scPDB - 2i3g entry

Protein Data Bank Entry:

PDB ID : 2i3g

Resolution :1.850 Å

Experimental Method : X-ray

Deposition Date : 2006-08-18

Activity from ChEMBL: What is pChEMBL ?

	Min	Mean	Median	Standard Deviation	Max	Count
pChEMBL:

List of CHEMBLId :

Binding Site :

Uniprot Annotation

Name:	N-acetyl-gamma-glutamyl-phosphate reductase
ID:	ARGC_MYCTU
AC:	P9WPZ9
Organism:	Mycobacterium tuberculosis
Reign:	Bacteria
TaxID:	83332
EC Number:	1.2.1.38

Chains:

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

Ligand binding site composition:

B-Factor:	15.047
Number of residues:	50
Including
Standard Amino Acids:	46
Non Standard Amino Acids:	0
Water Molecules:	4
Cofactors:
Metals:

Cavity properties

Ligandability	Volume (Å3)
1.268	1029.375

% Hydrophobic	% Polar
38.69	61.31
According to VolSite

Ligand :

HET Code:	NAP
Formula:	C21H25N7O17P3
Molecular weight:	740.381 g/mol
DrugBank ID:	DB03461
Buried Surface Area:	63.8 %
Polar Surface area:	405.54 Å2

Number of
H-Bond Acceptors:	21
H-Bond Donors:	5
Rings:	5
Aromatic rings:	3
Anionic atoms:	4
Cationic atoms:	1
Rule of Five Violation:	2
Rotatable Bonds:	13

Mass center Coordinates

X	Y	Z
-9.57075	28.4802	-10.8523

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
O3B	N	SER- 18	3.37	121.67	H-Bond (Protein Donor)	false
O3X	OG	SER- 18	2.57	144.87	H-Bond (Protein Donor)	false
O3B	OG	SER- 18	2.65	159.35	H-Bond (Ligand Donor)	false
O1A	N	TYR- 20	2.86	168.13	H-Bond (Protein Donor)	false
O2N	N	ALA- 21	2.87	154.91	H-Bond (Protein Donor)	false
O2B	N	ALA- 48	3.48	159.76	H-Bond (Protein Donor)	false
O1X	N	ALA- 48	2.83	133.14	H-Bond (Protein Donor)	false
O1X	N	SER- 50	2.8	169.39	H-Bond (Protein Donor)	false
O3X	OG	SER- 50	2.53	162.22	H-Bond (Protein Donor)	false
C1B	CD2	LEU- 88	4.38	0	Hydrophobic	false
O3D	O	LEU- 88	2.55	155.82	H-Bond (Ligand Donor)	false
C4N	CB	CYS- 158	4.13	0	Hydrophobic	false
N7N	O	SER- 189	3.2	137.02	H-Bond (Ligand Donor)	false
O1A	N	ARG- 193	2.95	120.64	H-Bond (Protein Donor)	false
O2A	N	ARG- 193	3.04	157.46	H-Bond (Protein Donor)	false
O2A	N	ALA- 194	3.45	127.59	H-Bond (Protein Donor)	false
O7N	ND2	ASN- 320	3.09	153.88	H-Bond (Protein Donor)	false
C4N	CG2	THR- 325	3.66	0	Hydrophobic	false
O2D	O	HOH- 672	3.11	142.24	H-Bond (Protein Donor)	false
O2N	O	HOH- 839	2.74	177	H-Bond (Protein Donor)	false