scPDB - 1o1s entry

Protein Data Bank Entry:

PDB ID : 1o1s

Resolution :2.300 Å

Experimental Method : X-ray

Deposition Date : 2003-01-14

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	24 %
B	76 %

Ligand binding site composition:

B-Factor:	26.365
Number of residues:	45
Including
Standard Amino Acids:	41
Non Standard Amino Acids:	1
Water Molecules:	3
Cofactors:
Metals:	ZN

Cavity properties

Ligandability	Volume (Å3)
0.538	931.500

% Hydrophobic	% Polar
39.13	60.87
According to VolSite

Ligand :

HET Code:	1NH
Formula:	C24H27O9P2
Molecular weight:	521.413 g/mol
DrugBank ID:	-
Buried Surface Area:	52.05 %
Polar Surface area:	167.7 Å2

Number of
H-Bond Acceptors:	9
H-Bond Donors:	0
Rings:	2
Aromatic rings:	2
Anionic atoms:	3
Cationic atoms:	0
Rule of Five Violation:	1
Rotatable Bonds:	14

Mass center Coordinates

X	Y	Z
189.663	123.518	31.2069

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
C13	CZ2	TRP- 102	3.33	0	Hydrophobic	false
C19	CB	ALA- 151	4.18	0	Hydrophobic	false
C22	CB	ALA- 151	4.19	0	Hydrophobic	false
C13	CB	ALA- 151	3.76	0	Hydrophobic	false
O7	NZ	LYS- 164	2.86	166.49	H-Bond (Protein Donor)	false
O7	NZ	LYS- 164	2.86	0	Ionic (Protein Cationic)	false
O1	NZ	LYS- 164	3.57	0	Ionic (Protein Cationic)	false
C4	CZ	TYR- 166	4.47	0	Hydrophobic	false
C23	CE	MET- 193	3.69	0	Hydrophobic	false
C4	CB	TYR- 200	3.88	0	Hydrophobic	false
C10	CB	TYR- 200	4.18	0	Hydrophobic	false
C9	CD	ARG- 202	4.32	0	Hydrophobic	false
C18	CG	ARG- 202	4.36	0	Hydrophobic	false
C12	CB	ARG- 202	4.32	0	Hydrophobic	false
C16	CD	ARG- 202	3.8	0	Hydrophobic	false
C14	CD	ARG- 202	3.82	0	Hydrophobic	false
C12	SG	CYS- 206	3.67	0	Hydrophobic	false
O5	NE2	HIS- 248	2.83	145.86	H-Bond (Protein Donor)	false
C3	CE1	TYR- 251	3.58	0	Hydrophobic	false
C9	SG	CYS- 254	4.45	0	Hydrophobic	false
C11	SG	CYS- 254	3.82	0	Hydrophobic	false
O1	CZ	ARG- 291	3.77	0	Ionic (Protein Cationic)	false
O5	CZ	ARG- 291	3.53	0	Ionic (Protein Cationic)	false
O1	NH2	ARG- 291	2.58	136.4	H-Bond (Protein Donor)	false
O5	NE	ARG- 291	2.73	172.62	H-Bond (Protein Donor)	false
O5	NH2	ARG- 291	3.48	128.27	H-Bond (Protein Donor)	false
O1	NZ	LYS- 294	3.51	0	Ionic (Protein Cationic)	false
O6	NZ	LYS- 294	2.61	0	Ionic (Protein Cationic)	false
O6	NZ	LYS- 294	2.61	148.06	H-Bond (Protein Donor)	false
O4	OH	TYR- 300	2.72	149.32	H-Bond (Protein Donor)	false
C8	CE2	TRP- 303	4.18	0	Hydrophobic	false
C11	CZ2	TRP- 303	3.48	0	Hydrophobic	false
O4	O	HOH- 2009	2.75	158.19	H-Bond (Protein Donor)	false