scPDB - 2xls entry

Protein Data Bank Entry:

PDB ID : 2xls

Resolution :3.000 Å

Experimental Method : X-ray

Deposition Date : 2010-07-21

Activity from ChEMBL: What is pChEMBL ?

	Min	Mean	Median	Standard Deviation	Max	Count
pChEMBL:

List of CHEMBLId :

Binding Site :

Uniprot Annotation

Name:	Putative flavin-containing monooxygenase
ID:	Q83XK4_9GAMM
AC:	Q83XK4
Organism:	Methylophaga aminisulfidivorans
Reign:	Bacteria
TaxID:	230105
EC Number:	/

Chains:

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

Ligand binding site composition:

B-Factor:	28.004
Number of residues:	60
Including
Standard Amino Acids:	57
Non Standard Amino Acids:	1
Water Molecules:	2
Cofactors:	NAP
Metals:

Cavity properties

Ligandability	Volume (Å3)
1.130	1208.250

% Hydrophobic	% Polar
41.62	58.38
According to VolSite

Ligand :

HET Code:	FAD
Formula:	C27H31N9O15P2
Molecular weight:	783.534 g/mol
DrugBank ID:	DB03147
Buried Surface Area:	72.1 %
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
84.6196	26.6308	8.20496

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'	CG	PRO- 17	3.82	0	Hydrophobic	false
O1P	N	SER- 18	2.89	168.22	H-Bond (Protein Donor)	false
O2P	OG	SER- 18	2.5	142.61	H-Bond (Protein Donor)	false
O3B	OE1	GLU- 43	2.72	156.7	H-Bond (Ligand Donor)	false
N3A	N	LYS- 44	3.32	125.59	H-Bond (Protein Donor)	false
O2B	NE2	GLN- 45	3.06	176.75	H-Bond (Protein Donor)	false
O2A	N	GLN- 51	2.95	167.25	H-Bond (Protein Donor)	false
C2'	CG	GLN- 51	4.49	0	Hydrophobic	false
C8M	CG	GLN- 51	4.35	0	Hydrophobic	false
O3'	NE1	TRP- 52	3.25	142.66	H-Bond (Protein Donor)	false
O4'	NE1	TRP- 52	3.16	128.46	H-Bond (Protein Donor)	false
O1A	NE2	HIS- 68	2.59	166.32	H-Bond (Protein Donor)	false
C2B	CB	HIS- 68	4.35	0	Hydrophobic	false
C7M	CB	SER- 70	4.07	0	Hydrophobic	false
C8M	CB	SER- 70	3.72	0	Hydrophobic	false
C7M	CG	MET- 71	4	0	Hydrophobic	false
C6	CE	MET- 71	3.34	0	Hydrophobic	false
C7M	CE1	TYR- 72	4.4	0	Hydrophobic	false
C6	CD1	LEU- 75	3.87	0	Hydrophobic	false
C7M	CD1	LEU- 75	4.28	0	Hydrophobic	false
O4	N	LYS- 78	3.03	124.23	H-Bond (Protein Donor)	false
N1A	N	VAL- 131	2.91	170.79	H-Bond (Protein Donor)	false
C8M	CB	PHE- 170	3.6	0	Hydrophobic	false
C1'	CE2	PHE- 170	4.21	0	Hydrophobic	false
C2'	CD2	PHE- 170	4.33	0	Hydrophobic	false
O2'	OE1	GLN- 323	2.78	160.31	H-Bond (Ligand Donor)	false
C4'	CE1	PHE- 327	4.42	0	Hydrophobic	false
C3'	CZ	PHE- 330	4.3	0	Hydrophobic	false
C5'	CE2	PHE- 330	3.54	0	Hydrophobic	false
C9	C1D	NAP- 501	4.03	0	Hydrophobic	false
O1P	O	HOH- 2002	2.67	161.44	H-Bond (Protein Donor)	false
O2P	O	HOH- 2011	3.01	179.97	H-Bond (Protein Donor)	false