scPDB - 3eq6 entry

Protein Data Bank Entry:

PDB ID : 3eq6

Resolution :2.400 Å

Experimental Method : X-ray

Deposition Date : 2008-09-30

Activity from ChEMBL: What is pChEMBL ?

	Min	Mean	Median	Standard Deviation	Max	Count
pChEMBL:

List of CHEMBLId :

Binding Site :

Uniprot Annotation

Name:	Acyl-coenzyme A synthetase ACSM2A, mitochondrial
ID:	ACS2A_HUMAN
AC:	Q08AH3
Organism:	Homo sapiens
Reign:	Eukaryota
TaxID:	9606
EC Number:	6.2.1.2

Chains:

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

Ligand binding site composition:

B-Factor:	21.977
Number of residues:	44
Including
Standard Amino Acids:	42
Non Standard Amino Acids:	1
Water Molecules:	1
Cofactors:	AMP
Metals:

Cavity properties

Ligandability	Volume (Å3)
0.848	860.625

% Hydrophobic	% Polar
50.98	49.02
According to VolSite

Ligand :

HET Code:	BCO
Formula:	C25H38N7O17P3S
Molecular weight:	833.592 g/mol
DrugBank ID:	-
Buried Surface Area:	47.82 %
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:	22

Mass center Coordinates

X	Y	Z
-15.8801	57.8635	-39.9899

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
O12	NE2	GLN- 139	3.14	165.61	H-Bond (Protein Donor)	false
S1	CB	TRP- 265	3.87	0	Hydrophobic	false
S1	CG2	ILE- 266	4.12	0	Hydrophobic	false
C24	CG2	ILE- 266	3.85	0	Hydrophobic	false
S1	CB	LEU- 267	3.67	0	Hydrophobic	false
C23	CB	LEU- 267	4.21	0	Hydrophobic	false
C25	CD1	LEU- 270	4.39	0	Hydrophobic	false
C13	CE1	PHE- 291	3.4	0	Hydrophobic	false
C14	CE2	PHE- 291	4.11	0	Hydrophobic	false
C14	CG2	ILE- 313	3.59	0	Hydrophobic	false
C14	CE	MET- 317	3.84	0	Hydrophobic	false
C23	CG1	VAL- 337	3.9	0	Hydrophobic	false
C24	CG2	VAL- 337	4.4	0	Hydrophobic	false
C25	CD1	LEU- 368	3.62	0	Hydrophobic	false
N6	O	SER- 469	2.79	120.02	H-Bond (Ligand Donor)	false
N7	O	GLY- 470	2.71	159.55	H-Bond (Ligand Donor)	false
O12	OH	TYR- 471	2.56	127.46	H-Bond (Protein Donor)	false
O11	OH	TYR- 471	3.05	126.5	H-Bond (Protein Donor)	false
C10	CE2	TYR- 471	4.13	0	Hydrophobic	false
C18	CE1	TYR- 471	3.94	0	Hydrophobic	false
O6	NZ	LYS- 532	3.13	159.73	H-Bond (Protein Donor)	false
O2	NZ	LYS- 532	3.42	129.51	H-Bond (Protein Donor)	false
O6	NZ	LYS- 532	3.13	0	Ionic (Protein Cationic)	false
C4	CB	PRO- 537	3.8	0	Hydrophobic	false
C3	CB	PRO- 537	3.88	0	Hydrophobic	false
C5	CB	TYR- 538	4.28	0	Hydrophobic	false
C3	CE2	TYR- 540	4.49	0	Hydrophobic	false
O9	NH2	ARG- 542	2.76	138.6	H-Bond (Protein Donor)	false
O9	NH1	ARG- 542	2.67	142.58	H-Bond (Protein Donor)	false
O9	CZ	ARG- 542	3.12	0	Ionic (Protein Cationic)	false
O16	O	HOH- 1109	3.07	165.49	H-Bond (Protein Donor)	false