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Potassium in PDB 4mkk: Crystal Structure of C115A Mutant L-Methionine Gamma-Lyase From Citrobacter Freundii Modified By Allicine

Enzymatic activity of Crystal Structure of C115A Mutant L-Methionine Gamma-Lyase From Citrobacter Freundii Modified By Allicine

All present enzymatic activity of Crystal Structure of C115A Mutant L-Methionine Gamma-Lyase From Citrobacter Freundii Modified By Allicine:
4.4.1.11;

Protein crystallography data

The structure of Crystal Structure of C115A Mutant L-Methionine Gamma-Lyase From Citrobacter Freundii Modified By Allicine, PDB code: 4mkk was solved by S.V.Revtovich, A.D.Nikulin, E.A.Morozova, L.N.Zakomirdina, T.V.Demidkina, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 35.00 / 1.45
Space group I 2 2 2
Cell size a, b, c (Å), α, β, γ (°) 56.690, 122.860, 128.600, 90.00, 90.00, 90.00
R / Rfree (%) 13.8 / 17.3

Other elements in 4mkk:

The structure of Crystal Structure of C115A Mutant L-Methionine Gamma-Lyase From Citrobacter Freundii Modified By Allicine also contains other interesting chemical elements:

Chlorine (Cl) 1 atom
Sodium (Na) 5 atoms

Potassium Binding Sites:

The binding sites of Potassium atom in the Crystal Structure of C115A Mutant L-Methionine Gamma-Lyase From Citrobacter Freundii Modified By Allicine (pdb code 4mkk). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total only one binding site of Potassium was determined in the Crystal Structure of C115A Mutant L-Methionine Gamma-Lyase From Citrobacter Freundii Modified By Allicine, PDB code: 4mkk:

Potassium binding site 1 out of 1 in 4mkk

Go back to Potassium Binding Sites List in 4mkk
Potassium binding site 1 out of 1 in the Crystal Structure of C115A Mutant L-Methionine Gamma-Lyase From Citrobacter Freundii Modified By Allicine


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Crystal Structure of C115A Mutant L-Methionine Gamma-Lyase From Citrobacter Freundii Modified By Allicine within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K409

b:70.9
occ:1.00
 OH A:TYR113 2.4 29.0 0.5
O A:VAL338 2.7 17.3 0.5
CZ A:TYR113 3.3 26.8 0.5
O A:HOH788 3.3 43.9 1.0
CE2 A:TYR113 3.4 25.8 0.5
O A:VAL338 3.8 23.6 0.5
CG2 A:VAL338 3.8 22.2 0.5
C A:VAL338 3.8 17.4 0.5
CA A:SER339 3.9 15.2 0.5
CE1 A:TYR113 3.9 22.5 0.5
NH2 A:ARG374 4.0 37.0 1.0
C A:VAL338 4.0 20.3 0.5
N A:SER339 4.2 18.0 0.5
CA A:SER339 4.3 17.9 0.5
NZ A:LLP210 4.3 17.9 1.0
N A:SER339 4.5 17.3 0.5
CE1 A:TYR113 4.5 26.0 0.5
OH A:TYR113 4.5 26.5 0.5
C A:SER339 4.6 14.7 0.5
CE A:LLP210 4.6 18.0 1.0
C4' A:LLP210 4.6 19.0 1.0
NH1 A:ARG374 4.7 35.9 1.0
CB A:VAL338 4.7 18.2 0.5
CD2 A:TYR113 4.7 26.2 0.5
CZ A:TYR113 4.7 23.2 0.5
CZ A:ARG374 4.8 36.4 1.0
CD1 A:TYR113 4.8 22.8 0.5
C A:SER339 4.8 16.7 0.5
CA A:VAL338 4.9 17.4 0.5
CA A:VAL338 4.9 20.1 0.5
CG2 A:VAL338 4.9 20.3 0.5
CB A:VAL338 4.9 20.9 0.5
CD2 A:LEU340 4.9 28.3 1.0

Reference:

E.A.Morozova, S.V.Revtovich, N.V.Anufrieva, V.V.Kulikova, A.D.Nikulin, T.V.Demidkina. Alliin Is A Suicide Substrate of Citrobacter Freundii Methionine [Gamma]-Lyase: Structural Bases of Inactivation of the Enzyme Acta Crystallogr.,Sect.D V. 70 3034 2014.
ISSN: ISSN 0907-4449
DOI: 10.1107/S1399004714020938
Page generated: Mon Aug 12 11:35:01 2024

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