scPDB - 1z7e entry

Protein Data Bank Entry:

PDB ID : 1z7e

Resolution :3.000 Å

Experimental Method : X-ray

Deposition Date : 2005-03-24

Activity from ChEMBL: What is pChEMBL ?

	Min	Mean	Median	Standard Deviation	Max	Count
pChEMBL:

List of CHEMBLId :

Binding Site :

Uniprot Annotation

Name:	Bifunctional polymyxin resistance protein ArnA
ID:	ARNA_ECOLI
AC:	P77398
Organism:	Escherichia coli
Reign:	Bacteria
TaxID:	83333
EC Number:	/

Chains:

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

Ligand binding site composition:

B-Factor:	31.546
Number of residues:	46
Including
Standard Amino Acids:	45
Non Standard Amino Acids:	1
Water Molecules:	0
Cofactors:	ATP
Metals:

Cavity properties

Ligandability	Volume (Å3)
0.569	820.125

% Hydrophobic	% Polar
35.80	64.20
According to VolSite

Ligand :

HET Code:	UGA
Formula:	C15H19N2O18P2
Molecular weight:	577.261 g/mol
DrugBank ID:	DB03041
Buried Surface Area:	76.06 %
Polar Surface area:	336.72 Å2

Number of
H-Bond Acceptors:	18
H-Bond Donors:	6
Rings:	3
Aromatic rings:	0
Anionic atoms:	3
Cationic atoms:	0
Rule of Five Violation:	3
Rotatable Bonds:	9

Mass center Coordinates

X	Y	Z
125.471	25.781	99.5979

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
C1'	CG	PRO- 395	4.13	0	Hydrophobic	false
O2'	OH	TYR- 398	2.77	135.21	H-Bond (Protein Donor)	false
O3'	OH	TYR- 398	3.32	137.04	H-Bond (Protein Donor)	false
O'Q	OG	SER- 433	2.81	133.56	H-Bond (Protein Donor)	false
O2'	OE2	GLU- 434	3.32	171.82	H-Bond (Ligand Donor)	false
C3'	CB	GLU- 434	4.28	0	Hydrophobic	false
O2B	CZ	ARG- 460	3.79	0	Ionic (Protein Cationic)	false
O2B	NH2	ARG- 460	3.12	159.91	H-Bond (Protein Donor)	false
C3'	CE2	TYR- 463	4.02	0	Hydrophobic	false
O'Q	N	ASN- 492	2.68	162.94	H-Bond (Protein Donor)	false
O1B	ND2	ASN- 492	2.66	148.64	H-Bond (Protein Donor)	false
C1'	CD	ARG- 510	4.06	0	Hydrophobic	false
O1A	N	ALA- 511	3.47	132.29	H-Bond (Protein Donor)	false
C5D	CB	ALA- 511	4.05	0	Hydrophobic	false
N3	O	LYS- 526	2.83	168.2	H-Bond (Ligand Donor)	false
O2	N	ILE- 528	2.78	144.81	H-Bond (Protein Donor)	false
C2D	CB	ILE- 528	4.06	0	Hydrophobic	false
O2D	NE2	GLN- 533	2.85	128.64	H-Bond (Protein Donor)	false
O1B	NE	ARG- 535	3.24	160.78	H-Bond (Protein Donor)	false
O2B	NH2	ARG- 535	3.15	162.9	H-Bond (Protein Donor)	false
O2B	CZ	ARG- 535	3.86	0	Ionic (Protein Cationic)	false
C5D	CD1	ILE- 574	4.06	0	Hydrophobic	false
C4D	CG1	ILE- 574	3.92	0	Hydrophobic	false
C1D	CG1	ILE- 574	3.8	0	Hydrophobic	false
C3D	CZ	TYR- 609	4.43	0	Hydrophobic	false
C2D	CE1	TYR- 609	4.16	0	Hydrophobic	false
O1B	NH1	ARG- 619	3.36	122.81	H-Bond (Protein Donor)	false