scPDB - 3ust entry

Protein Data Bank Entry:

PDB ID : 3ust

Resolution :2.100 Å

Experimental Method : X-ray

Deposition Date : 2011-11-23

Activity from ChEMBL: What is pChEMBL ?

	Min	Mean	Median	Standard Deviation	Max	Count
pChEMBL:

List of CHEMBLId :

Binding Site :

Uniprot Annotation

Name:	AcMNPV orf92
ID:	O92452_NPVBM
AC:	O92452
Organism:	Bombyx mori nuclear polyhedrosis virus
Reign:	Viruses
TaxID:	271108
EC Number:	/

Chains:

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

Ligand binding site composition:

B-Factor:	19.806
Number of residues:	41
Including
Standard Amino Acids:	39
Non Standard Amino Acids:	0
Water Molecules:	2
Cofactors:
Metals:

Cavity properties

Ligandability	Volume (Å3)
0.633	290.250

% Hydrophobic	% Polar
65.12	34.88
According to VolSite

Ligand :

HET Code:	FAD
Formula:	C27H31N9O15P2
Molecular weight:	783.534 g/mol
DrugBank ID:	DB03147
Buried Surface Area:	60.13 %
Polar Surface area:	381.7 Å2

Number of
H-Bond Acceptors:	22
H-Bond Donors:	7
Rings:	6
Aromatic rings:	3
Anionic atoms:	2
Cationic atoms:	0
Rule of Five Violation:	3
Rotatable Bonds:	13

Mass center Coordinates

X	Y	Z
-10.7456	31.0643	46.6592

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
C1'	CD1	PHE- 106	3.58	0	Hydrophobic	false
C3'	CB	PHE- 106	4.31	0	Hydrophobic	false
C4'	CD2	PHE- 106	3.82	0	Hydrophobic	false
C5B	CG2	THR- 107	3.8	0	Hydrophobic	false
C8M	CG2	ILE- 109	3.75	0	Hydrophobic	false
C7M	CH2	TRP- 110	4.31	0	Hydrophobic	false
C8M	CE2	TRP- 110	3.38	0	Hydrophobic	false
O2'	NE1	TRP- 110	2.94	150.54	H-Bond (Protein Donor)	false
O3'	NE1	TRP- 110	3.06	130.23	H-Bond (Protein Donor)	false
C7M	SD	MET- 113	3.88	0	Hydrophobic	false
C8M	SD	MET- 113	4.38	0	Hydrophobic	false
C7M	CZ	PHE- 151	3.48	0	Hydrophobic	false
C8M	CE1	PHE- 151	4.19	0	Hydrophobic	false
C7	CE1	PHE- 151	3.38	0	Hydrophobic	false
C6	CB	CYS- 158	4.43	0	Hydrophobic	false
C9A	SG	CYS- 158	4.02	0	Hydrophobic	false
C1'	SG	CYS- 158	4.46	0	Hydrophobic	false
C7M	CD1	TYR- 162	3.55	0	Hydrophobic	false
N6A	O	MET- 222	2.77	156.76	H-Bond (Ligand Donor)	false
O2A	NE2	HIS- 225	2.56	170.09	H-Bond (Protein Donor)	false
DuAr	DuAr	HIS- 225	3.76	0	Aromatic Face/Face	false
N6A	OD1	ASN- 226	2.86	135.59	H-Bond (Ligand Donor)	false
C6	CG1	VAL- 228	4.08	0	Hydrophobic	false
C9A	CG1	VAL- 228	3.83	0	Hydrophobic	false
O2A	ND2	ASN- 229	2.86	171.89	H-Bond (Protein Donor)	false
O2'	OD1	ASN- 229	2.77	160.91	H-Bond (Ligand Donor)	false
C2'	CD	LYS- 232	4.46	0	Hydrophobic	false
O4'	NZ	LYS- 232	2.64	159.48	H-Bond (Protein Donor)	false
N3	OE1	GLN- 235	2.88	133.19	H-Bond (Ligand Donor)	false
O4	NE2	GLN- 235	3	157.63	H-Bond (Protein Donor)	false
C1B	CE	MET- 247	4.49	0	Hydrophobic	false
N7A	O	HOH- 284	2.99	172.5	H-Bond (Protein Donor)	false