scPDB - 3dme entry

Protein Data Bank Entry:

PDB ID : 3dme

Resolution :1.700 Å

Experimental Method : X-ray

Deposition Date : 2008-06-30

Activity from ChEMBL: What is pChEMBL ?

	Min	Mean	Median	Standard Deviation	Max	Count
pChEMBL:

List of CHEMBLId :

Binding Site :

Uniprot Annotation

Name:	Putative conserved exported protein
ID:	Q7VU70_BORPE
AC:	Q7VU70
Organism:	Bordetella pertussis
Reign:	Bacteria
TaxID:	257313
EC Number:	/

Chains:

Chain Name:	Percentage of Residues within binding site
A	96 %
B	4 %

Ligand binding site composition:

B-Factor:	13.759
Number of residues:	73
Including
Standard Amino Acids:	69
Non Standard Amino Acids:	0
Water Molecules:	4
Cofactors:
Metals:

Cavity properties

Ligandability	Volume (Å3)
1.206	887.625

% Hydrophobic	% Polar
45.25	54.75
According to VolSite

Ligand :

HET Code:	FAD
Formula:	C27H31N9O15P2
Molecular weight:	783.534 g/mol
DrugBank ID:	DB03147
Buried Surface Area:	74.26 %
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
9.17266	42.9443	21.3114

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
C4'	CG2	VAL- 14	3.65	0	Hydrophobic	false
C5'	CG2	VAL- 15	4.06	0	Hydrophobic	false
O1P	N	VAL- 15	3.17	140.76	H-Bond (Protein Donor)	false
O3B	OE1	GLU- 34	2.69	169.79	H-Bond (Ligand Donor)	false
O3B	OE2	GLU- 34	3.18	129.13	H-Bond (Ligand Donor)	false
O2B	OE2	GLU- 34	2.5	159.41	H-Bond (Ligand Donor)	false
N3A	N	ALA- 35	3.16	138.01	H-Bond (Protein Donor)	false
O1A	N	THR- 43	3.3	154.96	H-Bond (Protein Donor)	false
O2'	O	THR- 43	2.88	133.33	H-Bond (Ligand Donor)	false
C3'	CG2	THR- 43	4.24	0	Hydrophobic	false
C8M	CG2	THR- 43	3.52	0	Hydrophobic	false
O2A	OG	SER- 44	2.61	156.84	H-Bond (Protein Donor)	false
O4'	OG	SER- 44	2.74	150.56	H-Bond (Ligand Donor)	false
C2'	CB	ASN- 47	4.42	0	Hydrophobic	false
C9A	CB	ASN- 47	3.25	0	Hydrophobic	false
O4	OG	SER- 48	2.95	150.05	H-Bond (Protein Donor)	false
N5	N	SER- 48	3.32	171.39	H-Bond (Protein Donor)	false
N5	OG	SER- 48	3.16	125.88	H-Bond (Protein Donor)	false
N3	O	VAL- 50	2.77	159.55	H-Bond (Ligand Donor)	false
O4	N	VAL- 50	3.07	155.11	H-Bond (Protein Donor)	false
N6A	O	LEU- 173	2.91	158.97	H-Bond (Ligand Donor)	false
N1A	N	LEU- 173	2.93	155.45	H-Bond (Protein Donor)	false
C7M	CE2	TYR- 234	4.05	0	Hydrophobic	false
C7M	CB	PRO- 272	4.12	0	Hydrophobic	false
C8M	CG	ARG- 316	3.37	0	Hydrophobic	false
O3'	O	ILE- 348	2.79	159.35	H-Bond (Ligand Donor)	false
C9A	CB	SER- 350	4.07	0	Hydrophobic	false
C1'	CB	SER- 350	4.18	0	Hydrophobic	false
C2'	CB	LEU- 353	4.2	0	Hydrophobic	false
O2	OG1	THR- 354	2.83	164.09	H-Bond (Protein Donor)	false
O2	N	THR- 354	2.8	152.32	H-Bond (Protein Donor)	false
O1A	O	HOH- 1037	2.68	151.75	H-Bond (Protein Donor)	false
O1P	O	HOH- 1263	2.65	161.31	H-Bond (Protein Donor)	false