scPDB - 4xrg entry

Protein Data Bank Entry:

PDB ID : 4xrg

Resolution :1.300 Å

Experimental Method : X-ray

Deposition Date : 2015-01-21

Activity from ChEMBL: What is pChEMBL ?

	Min	Mean	Median	Standard Deviation	Max	Count
pChEMBL:

List of CHEMBLId :

Binding Site :

Uniprot Annotation

Name:	Homospermidine synthase
ID:	HSS_BLAVI
AC:	O32323
Organism:	Blastochloris viridis
Reign:	Bacteria
TaxID:	1079
EC Number:	2.5.1.44

Chains:

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

Ligand binding site composition:

B-Factor:	18.785
Number of residues:	55
Including
Standard Amino Acids:	51
Non Standard Amino Acids:	0
Water Molecules:	4
Cofactors:
Metals:

Cavity properties

Ligandability	Volume (Å3)
1.181	1194.750

% Hydrophobic	% Polar
47.74	52.26
According to VolSite

Ligand :

HET Code:	NAD
Formula:	C21H26N7O14P2
Molecular weight:	662.417 g/mol
DrugBank ID:	-
Buried Surface Area:	71.16 %
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
17.6114	21.9298	-10.0789

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
O2A	N	SER- 21	2.96	173.56	H-Bond (Protein Donor)	false
O2N	OG	SER- 21	2.67	149.02	H-Bond (Protein Donor)	false
O1N	N	ILE- 22	2.85	171.93	H-Bond (Protein Donor)	false
C5D	CG1	ILE- 22	4.11	0	Hydrophobic	false
C5N	CG1	ILE- 22	4	0	Hydrophobic	false
O3B	OD2	ASP- 45	2.59	145.12	H-Bond (Ligand Donor)	false
O3B	OD1	ASP- 45	3.44	155.78	H-Bond (Ligand Donor)	false
O2B	OD2	ASP- 45	3.46	126.94	H-Bond (Ligand Donor)	false
O2B	OD1	ASP- 45	2.68	147.33	H-Bond (Ligand Donor)	false
N6A	O	VAL- 66	2.98	162.2	H-Bond (Ligand Donor)	false
N1A	N	VAL- 66	3	160.76	H-Bond (Protein Donor)	false
O3D	O	SER- 92	2.87	163.6	H-Bond (Ligand Donor)	false
C5B	CG2	VAL- 93	4.02	0	Hydrophobic	false
C1B	CG2	VAL- 93	4.38	0	Hydrophobic	false
C3D	CG1	VAL- 93	3.73	0	Hydrophobic	false
C3N	CB	THR- 114	4.13	0	Hydrophobic	false
N7N	O	THR- 114	3	157.95	H-Bond (Ligand Donor)	false
O7N	N	ALA- 161	2.86	127.23	H-Bond (Protein Donor)	false
O7N	N	ASN- 162	2.94	169.96	H-Bond (Protein Donor)	false
N7N	O	PRO- 163	3.14	162.79	H-Bond (Ligand Donor)	false
C2D	CZ3	TRP- 229	4.12	0	Hydrophobic	false
C5N	CB	TRP- 229	4.37	0	Hydrophobic	false
O1A	OG	SER- 230	2.85	169.82	H-Bond (Protein Donor)	false
O2N	N	SER- 230	2.88	139.61	H-Bond (Protein Donor)	false
C2D	CB	SER- 230	4.32	0	Hydrophobic	false
C3N	CG1	VAL- 400	4.05	0	Hydrophobic	false
C4N	CG2	VAL- 400	3.41	0	Hydrophobic	false
O1N	O	HOH- 1070	2.64	179.96	H-Bond (Protein Donor)	false