scPDB - 3fap entry

Protein Data Bank Entry:

PDB ID : 3fap

Resolution :1.850 Å

Experimental Method : X-ray

Deposition Date : 1999-05-06

Activity from ChEMBL: What is pChEMBL ?

	Min	Mean	Median	Standard Deviation	Max	Count
pChEMBL:

List of CHEMBLId :

Binding Site :

Uniprot Annotation

Name:	Peptidyl-prolyl cis-trans isomerase FKBP1A	Serine/threonine-protein kinase mTOR
ID:	FKB1A_HUMAN	MTOR_HUMAN
AC:	P62942	P42345
Organism:	Homo sapiens
Reign:	Eukaryota
TaxID:	9606
EC Number:	5.2.1.8	2.7.11.1

Chains:

Chain Name:	Percentage of Residues within binding site
A	50 %
B	50 %

Ligand binding site composition:

B-Factor:	31.250
Number of residues:	44
Including
Standard Amino Acids:	44
Non Standard Amino Acids:	0
Water Molecules:	0
Cofactors:
Metals:

Cavity properties

Ligandability	Volume (Å3)
0.961	1410.750

% Hydrophobic	% Polar
43.06	56.94
According to VolSite

Ligand :

HET Code:	ARD
Formula:	C55H81NO12S
Molecular weight:	980.296 g/mol
DrugBank ID:	-
Buried Surface Area:	68.75 %
Polar Surface area:	214.44 Å2

Number of
H-Bond Acceptors:	12
H-Bond Donors:	3
Rings:	5
Aromatic rings:	1
Anionic atoms:	0
Cationic atoms:	0
Rule of Five Violation:	3
Rotatable Bonds:	6

Mass center Coordinates

X	Y	Z
-8.62957	26.5279	36.5199

Binding mode :

What is Poseview ?

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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
C5	CZ	TYR- 26	3.61	0	Hydrophobic	false
C42	CD1	PHE- 36	3.64	0	Hydrophobic	false
O6	OD2	ASP- 37	2.77	149.21	H-Bond (Ligand Donor)	false
C43	CE1	PHE- 46	3.77	0	Hydrophobic	false
C47	CZ	PHE- 46	4.03	0	Hydrophobic	false
C4	CE2	PHE- 46	3.64	0	Hydrophobic	false
O13	O	GLN- 53	2.57	159.06	H-Bond (Ligand Donor)	false
O10	O	GLU- 54	2.8	167.57	H-Bond (Ligand Donor)	false
C3	CB	VAL- 55	4.41	0	Hydrophobic	false
C4	CG1	VAL- 55	3.97	0	Hydrophobic	false
O2	N	ILE- 56	2.92	157.68	H-Bond (Protein Donor)	false
C3	CG1	ILE- 56	4.28	0	Hydrophobic	false
C41	CG2	ILE- 56	4.2	0	Hydrophobic	false
C3	CE2	TRP- 59	3.41	0	Hydrophobic	false
C4	CD2	TRP- 59	3.64	0	Hydrophobic	false
C5	CZ2	TRP- 59	4.03	0	Hydrophobic	false
C34	CE1	TYR- 82	4.12	0	Hydrophobic	false
C48	CZ	TYR- 82	3.99	0	Hydrophobic	false
C11	CD1	ILE- 90	3.88	0	Hydrophobic	false
C42	CG2	ILE- 90	3.95	0	Hydrophobic	false
C42	CD1	ILE- 91	3.82	0	Hydrophobic	false
C3	CZ	PHE- 99	4.38	0	Hydrophobic	false
C44	CB	LEU- 120	3.75	0	Hydrophobic	false
C50	CG	GLU- 121	4.25	0	Hydrophobic	false
C26	CB	SER- 124	4.46	0	Hydrophobic	false
C46	CB	SER- 124	4.27	0	Hydrophobic	false
C23	CB	SER- 124	4.12	0	Hydrophobic	false
C50	CB	ARG- 125	4.31	0	Hydrophobic	false
C51	CG	ARG- 125	4.48	0	Hydrophobic	false
C12	CE1	PHE- 128	3.95	0	Hydrophobic	false
C14	CE1	PHE- 128	4.01	0	Hydrophobic	false
C46	CD2	PHE- 128	3.46	0	Hydrophobic	false
C48	CD1	PHE- 128	3.85	0	Hydrophobic	false
C37	CB	PHE- 128	3.85	0	Hydrophobic	false
C35	CB	PHE- 128	3.75	0	Hydrophobic	false
C55	CB	THR- 187	4.41	0	Hydrophobic	false
S1	CB	THR- 187	4.08	0	Hydrophobic	false
C12	CG2	THR- 187	4.21	0	Hydrophobic	false
C44	CZ3	TRP- 190	4.05	0	Hydrophobic	false
C55	CB	ASP- 191	3.53	0	Hydrophobic	false
S1	CB	ASP- 191	3.92	0	Hydrophobic	false
C43	CD2	TYR- 194	4.04	0	Hydrophobic	false
C22	CD1	TYR- 194	3.87	0	Hydrophobic	false
C45	CE1	TYR- 194	3.68	0	Hydrophobic	false
C47	CZ	TYR- 194	3.71	0	Hydrophobic	false
C22	CD2	PHE- 197	3.92	0	Hydrophobic	false
C44	CG	PHE- 197	3.46	0	Hydrophobic	false
C23	CE2	PHE- 197	4.03	0	Hydrophobic	false
C45	CE2	PHE- 197	3.9	0	Hydrophobic	false