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Chlorine in PDB 1fcn: Crystal Structure of the E. Coli Ampc Beta-Lactamase Mutant Q120L/Y150E Covalently Acylated with the Substrate Beta-Lactam Loracarbef

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

All present enzymatic activity of Crystal Structure of the E. Coli Ampc Beta-Lactamase Mutant Q120L/Y150E Covalently Acylated with the Substrate Beta-Lactam Loracarbef:
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 Substrate Beta-Lactam Loracarbef, PDB code: 1fcn 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) 8.00 / 2.35
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 119.360, 76.264, 98.355, 90.00, 116.00, 90.00
R / Rfree (%) 20.8 / 25.7

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 Substrate Beta-Lactam Loracarbef (pdb code 1fcn). 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 Substrate Beta-Lactam Loracarbef, PDB code: 1fcn:
Jump to Chlorine binding site number: 1; 2;

Chlorine binding site 1 out of 2 in 1fcn

Go back to Chlorine Binding Sites List in 1fcn
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 Substrate Beta-Lactam Loracarbef


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 Substrate Beta-Lactam Loracarbef within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl961

b:51.4
occ:1.00
CL A:LOR961 0.0 51.4 1.0
C6 A:LOR961 1.7 49.3 1.0
C7 A:LOR961 2.9 48.6 1.0
C5 A:LOR961 3.0 47.8 1.0
C8 A:LOR961 3.4 49.4 1.0
O82 A:LOR961 3.7 50.0 1.0
N8 A:LOR961 4.2 46.1 1.0
C4 A:LOR961 4.3 44.8 1.0
O81 A:LOR961 4.3 49.5 1.0
CD2 A:LEU116 4.8 34.7 1.0
C3 A:LOR961 4.8 41.5 1.0

Chlorine binding site 2 out of 2 in 1fcn

Go back to Chlorine Binding Sites List in 1fcn
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 Substrate Beta-Lactam Loracarbef


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 Substrate Beta-Lactam Loracarbef within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Cl961

b:36.9
occ:1.00
CL B:LOR961 0.0 36.9 1.0
C6 B:LOR961 1.7 33.2 1.0
C7 B:LOR961 2.8 32.7 1.0
C5 B:LOR961 2.9 35.2 1.0
O82 B:LOR961 3.2 32.5 1.0
C8 B:LOR961 3.3 32.0 1.0
OD1 B:ASN286 3.4 29.2 1.0
C26 B:LOR961 3.7 36.1 1.0
CD1 B:LEU290 3.9 27.3 1.0
N8 B:LOR961 4.1 29.5 1.0
C4 B:LOR961 4.2 33.1 1.0
C27 B:LOR961 4.2 35.0 1.0
C25 B:LOR961 4.3 35.4 1.0
O81 B:LOR961 4.3 33.0 1.0
CG B:ASN286 4.4 28.9 1.0
C3 B:LOR961 4.7 30.1 1.0
CD2 B:LEU116 4.8 20.0 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: Fri Jul 19 21:57:43 2024

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