scPDB - 3e33 entry

Protein Data Bank Entry:

PDB ID : 3e33

Resolution :1.900 Å

Experimental Method : X-ray

Deposition Date : 2008-08-06

Activity from ChEMBL: What is pChEMBL ?

	Min	Mean	Median	Standard Deviation	Max	Count
pChEMBL:

List of CHEMBLId :

Binding Site :

Uniprot Annotation

Name:	Protein farnesyltransferase subunit beta
ID:	FNTB_RAT
AC:	Q02293
Organism:	Rattus norvegicus
Reign:	Eukaryota
TaxID:	10116
EC Number:	2.5.1.58

Chains:

Chain Name:	Percentage of Residues within binding site
A	8 %
B	92 %

Ligand binding site composition:

B-Factor:	22.484
Number of residues:	27
Including
Standard Amino Acids:	24
Non Standard Amino Acids:	1
Water Molecules:	2
Cofactors:
Metals:	ZN

Cavity properties

Ligandability	Volume (Å3)
0.690	992.250

% Hydrophobic	% Polar
39.12	60.88
According to VolSite

Ligand :

HET Code:	ED7
Formula:	C28H29N5O2S
Molecular weight:	499.627 g/mol
DrugBank ID:	-
Buried Surface Area:	57.79 %
Polar Surface area:	90.6 Å2

Number of
H-Bond Acceptors:	5
H-Bond Donors:	0
Rings:	4
Aromatic rings:	4
Anionic atoms:	0
Cationic atoms:	0
Rule of Five Violation:	0
Rotatable Bonds:	10

Mass center Coordinates

X	Y	Z
-69.2274	-20.0819	2.31697

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
CAK	CD2	LEU- 96	4.15	0	Hydrophobic	false
CAP	CD1	LEU- 96	3.97	0	Hydrophobic	false
CAK	CB	SER- 99	4.49	0	Hydrophobic	false
CAJ	CB	TRP- 102	4.5	0	Hydrophobic	false
CAI	SG	CYS- 299	4.04	0	Hydrophobic	false
CAO	CB	ASP- 359	4.3	0	Hydrophobic	false
CAA	CE1	TYR- 361	4	0	Hydrophobic	false
CAW	CE1	TYR- 361	4.22	0	Hydrophobic	false
CBB	CB	TYR- 361	3.27	0	Hydrophobic	false
NAC	N	TYR- 361	3.39	159.03	H-Bond (Protein Donor)	false
NAZ	ZN	ZN- 1001	2.04	0	Metal Acceptor	false
DuAr	ZN	ZN- 1001	3.15	84.37	Pi/Cation	false