scPDB - 4wso entry

Protein Data Bank Entry:

PDB ID : 4wso

Resolution :2.050 Å

Experimental Method : X-ray

Deposition Date : 2014-10-28

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:	Q2SZT3_BURTA
AC:	Q2SZT3
Organism:	Burkholderia thailandensis
Reign:	Bacteria
TaxID:	271848
EC Number:	/

Chains:

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

Ligand binding site composition:

B-Factor:	20.658
Number of residues:	57
Including
Standard Amino Acids:	53
Non Standard Amino Acids:	0
Water Molecules:	4
Cofactors:
Metals:

Cavity properties

Ligandability	Volume (Å3)
0.633	823.500

% Hydrophobic	% Polar
38.93	61.07
According to VolSite

Ligand :

HET Code:	NAD
Formula:	C21H26N7O14P2
Molecular weight:	662.417 g/mol
DrugBank ID:	-
Buried Surface Area:	69.84 %
Polar Surface area:	343.54 Å2

Number of
H-Bond Acceptors:	18
H-Bond Donors:	6
Rings:	5
Aromatic rings:	3
Anionic atoms:	2
Cationic atoms:	1
Rule of Five Violation:	3
Rotatable Bonds:	11

Mass center Coordinates

X	Y	Z
35.7533	52.2478	22.1067

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	CD2	LEU- 34	4.09	0	Hydrophobic	false
O3	N	THR- 37	3.03	158.09	H-Bond (Protein Donor)	false
O1N	OG1	THR- 37	2.62	155.39	H-Bond (Protein Donor)	false
O1A	N	PHE- 38	2.87	173.12	H-Bond (Protein Donor)	false
C5B	CE1	PHE- 38	4.36	0	Hydrophobic	false
O5B	NE2	HIS- 45	3.23	123.41	H-Bond (Protein Donor)	false
C4B	CD2	LEU- 48	4.37	0	Hydrophobic	false
C1B	CD2	LEU- 48	3.75	0	Hydrophobic	false
C5N	CG	GLN- 71	4.09	0	Hydrophobic	false
O2A	NZ	LYS- 72	2.69	0	Ionic (Protein Cationic)	false
O1N	NZ	LYS- 72	2.89	0	Ionic (Protein Cationic)	false
O2N	NZ	LYS- 72	3.92	0	Ionic (Protein Cationic)	false
O1N	NZ	LYS- 72	2.89	148.35	H-Bond (Protein Donor)	false
O7N	N	THR- 114	2.95	164.01	H-Bond (Protein Donor)	false
O3B	N	GLY- 136	3.2	147.89	H-Bond (Protein Donor)	false
O2B	N	GLY- 136	3.02	120.58	H-Bond (Protein Donor)	false
O2B	OD1	ASP- 138	2.73	159.82	H-Bond (Ligand Donor)	false
O2B	OD2	ASP- 138	3.46	120.59	H-Bond (Ligand Donor)	false
C3B	CG	GLN- 139	4.22	0	Hydrophobic	false
C5D	CG	GLN- 139	4.31	0	Hydrophobic	false
O2N	NE2	GLN- 139	2.75	146.1	H-Bond (Protein Donor)	false
C4D	CH2	TRP- 146	4.19	0	Hydrophobic	false
C3N	CB	TRP- 146	4.02	0	Hydrophobic	false
N6A	O	LEU- 205	2.83	156.25	H-Bond (Ligand Donor)	false
N6A	O	VAL- 207	3.36	161.73	H-Bond (Ligand Donor)	false
O7N	O	HOH- 454	2.56	160.31	H-Bond (Protein Donor)	false
N1A	O	HOH- 467	2.83	179.97	H-Bond (Protein Donor)	false