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Chlorine in PDB 1fcm: Crystal Structure of the E.Coli Ampc Beta-Lactamase Mutant Q120L/Y150E Covalently Acylated with the Inhibitory Beta-Lactam, Cloxacillin

Enzymatic activity of Crystal Structure of the E.Coli Ampc Beta-Lactamase Mutant Q120L/Y150E Covalently Acylated with the Inhibitory Beta-Lactam, Cloxacillin

All present enzymatic activity of Crystal Structure of the E.Coli Ampc Beta-Lactamase Mutant Q120L/Y150E Covalently Acylated with the Inhibitory Beta-Lactam, Cloxacillin:
3.5.2.6;

Protein crystallography data

The structure of Crystal Structure of the E.Coli Ampc Beta-Lactamase Mutant Q120L/Y150E Covalently Acylated with the Inhibitory Beta-Lactam, Cloxacillin, PDB code: 1fcm was solved by A.Patera, L.C.Blaszczak, B.K.Shoichet, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 2.46
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 118.520, 76.190, 98.280, 90.00, 116.68, 90.00
R / Rfree (%) 20.7 / 26.5

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of the E.Coli Ampc Beta-Lactamase Mutant Q120L/Y150E Covalently Acylated with the Inhibitory Beta-Lactam, Cloxacillin (pdb code 1fcm). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Crystal Structure of the E.Coli Ampc Beta-Lactamase Mutant Q120L/Y150E Covalently Acylated with the Inhibitory Beta-Lactam, Cloxacillin, PDB code: 1fcm:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in 1fcm

Go back to Chlorine Binding Sites List in 1fcm
Chlorine binding site 1 out of 2 in the Crystal Structure of the E.Coli Ampc Beta-Lactamase Mutant Q120L/Y150E Covalently Acylated with the Inhibitory Beta-Lactam, Cloxacillin


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 the E.Coli Ampc Beta-Lactamase Mutant Q120L/Y150E Covalently Acylated with the Inhibitory Beta-Lactam, Cloxacillin within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl961

b:57.9
occ:1.00
CL A:CXU961 0.0 57.9 1.0
C29 A:CXU961 1.8 53.1 1.0
C30 A:CXU961 2.8 53.6 1.0
C28 A:CXU961 2.8 51.9 1.0
C26 A:CXU961 3.1 49.9 1.0
C22 A:CXU961 3.5 47.8 1.0
CD1 A:LEU117 3.7 23.4 1.0
C21 A:CXU961 3.7 46.8 1.0
N2 A:CXU961 3.8 45.4 1.0
N25 A:CXU961 3.9 49.6 1.0
CD2 A:LEU117 3.9 23.4 1.0
CD2 A:LEU116 4.0 32.6 1.0
S4 A:CXU961 4.0 49.2 1.0
C31 A:CXU961 4.1 54.6 1.0
C33 A:CXU961 4.1 52.5 1.0
CG A:LEU117 4.1 24.4 1.0
C23 A:CXU961 4.4 47.7 1.0
O21 A:CXU961 4.5 46.4 1.0
C32 A:CXU961 4.6 54.3 1.0
O24 A:CXU961 4.6 49.1 1.0
CG A:LEU116 4.8 30.8 1.0
C2 A:CXU961 4.9 43.9 1.0

Chlorine binding site 2 out of 2 in 1fcm

Go back to Chlorine Binding Sites List in 1fcm
Chlorine binding site 2 out of 2 in the Crystal Structure of the E.Coli Ampc Beta-Lactamase Mutant Q120L/Y150E Covalently Acylated with the Inhibitory Beta-Lactam, Cloxacillin


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 the E.Coli Ampc Beta-Lactamase Mutant Q120L/Y150E Covalently Acylated with the Inhibitory Beta-Lactam, Cloxacillin within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl961

b:51.8
occ:1.00
CL B:CXU961 0.0 51.8 1.0
C29 B:CXU961 1.8 43.0 1.0
C30 B:CXU961 2.7 42.3 1.0
C28 B:CXU961 2.8 42.7 1.0
C26 B:CXU961 3.1 40.9 1.0
N2 B:CXU961 3.4 34.3 1.0
CD2 B:LEU117 3.4 26.6 1.0
C22 B:CXU961 3.5 39.3 1.0
C21 B:CXU961 3.5 37.6 1.0
S4 B:CXU961 3.8 26.4 1.0
CG B:LEU117 3.9 26.0 1.0
CD1 B:LEU117 3.9 24.9 1.0
C31 B:CXU961 4.0 43.7 1.0
N25 B:CXU961 4.1 40.5 1.0
C33 B:CXU961 4.1 41.6 1.0
CD2 B:LEU116 4.2 18.0 1.0
O21 B:CXU961 4.3 37.4 1.0
CG B:LEU116 4.4 22.8 1.0
C2 B:CXU961 4.4 29.0 1.0
C23 B:CXU961 4.5 40.1 1.0
C32 B:CXU961 4.6 43.4 1.0
C3 B:CXU961 4.7 29.1 1.0
O24 B:CXU961 4.8 41.3 1.0
CD1 B:LEU116 4.9 18.7 1.0

Reference:

A.Patera, L.C.Blaszczak, B.K.Shoichet. Crystal Structures of Substrate and Inhibitor Complexes with Ampc -Lactamase: Possible Implications For Substrate-Assisted Catalysis J.Am.Chem.Soc. V. 122 10504 2000.
ISSN: ISSN 0002-7863
DOI: 10.1021/JA001676X
Page generated: Thu Jul 10 16:52:12 2025

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