scPDB - 2aqi entry

Protein Data Bank Entry:

PDB ID : 2aqi

Resolution :2.200 Å

Experimental Method : X-ray

Deposition Date : 2005-08-18

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
A	100 %

Ligand binding site composition:

B-Factor:	26.770
Number of residues:	54
Including
Standard Amino Acids:	49
Non Standard Amino Acids:	0
Water Molecules:	5
Cofactors:
Metals:

Cavity properties

Ligandability	Volume (Å3)
1.623	1059.750

% Hydrophobic	% Polar
57.32	42.68
According to VolSite

Ligand :

HET Code:	NAI
Formula:	C21H27N7O14P2
Molecular weight:	663.425 g/mol
DrugBank ID:	DB00157
Buried Surface Area:	69.76 %
Polar Surface area:	342.9 Å2

Number of
H-Bond Acceptors:	19
H-Bond Donors:	6
Rings:	5
Aromatic rings:	2
Anionic atoms:	2
Cationic atoms:	0
Rule of Five Violation:	3
Rotatable Bonds:	11

Mass center Coordinates

X	Y	Z
2.08914	-31.9661	14.0043

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
C3B	CG2	ILE- 16	3.85	0	Hydrophobic	false
O2A	OG	SER- 20	2.59	163.88	H-Bond (Protein Donor)	false
O2N	N	ILE- 21	2.77	160.05	H-Bond (Protein Donor)	false
C1D	CD1	ILE- 21	4.45	0	Hydrophobic	false
C4N	CD1	ILE- 21	4.36	0	Hydrophobic	false
DuAr	DuAr	PHE- 41	3.99	0	Aromatic Face/Face	false
N6A	OD1	ASP- 64	3	147.69	H-Bond (Ligand Donor)	false
N1A	N	VAL- 65	2.96	145.01	H-Bond (Protein Donor)	false
C5D	CB	SER- 94	4.17	0	Hydrophobic	false
C1B	CG1	ILE- 95	4.22	0	Hydrophobic	false
O3D	O	ILE- 95	3.05	129.29	H-Bond (Ligand Donor)	false
O4B	N	GLY- 96	3.36	157.56	H-Bond (Protein Donor)	false
C1D	CB	MET- 147	3.66	0	Hydrophobic	false
C4D	CB	MET- 147	3.42	0	Hydrophobic	false
C4N	CD1	PHE- 149	3.7	0	Hydrophobic	false
O3D	NZ	LYS- 165	2.95	136.85	H-Bond (Protein Donor)	false
O2D	NZ	LYS- 165	2.98	138.62	H-Bond (Protein Donor)	false
C4N	CB	ALA- 191	4.19	0	Hydrophobic	false
O7N	N	ILE- 194	2.59	176.88	H-Bond (Protein Donor)	false
N7N	O	ILE- 194	3.13	137.46	H-Bond (Ligand Donor)	false
O1N	OG1	THR- 196	3.11	165.41	H-Bond (Protein Donor)	false
O2N	O	HOH- 271	2.7	179.94	H-Bond (Protein Donor)	false
O2B	O	HOH- 272	3.17	159.16	H-Bond (Protein Donor)	false
O3D	O	HOH- 287	3.3	127.57	H-Bond (Ligand Donor)	false
O3D	O	HOH- 288	2.86	128.67	H-Bond (Protein Donor)	false