CD A:GLU145 4.0 26.1 1.0
CG2 A:VAL302 4.0 25.6 1.0
ND1 A:HIS143 4.0 26.4 1.0
CG1 A:ILE309 4.0 29.9 1.0
CB A:HIS143 4.0 23.4 1.0
CB A:THR300 4.0 22.4 1.0
CG2 A:THR300 4.1 20.7 1.0
CG A:HIS143 4.4 24.9 1.0
O B:HOH1147 4.6 29.7 1.0
CD B:GLU145 4.7 24.6 1.0
OE1 B:GLU145 4.8 20.1 1.0
CB A:GLU145 5.0 26.2 1.0

Chlorine binding site 2 out of 4 in 1vqq

Go back to Chlorine Binding Sites List in 1vqq
Chlorine binding site 2 out of 4 in the Structure of Penicillin Binding Protein 2A From Methicillin Resistant Staphylococcus Aureus Strain 27R at 1.80 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 Penicillin Binding Protein 2A From Methicillin Resistant Staphylococcus Aureus Strain 27R at 1.80 A Resolution. within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl1008

b:27.0
occ:1.00
CD B:CD1002 2.5 24.2 1.0
OG1 B:THR300 3.1 21.3 1.0
O B:HOH1090 3.4 35.2 1.0
OE1 B:GLU145 3.6 20.1 1.0
CG B:GLU145 3.6 25.4 1.0
OE2 A:GLU145 3.6 25.8 1.0
O A:HOH1134 3.7 22.7 1.0
CD1 B:ILE309 3.8 34.1 1.0
CG2 B:VAL302 3.9 27.0 1.0
ND1 B:HIS143 3.9 25.4 1.0
CB B:HIS143 3.9 21.0 1.0
CD B:GLU145 4.0 24.6 1.0
CG1 B:ILE309 4.0 29.5 1.0
CG2 B:THR300 4.1 24.7 1.0
CB B:THR300 4.1 22.4 1.0
CG B:HIS143 4.3 23.5 1.0
CD A:GLU145 4.6 26.1 1.0
OE1 A:GLU145 4.8 24.5 1.0
CE1 B:HIS143 5.0 20.9 1.0
CB B:GLU145 5.0 24.4 1.0

Chlorine binding site 3 out of 4 in 1vqq

Go back to Chlorine Binding Sites List in 1vqq
Chlorine binding site 3 out of 4 in the Structure of Penicillin Binding Protein 2A From Methicillin Resistant Staphylococcus Aureus Strain 27R at 1.80 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 Penicillin Binding Protein 2A From Methicillin Resistant Staphylococcus Aureus Strain 27R at 1.80 A Resolution. within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl1010

b:29.6
occ:1.00
CD B:CD1003 2.4 27.1 1.0
O A:HOH1169 3.2 29.6 1.0
CD B:GLN137 3.4 39.3 1.0
NE2 B:GLN140 3.4 28.0 1.0
CG B:GLN137 3.5 35.9 1.0
CG A:GLN207 3.6 36.5 1.0
NE2 B:HIS311 3.6 30.5 1.0
NE2 B:GLN137 3.6 38.1 1.0
O B:GLY135 3.7 29.1 1.0
OD2 A:ASP209 3.7 30.3 1.0
CB B:ALA310 3.8 25.2 1.0
OE1 B:GLN137 3.8 41.2 1.0
CB A:GLN207 4.0 32.2 1.0
CD2 B:HIS311 4.1 27.7 1.0
CD B:GLN140 4.3 27.3 1.0
OE1 B:GLN140 4.4 26.5 1.0
CE1 B:HIS311 4.6 25.4 1.0
CG A:ASP209 4.6 33.2 1.0
OD1 A:ASP209 4.6 32.9 1.0
OG1 A:THR210 4.7 29.9 1.0
CB B:GLN137 4.7 31.3 1.0
CD A:GLN207 4.8 41.2 1.0
C B:GLY135 4.9 26.2 1.0
CA B:ALA310 5.0 24.3 1.0

Chlorine binding site 4 out of 4 in 1vqq

Go back to Chlorine Binding Sites List in 1vqq
Chlorine binding site 4 out of 4 in the Structure of Penicillin Binding Protein 2A From Methicillin Resistant Staphylococcus Aureus Strain 27R at 1.80 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 Penicillin Binding Protein 2A From Methicillin Resistant Staphylococcus Aureus Strain 27R at 1.80 A Resolution. within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl1011

b:27.5
occ:1.00
CD A:CD1005 2.5 27.1 1.0
O B:HOH1103 3.2 28.0 1.0
CG B:GLN207 3.4 30.8 1.0
NE2 A:GLN137 3.5 36.2 1.0
NE2 A:GLN140 3.5 27.7 1.0
NE2 A:HIS311 3.5 26.1 1.0
O A:HOH1132 3.6 26.8 1.0
CD A:GLN137 3.6 38.6 1.0
CG A:GLN137 3.8 38.1 1.0
O A:GLY135 3.8 27.0 1.0
CB A:ALA310 3.9 24.9 1.0
OD1 B:ASP209 3.9 31.2 1.0
CB B:GLN207 4.0 27.2 1.0
CD2 A:HIS311 4.0 21.8 1.0
OE1 A:GLN137 4.2 39.4 1.0
O B:HOH1233 4.4 39.8 1.0
CD A:GLN140 4.5 29.0 1.0
CE1 A:HIS311 4.5 20.9 1.0
OE1 A:GLN140 4.5 27.8 1.0
CD B:GLN207 4.6 35.2 1.0
CG B:ASP209 4.8 29.4 1.0
OG1 B:THR210 4.8 29.9 1.0
OD2 B:ASP209 4.9 26.4 1.0
CB A:GLN137 4.9 30.8 1.0
CA A:ALA310 5.0 27.0 1.0

Reference:

D.Lim, N.C.J.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 20:05:59 2025

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