scPDB - 3e2s entry

Protein Data Bank Entry:

PDB ID : 3e2s

Resolution :2.000 Å

Experimental Method : X-ray

Deposition Date : 2008-08-06

Activity from ChEMBL: What is pChEMBL ?

	Min	Mean	Median	Standard Deviation	Max	Count
pChEMBL:

List of CHEMBLId :

Binding Site :

Uniprot Annotation

Name:	Bifunctional protein PutA
ID:	PUTA_ECOLI
AC:	P09546
Organism:	Escherichia coli
Reign:	Bacteria
TaxID:	83333
EC Number:	1.5.5.2

Chains:

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

Ligand binding site composition:

B-Factor:	22.058
Number of residues:	58
Including
Standard Amino Acids:	53
Non Standard Amino Acids:	0
Water Molecules:	5
Cofactors:
Metals:

Cavity properties

Ligandability	Volume (Å3)
1.121	860.625

% Hydrophobic	% Polar
50.98	49.02
According to VolSite

Ligand :

HET Code:	FAD
Formula:	C27H31N9O15P2
Molecular weight:	783.534 g/mol
DrugBank ID:	DB03147
Buried Surface Area:	76.53 %
Polar Surface area:	381.7 Å2

Number of
H-Bond Acceptors:	22
H-Bond Donors:	7
Rings:	6
Aromatic rings:	3
Anionic atoms:	2
Cationic atoms:	0
Rule of Five Violation:	3
Rotatable Bonds:	13

Mass center Coordinates

X	Y	Z
4.10098	45.9046	46.4655

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
N5	N	PRO- 1	3.24	162.09	H-Bond (Protein Donor)	false
C6	CG	PRO- 1	4.11	0	Hydrophobic	false
C1'	CB	PRO- 1	4.23	0	Hydrophobic	false
C9A	CB	PRO- 1	3.77	0	Hydrophobic	false
N3	O	ALA- 371	2.84	153.37	H-Bond (Ligand Donor)	false
O4	N	ALA- 371	2.95	146.72	H-Bond (Protein Donor)	false
O2	NE2	GLN- 404	2.89	168.27	H-Bond (Protein Donor)	false
C2B	CD2	TYR- 406	4.19	0	Hydrophobic	false
C6	CG1	VAL- 433	4.29	0	Hydrophobic	false
C1'	CB	VAL- 433	4.3	0	Hydrophobic	false
C9A	CG1	VAL- 433	3.61	0	Hydrophobic	false
O2A	NZ	LYS- 434	2.93	153.23	H-Bond (Protein Donor)	false
O2A	NZ	LYS- 434	2.93	0	Ionic (Protein Cationic)	false
O1P	NZ	LYS- 434	2.89	0	Ionic (Protein Cationic)	false
C5B	CD	LYS- 434	4.39	0	Hydrophobic	false
C2B	CB	LYS- 434	4.36	0	Hydrophobic	false
C4'	CB	LYS- 434	4.04	0	Hydrophobic	false
O2B	O	GLY- 435	2.57	167.56	H-Bond (Ligand Donor)	false
O4'	O	GLY- 435	3.02	124.5	H-Bond (Ligand Donor)	false
O2'	N	GLY- 435	2.82	123.84	H-Bond (Protein Donor)	false
O4'	N	GLY- 435	2.85	146.4	H-Bond (Protein Donor)	false
O2	N	ALA- 436	2.63	154.5	H-Bond (Protein Donor)	false
N6A	O	THR- 457	2.84	157.92	H-Bond (Ligand Donor)	false
O1A	NZ	LYS- 459	3.77	0	Ionic (Protein Cationic)	false
O2A	NZ	LYS- 459	2.87	0	Ionic (Protein Cationic)	false
O2A	NZ	LYS- 459	2.87	160.71	H-Bond (Protein Donor)	false
C1B	CG	LYS- 459	4.28	0	Hydrophobic	false
C1B	CG2	THR- 462	4.19	0	Hydrophobic	false
N3A	OG1	THR- 462	2.74	161.07	H-Bond (Protein Donor)	false
C7	CB	ALA- 485	4.1	0	Hydrophobic	false
C8	CB	ALA- 485	3.7	0	Hydrophobic	false
O1P	OG1	THR- 486	2.68	159.98	H-Bond (Protein Donor)	false
O2P	N	HIS- 487	2.73	159.02	H-Bond (Protein Donor)	false
O2A	ND2	ASN- 488	2.92	174.21	H-Bond (Protein Donor)	false
C7M	CB	GLN- 511	3.93	0	Hydrophobic	false
C8	CD2	LEU- 513	3.27	0	Hydrophobic	false
C7M	CB	SER- 540	3.38	0	Hydrophobic	false
O3'	OE2	GLU- 559	2.71	153.57	H-Bond (Ligand Donor)	false
O3'	OE1	GLU- 559	3.34	146.65	H-Bond (Ligand Donor)	false
O1A	N	PHE- 566	2.66	168.01	H-Bond (Protein Donor)	false
O5'	O	HOH- 2004	2.96	158.48	H-Bond (Protein Donor)	false