scPDB - 1f3l entry

Protein Data Bank Entry:

PDB ID : 1f3l

Resolution :2.030 Å

Experimental Method : X-ray

Deposition Date : 2000-06-05

Activity from ChEMBL: What is pChEMBL ?

	Min	Mean	Median	Standard Deviation	Max	Count
pChEMBL:

List of CHEMBLId :

Binding Site :

Uniprot Annotation

Name:	Protein arginine N-methyltransferase 3
ID:	ANM3_RAT
AC:	O70467
Organism:	Rattus norvegicus
Reign:	Eukaryota
TaxID:	10116
EC Number:	/

Chains:

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

Ligand binding site composition:

B-Factor:	24.964
Number of residues:	40
Including
Standard Amino Acids:	37
Non Standard Amino Acids:	0
Water Molecules:	3
Cofactors:
Metals:

Cavity properties

Ligandability	Volume (Å3)
0.374	307.125

% Hydrophobic	% Polar
53.85	46.15
According to VolSite

Ligand :

HET Code:	SAH
Formula:	C14H20N6O5S
Molecular weight:	384.411 g/mol
DrugBank ID:	DB01752
Buried Surface Area:	75.69 %
Polar Surface area:	212.38 Å2

Number of
H-Bond Acceptors:	10
H-Bond Donors:	4
Rings:	3
Aromatic rings:	2
Anionic atoms:	1
Cationic atoms:	1
Rule of Five Violation:	1
Rotatable Bonds:	7

Mass center Coordinates

X	Y	Z
68.2369	48.2948	219.07

Binding mode :

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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
N	O	HOH- 42	2.95	174.17	H-Bond (Ligand Donor)	false
OXT	O	HOH- 43	2.65	179.98	H-Bond (Protein Donor)	false
C2'	CE2	PHE- 218	4.41	0	Hydrophobic	false
C3'	CD2	TYR- 221	3.43	0	Hydrophobic	false
C2'	CD1	TYR- 221	3.71	0	Hydrophobic	false
SD	CE2	TYR- 221	3.79	0	Hydrophobic	false
CB	SD	MET- 230	4.46	0	Hydrophobic	false
SD	CE	MET- 230	3.28	0	Hydrophobic	false
O	NH1	ARG- 236	3.01	162.88	H-Bond (Protein Donor)	false
O	NH2	ARG- 236	3.47	137.05	H-Bond (Protein Donor)	false
OXT	NH2	ARG- 236	3.08	151.85	H-Bond (Protein Donor)	false
O	CZ	ARG- 236	3.7	0	Ionic (Protein Cationic)	false
OXT	CZ	ARG- 236	3.89	0	Ionic (Protein Cationic)	false
N	O	GLY- 260	2.91	176.68	H-Bond (Ligand Donor)	false
O3'	OD2	ASP- 282	2.59	149.34	H-Bond (Ligand Donor)	false
O3'	OD1	ASP- 282	3.23	128.92	H-Bond (Ligand Donor)	false
O2'	OD1	ASP- 282	2.96	152.84	H-Bond (Ligand Donor)	false
O2'	OG	SER- 284	3.05	150.24	H-Bond (Protein Donor)	false
N1	N	ILE- 310	3.13	170.28	H-Bond (Protein Donor)	false
N6	OE2	GLU- 311	2.79	136.4	H-Bond (Ligand Donor)	false
CG	CB	GLU- 326	4.44	0	Hydrophobic	false
C5'	SD	MET- 337	3.79	0	Hydrophobic	false
C4'	CE	MET- 337	4.38	0	Hydrophobic	false
C1'	CE	MET- 337	4.3	0	Hydrophobic	false
N6	OG	SER- 340	3.46	121.29	H-Bond (Ligand Donor)	false