Potassium in PDB 4u6c: Hsmetap in Complex with [(1R)-1-Amino-3-Cyclopentylpropyl]Phosphonic Acid

Enzymatic activity of Hsmetap in Complex with [(1R)-1-Amino-3-Cyclopentylpropyl]Phosphonic Acid

All present enzymatic activity of Hsmetap in Complex with [(1R)-1-Amino-3-Cyclopentylpropyl]Phosphonic Acid:
3.4.11.18;

Protein crystallography data

The structure of Hsmetap in Complex with [(1R)-1-Amino-3-Cyclopentylpropyl]Phosphonic Acid, PDB code: 4u6c was solved by T.Arya, A.Addlagatta, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

*Resolution Low / High (Å)*	21.00 / 1.91
*Space group*	P 1 2₁ 1
*Cell size a, b, c (Å), α, β, γ (°)*	47.076, 77.299, 47.420, 90.00, 91.38, 90.00
*R / R_free (%)*	18.3 / 22.9

Other elements in 4u6c:

The structure of Hsmetap in Complex with [(1R)-1-Amino-3-Cyclopentylpropyl]Phosphonic Acid also contains other interesting chemical elements:

Cobalt

(Co)

2 atoms

Potassium Binding Sites:

The binding sites of Potassium atom in the Hsmetap in Complex with [(1R)-1-Amino-3-Cyclopentylpropyl]Phosphonic Acid (pdb code 4u6c). 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 Hsmetap in Complex with [(1R)-1-Amino-3-Cyclopentylpropyl]Phosphonic Acid, PDB code: 4u6c:

Potassium binding site 1 out of 1 in 4u6c

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Potassium Binding Sites List in 4u6c

Potassium binding site 1 out of 1 in the Hsmetap in Complex with [(1R)-1-Amino-3-Cyclopentylpropyl]Phosphonic Acid

Mono view

Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Hsmetap in Complex with [(1R)-1-Amino-3-Cyclopentylpropyl]Phosphonic Acid within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
A:K402 b:70.9 occ:1.00	OE2	A:GLU208	2.7	39.5	1.0
	O	A:LEU96	2.7	40.5	1.0
	O	A:HOH546	2.8	42.9	1.0
	N	A:GLY94	3.2	41.9	1.0
	N	A:LEU96	3.3	45.1	1.0
	C	A:GLY94	3.3	40.8	1.0
	O	A:GLY94	3.3	43.4	1.0
	CA	A:GLY94	3.5	38.7	1.0
	C	A:LEU96	3.5	39.6	1.0
	CA	A:LEU96	3.7	45.2	1.0
	CB	A:LEU96	3.7	42.2	1.0
	CD	A:GLU208	3.7	37.0	1.0
	N	A:LYS95	3.8	44.9	1.0
	CB	A:TYR92	3.9	46.6	1.0
	NH1	A:ARG97	3.9	52.7	1.0
	N	A:THR93	4.0	45.6	1.0
	CZ2	A:TRP349	4.0	34.7	1.0
	CG	A:GLU208	4.1	36.1	1.0
	C	A:LYS95	4.1	49.8	1.0
	CD1	A:TYR92	4.3	48.9	1.0
	C	A:THR93	4.3	44.3	1.0
	OG1	A:THR93	4.4	35.0	1.0
	CA	A:LYS95	4.5	48.0	1.0
	C	A:TYR92	4.5	46.7	1.0
	CG	A:TYR92	4.5	47.0	1.0
	NE1	A:TRP349	4.5	35.5	1.0
	CA	A:THR93	4.6	42.0	1.0
	CA	A:TYR92	4.6	45.5	1.0
	CE2	A:TRP349	4.7	33.8	1.0
	OE1	A:GLU208	4.7	36.0	1.0
	N	A:ARG97	4.8	40.8	1.0
	O	A:LYS95	5.0	46.1	1.0

Reference:

T.Arya, R.Reddi, C.Kishor, R.J.Ganji, S.Bhukya, R.Gumpena, S.Mcgowan, M.Drag, A.Addlagatta. Identification of the Molecular Basis of Inhibitor Selectivity Between the Human and Streptococcal Type I Methionine Aminopeptidases J.Med.Chem. V. 58 2350 2015.
ISSN: ISSN 0022-2623
PubMed: 25699713
DOI: 10.1021/JM501790E

Page generated: Mon Aug 12 12:12:31 2024

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