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Potassium in PDB 3b3c: Crystal Structure of the M180A Mutant of the Aminopeptidase From Vibrio Proteolyticus in Complex with Leucine Phosphonic Acid

Enzymatic activity of Crystal Structure of the M180A Mutant of the Aminopeptidase From Vibrio Proteolyticus in Complex with Leucine Phosphonic Acid

All present enzymatic activity of Crystal Structure of the M180A Mutant of the Aminopeptidase From Vibrio Proteolyticus in Complex with Leucine Phosphonic Acid:
3.4.11.10;

Protein crystallography data

The structure of Crystal Structure of the M180A Mutant of the Aminopeptidase From Vibrio Proteolyticus in Complex with Leucine Phosphonic Acid, PDB code: 3b3c was solved by N.J.Ataie, Q.Q.Hoang, G.A.Petsko, D.Ringe, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.63 / 1.46
Space group P 61 2 2
Cell size a, b, c (Å), α, β, γ (°) 108.189, 108.189, 97.206, 90.00, 90.00, 120.00
R / Rfree (%) 19.7 / 22.6

Other elements in 3b3c:

The structure of Crystal Structure of the M180A Mutant of the Aminopeptidase From Vibrio Proteolyticus in Complex with Leucine Phosphonic Acid also contains other interesting chemical elements:

Zinc (Zn) 2 atoms
Sodium (Na) 6 atoms

Potassium Binding Sites:

The binding sites of Potassium atom in the Crystal Structure of the M180A Mutant of the Aminopeptidase From Vibrio Proteolyticus in Complex with Leucine Phosphonic Acid (pdb code 3b3c). 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 the M180A Mutant of the Aminopeptidase From Vibrio Proteolyticus in Complex with Leucine Phosphonic Acid, PDB code: 3b3c:

Potassium binding site 1 out of 1 in 3b3c

Go back to Potassium Binding Sites List in 3b3c
Potassium binding site 1 out of 1 in the Crystal Structure of the M180A Mutant of the Aminopeptidase From Vibrio Proteolyticus in Complex with Leucine Phosphonic Acid


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 the M180A Mutant of the Aminopeptidase From Vibrio Proteolyticus in Complex with Leucine Phosphonic Acid within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K600

b:25.6
occ:1.00
 O2 A:PLU500 2.2 18.5 1.0
OE2 A:GLU151 2.3 17.7 1.0
O A:HOH672 2.3 23.1 1.0
O A:HOH680 2.4 24.5 1.0
O A:CYS227 2.4 15.4 1.0
C A:CYS227 3.2 16.1 1.0
CD A:GLU151 3.3 17.1 1.0
P A:PLU500 3.4 18.8 1.0
O A:HOH713 3.7 27.8 1.0
O A:HOH645 3.7 18.2 1.0
O3 A:PLU500 3.7 19.3 1.0
OE1 A:GLU151 3.8 15.9 1.0
CD2 A:LEU155 3.8 21.3 1.0
N A:SER228 4.0 15.8 1.0
CA A:CYS227 4.0 15.3 1.0
O A:HOH724 4.1 40.8 1.0
CA A:PLU500 4.1 18.8 1.0
CA A:SER228 4.1 15.6 1.0
O A:GLU151 4.2 17.9 1.0
O A:HOH696 4.4 36.0 1.0
CG A:GLU151 4.5 17.6 1.0
O A:ALA226 4.6 17.1 1.0
CB A:PLU500 4.7 19.0 1.0
O1 A:PLU500 4.7 18.4 1.0
CB A:SER228 4.8 15.6 1.0
CB A:CYS227 4.9 16.1 1.0
CE2 A:TYR225 5.0 15.4 1.0

Reference:

N.J.Ataie, Q.Q.Hoang, M.P.Zahniser, Y.Tu, A.Milne, G.A.Petsko, D.Ringe. Zinc Coordination Geometry and Ligand Binding Affinity: the Structural and Kinetic Analysis of the Second-Shell Serine 228 Residue and the Methionine 180 Residue of the Aminopeptidase From Vibrio Proteolyticus. Biochemistry V. 47 7673 2008.
ISSN: ISSN 0006-2960
PubMed: 18576673
DOI: 10.1021/BI702188E
Page generated: Sun Dec 13 23:14:31 2020

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