scPDB - 3fne entry

Protein Data Bank Entry:

PDB ID : 3fne

Resolution :1.980 Å

Experimental Method : X-ray

Deposition Date : 2008-12-24

Activity from ChEMBL: What is pChEMBL ?

	Min	Mean	Median	Standard Deviation	Max	Count
pChEMBL:

List of CHEMBLId :

Binding Site :

Uniprot Annotation

Name:	Enoyl-[acyl-carrier-protein] reductase [NADH]
ID:	INHA_MYCTU
AC:	P9WGR1
Organism:	Mycobacterium tuberculosis
Reign:	Bacteria
TaxID:	83332
EC Number:	1.3.1.9

Chains:

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

Ligand binding site composition:

B-Factor:	32.673
Number of residues:	32
Including
Standard Amino Acids:	30
Non Standard Amino Acids:	1
Water Molecules:	1
Cofactors:	NAD
Metals:

Cavity properties

Ligandability	Volume (Å3)
1.429	864.000

% Hydrophobic	% Polar
57.42	42.58
According to VolSite

Ligand :

HET Code:	8PC
Formula:	C18H13Cl2NO2
Molecular weight:	346.207 g/mol
DrugBank ID:	DB07287
Buried Surface Area:	79.61 %
Polar Surface area:	42.35 Å2

Number of
H-Bond Acceptors:	3
H-Bond Donors:	1
Rings:	3
Aromatic rings:	3
Anionic atoms:	0
Cationic atoms:	0
Rule of Five Violation:	1
Rotatable Bonds:	4

Mass center Coordinates

X	Y	Z
32.7767	39.173	9.10139

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
CL1	CD1	PHE- 97	4.01	0	Hydrophobic	false
CL1	CB	MET- 98	4.33	0	Hydrophobic	false
CL1	SD	MET- 103	4.38	0	Hydrophobic	false
C22	CE	MET- 103	3.53	0	Hydrophobic	false
C6	CB	PHE- 149	3.96	0	Hydrophobic	false
C7	CE1	PHE- 149	3.77	0	Hydrophobic	false
C28	CE2	PHE- 149	3.36	0	Hydrophobic	false
C27	CE	MET- 155	4.36	0	Hydrophobic	false
O22	OH	TYR- 158	2.55	131.77	H-Bond (Ligand Donor)	false
C27	CB	TYR- 158	4.11	0	Hydrophobic	false
C6	CE1	TYR- 158	3.44	0	Hydrophobic	false
C16	CE	MET- 161	3.53	0	Hydrophobic	false
C7	CB	PRO- 193	4.35	0	Hydrophobic	false
C3	CG2	THR- 196	4.41	0	Hydrophobic	false
CL2	CB	ALA- 198	3.43	0	Hydrophobic	false
C3	CB	ALA- 198	4.35	0	Hydrophobic	false
C14	CB	ALA- 198	3.37	0	Hydrophobic	false
C16	CB	ALA- 198	3.54	0	Hydrophobic	false
C4	CB	MET- 199	3.96	0	Hydrophobic	false
C22	CB	ALA- 201	4.3	0	Hydrophobic	false
CL1	CB	ALA- 201	3.82	0	Hydrophobic	false
C19	CD1	ILE- 202	3.83	0	Hydrophobic	false
C22	CG1	ILE- 202	3.94	0	Hydrophobic	false
C7	CD1	ILE- 202	4.28	0	Hydrophobic	false
C26	CG2	ILE- 202	3.91	0	Hydrophobic	false
C28	CD1	ILE- 202	3.6	0	Hydrophobic	false
C4	CD1	ILE- 202	3.41	0	Hydrophobic	false
C26	CD2	LEU- 218	4.47	0	Hydrophobic	false
CL2	C3D	NAD- 320	3.46	0	Hydrophobic	false
C7	C4N	NAD- 320	4.06	0	Hydrophobic	false
C14	C2D	NAD- 320	4.33	0	Hydrophobic	false
C1	C2D	NAD- 320	3.9	0	Hydrophobic	false
O13	O2D	NAD- 320	3.24	123.91	H-Bond (Protein Donor)	false