scPDB - 3ijr entry

Protein Data Bank Entry:

PDB ID : 3ijr

Resolution :2.050 Å

Experimental Method : X-ray

Deposition Date : 2009-08-04

Activity from ChEMBL: What is pChEMBL ?

	Min	Mean	Median	Standard Deviation	Max	Count
pChEMBL:

List of CHEMBLId :

Binding Site :

Uniprot Annotation

Name:	Oxidoreductase, short chain dehydrogenase/reductase family
ID:	Q81UV8_BACAN
AC:	Q81UV8
Organism:	Bacillus anthracis
Reign:	Bacteria
TaxID:	1392
EC Number:	/

Chains:

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

Ligand binding site composition:

B-Factor:	14.259
Number of residues:	62
Including
Standard Amino Acids:	58
Non Standard Amino Acids:	1
Water Molecules:	3
Cofactors:
Metals:	MG

Cavity properties

Ligandability	Volume (Å3)
1.117	928.125

% Hydrophobic	% Polar
46.55	53.45
According to VolSite

Ligand :

HET Code:	NAD
Formula:	C21H26N7O14P2
Molecular weight:	662.417 g/mol
DrugBank ID:	-
Buried Surface Area:	84.38 %
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
-74.74	42.3248	-43.6736

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
C2B	CB	PRO- 19	4.01	0	Hydrophobic	false
O3B	OD1	ASP- 53	2.6	131.81	H-Bond (Ligand Donor)	false
O2A	OG	SER- 54	2.63	154.48	H-Bond (Protein Donor)	false
O2N	N	ILE- 56	2.87	155.68	H-Bond (Protein Donor)	false
C5D	CB	ILE- 56	4.49	0	Hydrophobic	false
O2B	N	LEU- 76	3.38	163.79	H-Bond (Protein Donor)	false
O2B	OE1	GLU- 78	3.14	122.98	H-Bond (Ligand Donor)	false
N6A	OD1	ASP- 102	2.82	164.08	H-Bond (Ligand Donor)	false
N1A	N	LEU- 103	2.75	177.43	H-Bond (Protein Donor)	false
C1B	CG1	VAL- 130	3.73	0	Hydrophobic	false
O4B	N	ALA- 131	3.45	156.9	H-Bond (Protein Donor)	false
C3D	CB	ALA- 131	3.3	0	Hydrophobic	false
N7A	NE2	GLN- 132	3.1	134.94	H-Bond (Protein Donor)	false
C4D	CG2	THR- 178	3.79	0	Hydrophobic	false
C5N	CB	SER- 180	3.51	0	Hydrophobic	false
O2D	OH	TYR- 193	2.75	140.87	H-Bond (Protein Donor)	false
O3D	NZ	LYS- 197	3	140.02	H-Bond (Protein Donor)	false
O2D	NZ	LYS- 197	2.61	139.38	H-Bond (Protein Donor)	false
C5N	CB	PRO- 223	3.86	0	Hydrophobic	false
O7N	N	ILE- 226	2.92	160.05	H-Bond (Protein Donor)	false
N7N	O	ILE- 226	2.99	136.29	H-Bond (Ligand Donor)	false
O1N	OG1	THR- 228	2.56	172.84	H-Bond (Protein Donor)	false
C2D	CD2	LEU- 230	4	0	Hydrophobic	false
C3N	CD2	LEU- 230	4.39	0	Hydrophobic	false
O3B	MG	MG- 300	2.31	0	Metal Acceptor	false
O5B	O	HOH- 384	2.92	131.59	H-Bond (Protein Donor)	false