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Chlorine in PDB 6z21: Crystal Structure of Deacylation Mutant Kpc-2 (E166Q)

Enzymatic activity of Crystal Structure of Deacylation Mutant Kpc-2 (E166Q)

All present enzymatic activity of Crystal Structure of Deacylation Mutant Kpc-2 (E166Q):
3.5.2.6;

Protein crystallography data

The structure of Crystal Structure of Deacylation Mutant Kpc-2 (E166Q), PDB code: 6z21 was solved by C.L.Tooke, P.Hinchliffe, J.Spencer, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 32.86 / 1.30
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 60.200, 78.440, 55.960, 90.00, 90.00, 90.00
R / Rfree (%) 14.3 / 17.3

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of Deacylation Mutant Kpc-2 (E166Q) (pdb code 6z21). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the Crystal Structure of Deacylation Mutant Kpc-2 (E166Q), PDB code: 6z21:

Chlorine binding site 1 out of 1 in 6z21

Go back to Chlorine Binding Sites List in 6z21
Chlorine binding site 1 out of 1 in the Crystal Structure of Deacylation Mutant Kpc-2 (E166Q)


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 Deacylation Mutant Kpc-2 (E166Q) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl309

b:50.4
occ:1.00
HH21 A:ARG220 2.3 20.8 1.0
NE2 A:HIS274 2.9 23.2 1.0
NH2 A:ARG220 3.0 17.4 1.0
HH22 A:ARG220 3.1 20.8 1.0
CD A:GLU276 3.2 20.8 1.0
HG3 A:GLU276 3.2 22.8 1.0
OE2 A:GLU276 3.3 21.0 1.0
HG2 A:GLU276 3.4 22.8 1.0
CG A:GLU276 3.5 19.0 1.0
OE1 A:GLU276 3.5 22.8 1.0
CE1 A:HIS274 3.7 24.2 1.0
HE1 A:HIS274 3.8 29.1 1.0
CD2 A:HIS274 3.9 21.6 1.0
O A:HOH470 4.0 43.7 1.0
HG21 A:THR237 4.0 22.1 1.0
HE A:ARG220 4.1 19.1 1.0
HD2 A:HIS274 4.1 25.9 1.0
CZ A:ARG220 4.2 16.1 1.0
O A:HOH521 4.4 29.7 1.0
NE A:ARG220 4.5 15.9 1.0
OG1 A:THR237 4.6 16.8 1.0
HG23 A:THR237 4.7 22.1 1.0
CG2 A:THR237 4.7 18.4 1.0
ND1 A:HIS274 4.9 24.9 1.0
CB A:GLU276 5.0 18.0 1.0

Reference:

C.L.Tooke, P.Hinchliffe, R.A.Bonomo, C.J.Schofield, A.J.Mulholland, J.Spencer. Natural Variants Modify Klebsiella Pneumoniae Carbapenemase (Kpc) Acyl-Enzyme Conformational Dynamics to Extend Antibiotic Resistance. J.Biol.Chem. 2020.
ISSN: ESSN 1083-351X
PubMed: 33257320
DOI: 10.1074/JBC.RA120.016461
Page generated: Mon Jul 29 17:55:49 2024

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