scPDB - 2fxu entry

Protein Data Bank Entry:

PDB ID : 2fxu

Resolution :1.350 Å

Experimental Method : X-ray

Deposition Date : 2006-02-06

Activity from ChEMBL: What is pChEMBL ?

	Min	Mean	Median	Standard Deviation	Max	Count
pChEMBL:

List of CHEMBLId :

Binding Site :

Uniprot Annotation

Name:	Actin, alpha skeletal muscle
ID:	ACTS_RABIT
AC:	P68135
Organism:	Oryctolagus cuniculus
Reign:	Eukaryota
TaxID:	9986
EC Number:	/

Chains:

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

Ligand binding site composition:

B-Factor:	20.605
Number of residues:	36
Including
Standard Amino Acids:	34
Non Standard Amino Acids:	0
Water Molecules:	2
Cofactors:
Metals:

Cavity properties

Ligandability	Volume (Å3)
0.785	452.250

% Hydrophobic	% Polar
50.00	50.00
According to VolSite

Ligand :

HET Code:	BID
Formula:	C40H68N2O8
Molecular weight:	704.977 g/mol
DrugBank ID:	-
Buried Surface Area:	48.62 %
Polar Surface area:	143.42 Å2

Number of
H-Bond Acceptors:	8
H-Bond Donors:	4
Rings:	3
Aromatic rings:	0
Anionic atoms:	0
Cationic atoms:	0
Rule of Five Violation:	2
Rotatable Bonds:	18

Mass center Coordinates

X	Y	Z
13.6394	-16.7477	35.2588

Binding mode :

What is Poseview ?

2D View
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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
O5	OH	TYR- 133	2.68	164.37	H-Bond (Protein Donor)	false
C17	CB	ALA- 135	3.77	0	Hydrophobic	false
C15	CB	ILE- 136	4.17	0	Hydrophobic	false
C12	CD1	ILE- 136	3.26	0	Hydrophobic	false
O4	N	ILE- 136	2.93	172.37	H-Bond (Protein Donor)	false
C16	CG1	VAL- 139	3.71	0	Hydrophobic	false
C17	CD2	LEU- 140	3.66	0	Hydrophobic	false
N2	OH	TYR- 143	3.05	168.76	H-Bond (Ligand Donor)	false
C20	CE2	TYR- 143	4.11	0	Hydrophobic	false
C33	CD2	TYR- 143	3.85	0	Hydrophobic	false
C34	CG	TYR- 143	3.65	0	Hydrophobic	false
C35	CD2	TYR- 143	3.78	0	Hydrophobic	false
C38	CB	TYR- 143	4.07	0	Hydrophobic	false
C17	CE2	TYR- 143	3.93	0	Hydrophobic	false
C32	CZ	TYR- 143	3.97	0	Hydrophobic	false
C38	CG2	THR- 148	4.06	0	Hydrophobic	false
C40	CG2	THR- 148	4.41	0	Hydrophobic	false
C30	CG2	THR- 148	3.68	0	Hydrophobic	false
C11	CB	TYR- 169	4.29	0	Hydrophobic	false
C5	CD2	TYR- 169	4.29	0	Hydrophobic	false
C1	CE1	TYR- 169	4.11	0	Hydrophobic	false
C29	CE1	TYR- 169	4.15	0	Hydrophobic	false
O3	N	ALA- 170	2.87	165.9	H-Bond (Protein Donor)	false
C10	CB	ALA- 170	4.3	0	Hydrophobic	false
C12	CB	ALA- 170	4.3	0	Hydrophobic	false
C9	CG	PRO- 172	4.47	0	Hydrophobic	false
C10	CB	PRO- 172	3.81	0	Hydrophobic	false
C35	CG2	ILE- 345	3.93	0	Hydrophobic	false
C17	CD2	LEU- 346	4.39	0	Hydrophobic	false
C24	CD1	LEU- 346	4.32	0	Hydrophobic	false
C33	CD1	LEU- 346	4.39	0	Hydrophobic	false
C35	CD1	LEU- 346	4.23	0	Hydrophobic	false
C20	CD1	LEU- 346	4.08	0	Hydrophobic	false
C24	CD1	LEU- 349	4.18	0	Hydrophobic	false
C33	CD1	LEU- 349	4.28	0	Hydrophobic	false
C35	CD1	LEU- 349	4.1	0	Hydrophobic	false
C25	CG2	THR- 351	3.63	0	Hydrophobic	false
C24	CB	PHE- 352	3.95	0	Hydrophobic	false
C21	SD	MET- 355	3.68	0	Hydrophobic	false
C24	SD	MET- 355	3.86	0	Hydrophobic	false