scPDB - 2qtr entry

Protein Data Bank Entry:

PDB ID : 2qtr

Resolution :1.700 Å

Experimental Method : X-ray

Deposition Date : 2007-08-02

Activity from ChEMBL: What is pChEMBL ?

	Min	Mean	Median	Standard Deviation	Max	Count
pChEMBL:

List of CHEMBLId :

Binding Site :

Uniprot Annotation

Name:	Probable nicotinate-nucleotide adenylyltransferase
ID:	NADD_BACAC
AC:	C3L5T6
Organism:	Bacillus anthracis
Reign:	Bacteria
TaxID:	568206
EC Number:	/

Chains:

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

Ligand binding site composition:

B-Factor:	24.054
Number of residues:	56
Including
Standard Amino Acids:	51
Non Standard Amino Acids:	0
Water Molecules:	5
Cofactors:
Metals:

Cavity properties

Ligandability	Volume (Å3)
0.715	1120.500

% Hydrophobic	% Polar
37.95	62.05
According to VolSite

Ligand :

HET Code:	NXX
Formula:	C21H24N6O15P2
Molecular weight:	662.394 g/mol
DrugBank ID:	-
Buried Surface Area:	75.72 %
Polar Surface area:	340.58 Å2

Number of
H-Bond Acceptors:	19
H-Bond Donors:	5
Rings:	5
Aromatic rings:	3
Anionic atoms:	3
Cationic atoms:	1
Rule of Five Violation:	2
Rotatable Bonds:	11

Mass center Coordinates

X	Y	Z
21.6944	127.571	22.0389

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
C4B	CD1	ILE- 7	4.29	0	Hydrophobic	false
O1N	OG1	THR- 10	2.85	155.44	H-Bond (Protein Donor)	false
O3A	N	THR- 10	3.42	142.26	H-Bond (Protein Donor)	false
O1A	N	THR- 10	2.89	149.57	H-Bond (Protein Donor)	false
O1A	N	PHE- 11	3.03	177.18	H-Bond (Protein Donor)	false
C1B	CD1	ILE- 21	3.84	0	Hydrophobic	false
O2M	ND2	ASN- 39	3.33	171.86	H-Bond (Protein Donor)	false
C3N	CG	PRO- 43	3.74	0	Hydrophobic	false
C4N	CB	PRO- 43	4.05	0	Hydrophobic	false
C5N	CB	HIS- 44	4.04	0	Hydrophobic	false
O1N	NZ	LYS- 45	2.73	155.64	H-Bond (Protein Donor)	false
O1N	NZ	LYS- 45	2.73	0	Ionic (Protein Cationic)	false
O2A	NZ	LYS- 45	3.29	0	Ionic (Protein Cationic)	false
O7N	N	THR- 85	2.95	157.72	H-Bond (Protein Donor)	false
C4M	CE2	PHE- 103	4.43	0	Hydrophobic	false
O3B	N	GLY- 106	3.1	158.05	H-Bond (Protein Donor)	false
O2P	N	GLY- 106	2.95	125.42	H-Bond (Protein Donor)	false
O2P	OD2	ASP- 108	2.64	143.91	H-Bond (Ligand Donor)	false
C5N	SD	MET- 109	4.02	0	Hydrophobic	false
C5M	CG	MET- 109	4.06	0	Hydrophobic	false
C3B	CG	MET- 109	4.07	0	Hydrophobic	false
C4M	CH2	TRP- 116	4.3	0	Hydrophobic	false
C3N	CB	TRP- 116	4.32	0	Hydrophobic	false
DuAr	DuAr	TRP- 116	3.75	0	Aromatic Face/Face	false
O8N	N	TYR- 117	2.85	167.8	H-Bond (Protein Donor)	false
N6A	O	PHE- 152	2.83	165.97	H-Bond (Ligand Donor)	false
N6A	O	VAL- 154	2.96	135.07	H-Bond (Ligand Donor)	false
O3M	O	HOH- 193	2.64	162.46	H-Bond (Protein Donor)	false
O3M	O	HOH- 198	3.43	161.04	H-Bond (Ligand Donor)	false
N1A	O	HOH- 202	2.82	179.96	H-Bond (Protein Donor)	false
O7N	O	HOH- 206	2.72	179.95	H-Bond (Protein Donor)	false