scPDB - 3tlk entry

Protein Data Bank Entry:

PDB ID : 3tlk

Resolution :1.850 Å

Experimental Method : X-ray

Deposition Date : 2011-08-30

Activity from ChEMBL: What is pChEMBL ?

	Min	Mean	Median	Standard Deviation	Max	Count
pChEMBL:

List of CHEMBLId :

Binding Site :

Uniprot Annotation

Name:	Ferrienterobactin-binding periplasmic protein
ID:	FEPB_ECOLI
AC:	P0AEL6
Organism:	Escherichia coli
Reign:	Bacteria
TaxID:	83333
EC Number:	/

Chains:

Chain Name:	Percentage of Residues within binding site
A	19 %
B	81 %

Ligand binding site composition:

B-Factor:	19.089
Number of residues:	45
Including
Standard Amino Acids:	40
Non Standard Amino Acids:	3
Water Molecules:	2
Cofactors:
Metals:	FE FE

Cavity properties

Ligandability	Volume (Å3)
0.308	2369.250

% Hydrophobic	% Polar
39.32	60.68
According to VolSite

Ligand :

HET Code:	EB4
Formula:	C30H27N3O15
Molecular weight:	669.546 g/mol
DrugBank ID:	-
Buried Surface Area:	61.47 %
Polar Surface area:	287.57 Å2

Number of
H-Bond Acceptors:	15
H-Bond Donors:	9
Rings:	4
Aromatic rings:	3
Anionic atoms:	0
Cationic atoms:	0
Rule of Five Violation:	3
Rotatable Bonds:	6

Mass center Coordinates

X	Y	Z
-7.35229	-24.0822	-25.4599

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
C10	CG1	VAL- 54	3.6	0	Hydrophobic	false
O7	OG1	THR- 73	3.47	120.89	H-Bond (Protein Donor)	false
C13	CG2	THR- 73	3.83	0	Hydrophobic	false
O7	ND2	ASN- 77	2.98	142.03	H-Bond (Protein Donor)	false
O4	N	GLY- 126	2.69	159.66	H-Bond (Protein Donor)	false
C7	CB	ASP- 127	3.73	0	Hydrophobic	false
C15	CG2	VAL- 198	3.83	0	Hydrophobic	false
C14	CB	ALA- 201	4.26	0	Hydrophobic	false
C29	CB	ALA- 202	3.48	0	Hydrophobic	false
O9	ND2	ASN- 207	3.05	159.91	H-Bond (Protein Donor)	false
C15	CB	ASN- 207	3.83	0	Hydrophobic	false
C12	CH2	TRP- 209	3.34	0	Hydrophobic	false
O6	NH2	ARG- 242	2.84	155.38	H-Bond (Protein Donor)	false
O5	NH1	ARG- 242	2.83	160.49	H-Bond (Protein Donor)	false
C12	CG2	ILE- 245	3.52	0	Hydrophobic	false
C11	CD	LYS- 270	3.35	0	Hydrophobic	false
C11	CB	ALA- 274	4.43	0	Hydrophobic	false
C16	CE2	PHE- 300	3.49	0	Hydrophobic	false
C3	CZ	PHE- 300	3.45	0	Hydrophobic	false
O6	NH2	ARG- 301	2.79	167.19	H-Bond (Protein Donor)	false
O6	FE	FE- 327	2.06	0	Metal Acceptor	false
O4	FE	FE- 327	2.13	0	Metal Acceptor	false
O5	FE	FE- 327	2.05	0	Metal Acceptor	false
O3	FE	FE- 327	2.18	0	Metal Acceptor	false
O1	FE	FE- 327	2.11	0	Metal Acceptor	false
O2	FE	FE- 327	2.1	0	Metal Acceptor	false
O8	O	HOH- 438	2.71	153.83	H-Bond (Protein Donor)	false