scPDB - 4qt3 entry

Protein Data Bank Entry:

PDB ID : 4qt3

Resolution :1.400 Å

Experimental Method : X-ray

Deposition Date : 2014-07-07

Activity from ChEMBL: What is pChEMBL ?

	Min	Mean	Median	Standard Deviation	Max	Count
pChEMBL:

List of CHEMBLId :

Binding Site :

Uniprot Annotation

Name:	Peptidylprolyl isomerase
ID:	Q8I4V8_PLAF7
AC:	Q8I4V8
Organism:	Plasmodium falciparum
Reign:	Eukaryota
TaxID:	36329
EC Number:	/

Chains:

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

Ligand binding site composition:

B-Factor:	18.354
Number of residues:	27
Including
Standard Amino Acids:	25
Non Standard Amino Acids:	0
Water Molecules:	2
Cofactors:
Metals:

Cavity properties

Ligandability	Volume (Å3)
0.436	290.250

% Hydrophobic	% Polar
45.35	54.65
According to VolSite

Ligand :

HET Code:	RAP
Formula:	C51H79NO13
Molecular weight:	914.172 g/mol
DrugBank ID:	DB00877
Buried Surface Area:	37.38 %
Polar Surface area:	195.42 Å2

Number of
H-Bond Acceptors:	13
H-Bond Donors:	3
Rings:	4
Aromatic rings:	0
Anionic atoms:	0
Cationic atoms:	0
Rule of Five Violation:	3
Rotatable Bonds:	6

Mass center Coordinates

X	Y	Z
12.3632	12.4466	-3.01445

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
C5	CZ	TYR- 44	3.56	0	Hydrophobic	false
C10	CE1	PHE- 55	4.46	0	Hydrophobic	false
C43	CE1	PHE- 55	3.89	0	Hydrophobic	false
C10	CB	ASP- 56	4.47	0	Hydrophobic	false
O6	OD2	ASP- 56	2.58	167.87	H-Bond (Ligand Donor)	false
C44	CE2	PHE- 59	4.02	0	Hydrophobic	false
C4	CE2	PHE- 65	3.69	0	Hydrophobic	false
C5	CZ	PHE- 65	3.76	0	Hydrophobic	false
C44	CE1	PHE- 65	4.14	0	Hydrophobic	false
C48	CZ	PHE- 65	3.86	0	Hydrophobic	false
O13	O	GLY- 72	3.23	161.31	H-Bond (Ligand Donor)	false
O10	O	GLU- 73	2.74	163.75	H-Bond (Ligand Donor)	false
C3	CB	VAL- 74	4.2	0	Hydrophobic	false
C4	CG1	VAL- 74	3.88	0	Hydrophobic	false
O2	N	ILE- 75	2.92	154.52	H-Bond (Protein Donor)	false
C3	CG1	ILE- 75	4.2	0	Hydrophobic	false
C42	CG2	ILE- 75	4.08	0	Hydrophobic	false
C3	CE2	TRP- 78	3.49	0	Hydrophobic	false
C4	CD2	TRP- 78	3.65	0	Hydrophobic	false
C5	CZ2	TRP- 78	3.89	0	Hydrophobic	false
O3	OH	TYR- 101	2.66	177.42	H-Bond (Protein Donor)	false
C42	CE1	TYR- 101	4.4	0	Hydrophobic	false
C43	CE2	TYR- 101	4.42	0	Hydrophobic	false
C49	CE1	TYR- 101	3.88	0	Hydrophobic	false
C49	SG	CYS- 106	4.17	0	Hydrophobic	false
C12	SG	CYS- 106	4.06	0	Hydrophobic	false
C43	CD1	ILE- 110	3.57	0	Hydrophobic	false