scPDB - 1u2r entry

Protein Data Bank Entry:

PDB ID : 1u2r

Resolution :2.600 Å

Experimental Method : X-ray

Deposition Date : 2004-07-20

Activity from ChEMBL: What is pChEMBL ?

	Min	Mean	Median	Standard Deviation	Max	Count
pChEMBL:

List of CHEMBLId :

Binding Site :

Uniprot Annotation

Name:	Elongation factor 2
ID:	EF2_YEAST
AC:	P32324
Organism:	Saccharomyces cerevisiae
Reign:	Eukaryota
TaxID:	559292
EC Number:	/

Chains:

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

Ligand binding site composition:

B-Factor:	37.628
Number of residues:	29
Including
Standard Amino Acids:	29
Non Standard Amino Acids:	0
Water Molecules:	0
Cofactors:
Metals:

Cavity properties

Ligandability	Volume (Å3)
1.111	624.375

% Hydrophobic	% Polar
54.05	45.95
According to VolSite

Ligand :

HET Code:	SO1
Formula:	C27H41O8
Molecular weight:	493.610 g/mol
DrugBank ID:	-
Buried Surface Area:	55.3 %
Polar Surface area:	125.35 Å2

Number of
H-Bond Acceptors:	8
H-Bond Donors:	2
Rings:	5
Aromatic rings:	0
Anionic atoms:	1
Cationic atoms:	0
Rule of Five Violation:	0
Rotatable Bonds:	7

Mass center Coordinates

X	Y	Z
72.8482	53.7322	18.0876

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
O60	NE2	GLN- 490	3.01	134.88	H-Bond (Protein Donor)	false
C65	CD2	LEU- 519	4.19	0	Hydrophobic	false
C61	CD2	LEU- 519	4.31	0	Hydrophobic	false
C8	CE1	TYR- 521	4.05	0	Hydrophobic	false
C52	CZ	TYR- 521	4.16	0	Hydrophobic	false
C21	CZ	TYR- 521	4.19	0	Hydrophobic	false
C56	CE2	TYR- 521	3.65	0	Hydrophobic	false
C21	CB	SER- 523	3.87	0	Hydrophobic	false
O14	N	GLU- 524	3.28	146.98	H-Bond (Protein Donor)	false
O15	N	GLU- 524	2.67	149.77	H-Bond (Protein Donor)	false
C24	CG	GLU- 524	4.47	0	Hydrophobic	false
C9	CB	GLU- 524	4.02	0	Hydrophobic	false
C21	CG1	ILE- 529	3.83	0	Hydrophobic	false
C20	CB	PRO- 559	3.76	0	Hydrophobic	false
O19	N	ALA- 562	2.85	161.54	H-Bond (Protein Donor)	false
C10	CB	PRO- 727	3.53	0	Hydrophobic	false
C6	CE1	PHE- 729	4.05	0	Hydrophobic	false
C53	CE1	PHE- 729	3.64	0	Hydrophobic	false
C20	CG1	VAL- 774	4.13	0	Hydrophobic	false
C10	CG2	VAL- 774	3.88	0	Hydrophobic	false
C6	CB	PHE- 798	4.39	0	Hydrophobic	false
C10	CD1	PHE- 798	4.06	0	Hydrophobic	false
C18	CE1	PHE- 798	4.26	0	Hydrophobic	false
C24	CE2	PHE- 798	4.16	0	Hydrophobic	false
C22	CD2	PHE- 798	3.78	0	Hydrophobic	false
C16	CG	PHE- 798	3.69	0	Hydrophobic	false
C7	CB	PHE- 798	3.94	0	Hydrophobic	false
O57	N	PHE- 798	2.92	160.79	H-Bond (Protein Donor)	false
C18	CZ2	TRP- 801	3.54	0	Hydrophobic	false