scPDB - 3pw8 entry

Protein Data Bank Entry:

PDB ID : 3pw8

Resolution :2.970 Å

Experimental Method : X-ray

Deposition Date : 2010-12-07

Activity from ChEMBL: What is pChEMBL ?

	Min	Mean	Median	Standard Deviation	Max	Count
pChEMBL:

List of CHEMBLId :

Binding Site :

Uniprot Annotation

Name:	1,2-phenylacetyl-CoA epoxidase, subunit A
ID:	PAAA_ECOLI
AC:	P76077
Organism:	Escherichia coli
Reign:	Bacteria
TaxID:	83333
EC Number:	1.14.13.149

Chains:

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

Ligand binding site composition:

B-Factor:	43.129
Number of residues:	46
Including
Standard Amino Acids:	46
Non Standard Amino Acids:	0
Water Molecules:	0
Cofactors:
Metals:

Cavity properties

Ligandability	Volume (Å3)
0.770	867.375

% Hydrophobic	% Polar
37.35	62.65
According to VolSite

Ligand :

HET Code:	ACO
Formula:	C23H34N7O17P3S
Molecular weight:	805.539 g/mol
DrugBank ID:	-
Buried Surface Area:	64.02 %
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:	20

Mass center Coordinates

X	Y	Z
-14.4385	-18.1941	-36.2218

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
O7A	CZ	ARG- 33	3.91	0	Ionic (Protein Cationic)	false
O9A	CZ	ARG- 33	3.79	0	Ionic (Protein Cationic)	false
O5A	CZ	ARG- 33	3.74	0	Ionic (Protein Cationic)	false
O9A	NH1	ARG- 33	2.7	153.15	H-Bond (Protein Donor)	false
O5A	NH2	ARG- 33	3.29	150.6	H-Bond (Protein Donor)	false
O5A	NH1	ARG- 33	3.25	152.69	H-Bond (Protein Donor)	false
CAP	CG	GLN- 34	4.11	0	Hydrophobic	false
O9A	NE2	GLN- 37	2.8	151.92	H-Bond (Protein Donor)	false
C6P	CB	HIS- 38	3.91	0	Hydrophobic	false
S1P	CB	SER- 41	3.65	0	Hydrophobic	false
C1B	CD	LYS- 103	3.89	0	Hydrophobic	false
O8A	NZ	LYS- 103	2.74	166.1	H-Bond (Protein Donor)	false
O8A	NZ	LYS- 103	2.74	0	Ionic (Protein Cationic)	false
C2P	CB	SER- 105	4.1	0	Hydrophobic	false
N1A	N	SER- 106	2.7	139.9	H-Bond (Protein Donor)	false
N6A	OG	SER- 106	3.21	124.37	H-Bond (Ligand Donor)	false
CH3	CZ	PHE- 108	3.44	0	Hydrophobic	false
CH3	CG1	VAL- 125	4.34	0	Hydrophobic	false
CH3	CB	ALA- 129	3.67	0	Hydrophobic	false
C2P	CB	ALA- 129	3.86	0	Hydrophobic	false
O9P	ND2	ASN- 132	3.44	147.8	H-Bond (Protein Donor)	false
N6A	O	MET- 193	3.43	126.95	H-Bond (Ligand Donor)	false
N6A	O	MET- 194	3.37	132.89	H-Bond (Ligand Donor)	false
C2P	CE	MET- 194	3.44	0	Hydrophobic	false
CH3	CE	MET- 194	4	0	Hydrophobic	false
C5B	CG	PRO- 197	4.38	0	Hydrophobic	false
O1A	OG	SER- 202	3.13	161.52	H-Bond (Protein Donor)	false
C5B	CG	PRO- 203	4.03	0	Hydrophobic	false
O7A	ND2	ASN- 204	3.33	165.34	H-Bond (Protein Donor)	false
O1A	N	ASN- 204	3.04	146.68	H-Bond (Protein Donor)	false
O3A	ND2	ASN- 204	2.98	166.35	H-Bond (Protein Donor)	false
O2A	NZ	LYS- 214	3.72	0	Ionic (Protein Cationic)	false
O4A	NZ	LYS- 214	2.66	0	Ionic (Protein Cationic)	false
O4A	NZ	LYS- 214	2.66	160.13	H-Bond (Protein Donor)	false
O2A	ND2	ASN- 218	2.62	146.68	H-Bond (Protein Donor)	false