scPDB - 2wsa entry

Protein Data Bank Entry:

PDB ID : 2wsa

Resolution :1.600 Å

Experimental Method : X-ray

Deposition Date : 2009-09-04

Activity from ChEMBL: What is pChEMBL ?

	Min	Mean	Median	Standard Deviation	Max	Count
pChEMBL:

List of CHEMBLId :

Binding Site :

Uniprot Annotation

Name:	Glycylpeptide N-tetradecanoyltransferase
ID:	Q4Q5S8_LEIMA
AC:	Q4Q5S8
Organism:	Leishmania major
Reign:	Eukaryota
TaxID:	5664
EC Number:	/

Chains:

Chain Name:	Percentage of Residues within binding site
A	100 %

Ligand binding site composition:

B-Factor:	14.224
Number of residues:	55
Including
Standard Amino Acids:	51
Non Standard Amino Acids:	1
Water Molecules:	3
Cofactors:
Metals:

Cavity properties

Ligandability	Volume (Å3)
1.325	1076.625

% Hydrophobic	% Polar
56.43	43.57
According to VolSite

Ligand :

HET Code:	MYA
Formula:	C35H58N7O17P3S
Molecular weight:	973.858 g/mol
DrugBank ID:	DB02180
Buried Surface Area:	70.8 %
Polar Surface area:	429.68 Å2

Number of
H-Bond Acceptors:	22
H-Bond Donors:	5
Rings:	3
Aromatic rings:	2
Anionic atoms:	4
Cationic atoms:	0
Rule of Five Violation:	2
Rotatable Bonds:	32

Mass center Coordinates

X	Y	Z
29.9737	-9.78529	5.75459

Binding mode :

What is Poseview ?

2D View
3D View

Image generated by PoseView

Protein

Binding Site

Ligand

Interaction pattern

hydrophobic (CA)

aromatic (CZ)

hydrogen bond acceptor (O)

hydrogen bond acceptor/donor (OG)

hydrogen bond donor (N)

positively ionized (NZ)

negatively ionized (OD1)

metal (ZN)

Legend:

Represent the protein/ligand binding mode, centered on the ligand
Dashed lines represents hydrogen bonds and metal interactions
Green residue labels for amino acids with hydrophobic contacts (green lines) to the ligand

Image generated using PoseView by BioSolveIT

Ligand	Protein		Interaction
Atom	Atom	Residue	Distance (Å)	Angle (°)	Type
O9A	N	PHE- 14	2.89	134.64	H-Bond (Protein Donor)	false
N3A	NE1	TRP- 15	3.1	158.8	H-Bond (Protein Donor)	false
O9A	N	TRP- 15	2.72	170.7	H-Bond (Protein Donor)	false
C7M	CZ2	TRP- 15	3.69	0	Hydrophobic	false
C9M	CH2	TRP- 15	3.99	0	Hydrophobic	false
C6	CD1	TYR- 80	3.63	0	Hydrophobic	false
C2	CE1	TYR- 80	3.87	0	Hydrophobic	false
C6	CG2	VAL- 81	4.02	0	Hydrophobic	false
C2	CG2	VAL- 81	4.05	0	Hydrophobic	false
C8M	CG2	ILE- 166	3.93	0	Hydrophobic	false
C5M	CG2	ILE- 166	3.88	0	Hydrophobic	false
CAM	CG1	ILE- 166	3.85	0	Hydrophobic	false
C4M	CB	LEU- 169	3.8	0	Hydrophobic	false
C6M	CD2	LEU- 169	3.98	0	Hydrophobic	false
C13	CD2	LEU- 169	4.25	0	Hydrophobic	false
C14	CG	LEU- 169	3.64	0	Hydrophobic	false
O2M	N	LEU- 169	3.09	145.97	H-Bond (Protein Donor)	false
N4	O	LEU- 169	2.77	151.44	H-Bond (Ligand Donor)	false
O9	N	VAL- 171	2.9	170.95	H-Bond (Protein Donor)	false
C14	CG2	VAL- 171	3.65	0	Hydrophobic	false
C10	CB	VAL- 171	4.42	0	Hydrophobic	false
C10	CD	ARG- 176	3.56	0	Hydrophobic	false
O5A	N	GLU- 177	2.82	160.7	H-Bond (Protein Donor)	false
O7A	NH2	ARG- 179	2.71	158.94	H-Bond (Protein Donor)	false
O7A	NH1	ARG- 179	3.14	132.8	H-Bond (Protein Donor)	false
O2A	N	ARG- 179	2.93	143.12	H-Bond (Protein Donor)	false
O7A	CZ	ARG- 179	3.34	0	Ionic (Protein Cationic)	false
C14	CB	ALA- 181	4.02	0	Hydrophobic	false
C12	CB	ALA- 181	3.76	0	Hydrophobic	false
O1A	N	ALA- 181	2.72	163.46	H-Bond (Protein Donor)	false
C4X	CG	PRO- 182	4.03	0	Hydrophobic	false
CBM	CG2	ILE- 185	4.27	0	Hydrophobic	false
C9M	CG2	ILE- 185	4	0	Hydrophobic	false
C7M	CD1	ILE- 185	3.83	0	Hydrophobic	false
CCM	CB	THR- 189	4.35	0	Hydrophobic	false
CDM	CG2	THR- 189	4.18	0	Hydrophobic	false
CEM	CG1	VAL- 192	3.59	0	Hydrophobic	false
CAM	CB	ALA- 200	3.83	0	Hydrophobic	false
CDM	CB	ALA- 200	3.73	0	Hydrophobic	false
CAM	CD2	TYR- 202	4.33	0	Hydrophobic	false
C9M	CE2	TYR- 202	3.91	0	Hydrophobic	false
C8M	CD2	TYR- 202	4.06	0	Hydrophobic	false
C3M	CB	TYR- 202	4.29	0	Hydrophobic	false
C5M	CD1	TYR- 202	3.55	0	Hydrophobic	false
S1	CB	ALA- 204	4.07	0	Hydrophobic	false
CBM	CD1	TYR- 404	4.42	0	Hydrophobic	false
CAM	CB	TYR- 404	3.8	0	Hydrophobic	false
C9M	CD1	TYR- 404	3.85	0	Hydrophobic	false
CDM	CD2	TYR- 404	3.58	0	Hydrophobic	false
O5A	O	HOH- 2287	3.05	179.97	H-Bond (Protein Donor)	false