scPDB - 3r7k entry

Protein Data Bank Entry:

PDB ID : 3r7k

Resolution :2.500 Å

Experimental Method : X-ray

Deposition Date : 2011-03-22

Activity from ChEMBL: What is pChEMBL ?

	Min	Mean	Median	Standard Deviation	Max	Count
pChEMBL:

List of CHEMBLId :

Binding Site :

Uniprot Annotation

Name:	Probable acyl CoA dehydrogenase
ID:	B1MPB5_MYCA9
AC:	B1MPB5
Organism:	Mycobacterium abscessus
Reign:	Bacteria
TaxID:	561007
EC Number:	/

Chains:

Chain Name:	Percentage of Residues within binding site
A	63 %
B	33 %
C	3 %

Ligand binding site composition:

B-Factor:	50.534
Number of residues:	62
Including
Standard Amino Acids:	60
Non Standard Amino Acids:	0
Water Molecules:	2
Cofactors:
Metals:

Cavity properties

Ligandability	Volume (Å3)
0.376	2143.125

% Hydrophobic	% Polar
51.81	48.19
According to VolSite

Ligand :

HET Code:	FDA
Formula:	C27H33N9O15P2
Molecular weight:	785.550 g/mol
DrugBank ID:	-
Buried Surface Area:	68.77 %
Polar Surface area:	381.04 Å2

Number of
H-Bond Acceptors:	21
H-Bond Donors:	9
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
34.6157	-8.42696	-21.465

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
N3	O	LEU- 144	3.23	153.16	H-Bond (Ligand Donor)	false
O2	N	VAL- 146	2.94	146.65	H-Bond (Protein Donor)	false
N1	OG1	THR- 147	2.66	165.08	H-Bond (Protein Donor)	false
O2	N	THR- 147	2.81	169.99	H-Bond (Protein Donor)	false
C1'	CB	THR- 147	4.13	0	Hydrophobic	false
O1A	OG	SER- 153	2.58	157.58	H-Bond (Protein Donor)	false
O1A	N	SER- 153	3.32	151.45	H-Bond (Protein Donor)	false
C8M	CD1	PHE- 177	4.27	0	Hydrophobic	false
C1'	CB	PHE- 177	3.73	0	Hydrophobic	false
C9	CB	PHE- 177	3.4	0	Hydrophobic	false
O4	OG1	THR- 179	3.27	156.12	H-Bond (Protein Donor)	false
N5	OG1	THR- 179	3.1	132.39	H-Bond (Protein Donor)	false
C7M	CD	LYS- 221	3.94	0	Hydrophobic	false
C7M	CE3	TRP- 224	3.74	0	Hydrophobic	false
O2A	NH2	ARG- 288	3.41	138.29	H-Bond (Protein Donor)	false
O2A	NE	ARG- 288	3.13	152.15	H-Bond (Protein Donor)	false
O2P	NH2	ARG- 288	2.99	124.89	H-Bond (Protein Donor)	false
O2A	CZ	ARG- 288	3.72	0	Ionic (Protein Cationic)	false
N7A	OG1	THR- 290	2.96	169.03	H-Bond (Protein Donor)	false
C1B	CD2	LEU- 295	4.04	0	Hydrophobic	false
C5B	CD1	LEU- 295	4.13	0	Hydrophobic	false
N1A	NE2	GLN- 299	2.96	152.06	H-Bond (Protein Donor)	false
C1B	CD1	ILE- 301	4.24	0	Hydrophobic	false
O1P	N	GLY- 360	2.64	144.23	H-Bond (Protein Donor)	false
C7M	CD2	TYR- 363	4.38	0	Hydrophobic	false
C8M	CD2	TYR- 363	4.09	0	Hydrophobic	false
C8M	CE	MET- 364	3.73	0	Hydrophobic	false
C7M	CG1	ILE- 378	4.45	0	Hydrophobic	false
C8	CD1	ILE- 378	3.32	0	Hydrophobic	false
C5'	CG2	ILE- 381	4.39	0	Hydrophobic	false
O2B	OG1	THR- 385	2.7	155.92	H-Bond (Protein Donor)	false
C5'	CG2	THR- 385	4.01	0	Hydrophobic	false
C2B	CG2	THR- 385	4.03	0	Hydrophobic	false
O2B	OE1	GLU- 387	2.55	125.28	H-Bond (Ligand Donor)	false
O2P	O	HOH- 415	2.88	152.82	H-Bond (Protein Donor)	false