scPDB - 4fc0 entry

Protein Data Bank Entry:

PDB ID : 4fc0

Resolution :2.950 Å

Experimental Method : X-ray

Deposition Date : 2012-05-23

Activity from ChEMBL: What is pChEMBL ?

	Min	Mean	Median	Standard Deviation	Max	Count
pChEMBL:

List of CHEMBLId :

Binding Site :

Uniprot Annotation

Name:	Serine/threonine-protein kinase B-raf
ID:	BRAF_HUMAN
AC:	P15056
Organism:	Homo sapiens
Reign:	Eukaryota
TaxID:	9606
EC Number:	2.7.11.1

Chains:

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

Ligand binding site composition:

B-Factor:	25.911
Number of residues:	36
Including
Standard Amino Acids:	36
Non Standard Amino Acids:	0
Water Molecules:	0
Cofactors:
Metals:

Cavity properties

Ligandability	Volume (Å3)
1.433	793.125

% Hydrophobic	% Polar
62.13	37.87
According to VolSite

Ligand :

HET Code:	0T2
Formula:	C28H24ClFN6O3S
Molecular weight:	579.045 g/mol
DrugBank ID:	-
Buried Surface Area:	62.05 %
Polar Surface area:	148.47 Å2

Number of
H-Bond Acceptors:	7
H-Bond Donors:	2
Rings:	5
Aromatic rings:	4
Anionic atoms:	0
Cationic atoms:	0
Rule of Five Violation:	2
Rotatable Bonds:	8

Mass center Coordinates

X	Y	Z
44.8194	-35.5889	7.38337

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
S38	CG2	ILE- 462	4.34	0	Hydrophobic	false
C1	CG2	VAL- 470	4.15	0	Hydrophobic	false
C4	CG2	VAL- 470	4.39	0	Hydrophobic	false
C4	CB	ALA- 480	4.48	0	Hydrophobic	false
C28	CB	ALA- 480	3.54	0	Hydrophobic	false
C6	CD	LYS- 482	4.17	0	Hydrophobic	false
C25	CD	LYS- 482	4.42	0	Hydrophobic	false
C5	CB	LYS- 482	3.53	0	Hydrophobic	false
N9	OE2	GLU- 500	2.75	155.2	H-Bond (Ligand Donor)	false
C14	CG	GLU- 500	3.63	0	Hydrophobic	false
C16	CG1	VAL- 503	4.41	0	Hydrophobic	false
C20	CG1	VAL- 503	3.52	0	Hydrophobic	false
CL2	CD2	LEU- 504	3.28	0	Hydrophobic	false
F7	CD1	LEU- 504	3.51	0	Hydrophobic	false
C23	CD2	LEU- 504	3.9	0	Hydrophobic	false
CL2	CD2	LEU- 513	4.47	0	Hydrophobic	false
C27	CD2	LEU- 513	3.83	0	Hydrophobic	false
C28	CD1	LEU- 513	3.99	0	Hydrophobic	false
C25	CD2	LEU- 513	3.93	0	Hydrophobic	false
C5	CB	ILE- 526	4.48	0	Hydrophobic	false
F7	CG2	ILE- 526	3.3	0	Hydrophobic	false
C27	CB	THR- 528	4.46	0	Hydrophobic	false
C5	CG2	THR- 528	3.32	0	Hydrophobic	false
C5	CG2	THR- 528	3.32	0	Hydrophobic	false
S38	CZ3	TRP- 530	4.06	0	Hydrophobic	false
C35	CZ2	TRP- 530	3.44	0	Hydrophobic	false
C28	SG	CYS- 531	3.97	0	Hydrophobic	false
N30	N	CYS- 531	3.08	151.9	H-Bond (Protein Donor)	false
N32	O	CYS- 531	2.56	146.67	H-Bond (Ligand Donor)	false
C20	CD2	LEU- 566	3.95	0	Hydrophobic	false
C20	CG2	ILE- 571	3.77	0	Hydrophobic	false
C37	CZ	PHE- 582	3.97	0	Hydrophobic	false
O11	N	ASP- 593	2.91	158.36	H-Bond (Protein Donor)	false
C13	CB	ASP- 593	3.68	0	Hydrophobic	false
C1	CD2	PHE- 594	3.73	0	Hydrophobic	false