scPDB - 1uxy entry

Protein Data Bank Entry:

PDB ID : 1uxy

Resolution :1.800 Å

Experimental Method : X-ray

Deposition Date : 1996-11-08

Activity from ChEMBL: What is pChEMBL ?

	Min	Mean	Median	Standard Deviation	Max	Count
pChEMBL:

List of CHEMBLId :

Binding Site :

Uniprot Annotation

Name:	UDP-N-acetylenolpyruvoylglucosamine reductase
ID:	MURB_ECOLI
AC:	P08373
Organism:	Escherichia coli
Reign:	Bacteria
TaxID:	83333
EC Number:	1.3.1.98

Chains:

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

Ligand binding site composition:

B-Factor:	17.402
Number of residues:	43
Including
Standard Amino Acids:	41
Non Standard Amino Acids:	1
Water Molecules:	1
Cofactors:	FAD
Metals:

Cavity properties

Ligandability	Volume (Å3)
0.401	691.875

% Hydrophobic	% Polar
38.54	61.46
According to VolSite

Ligand :

HET Code:	EPU
Formula:	C20H26N3O19P2
Molecular weight:	674.377 g/mol
DrugBank ID:	-
Buried Surface Area:	65.15 %
Polar Surface area:	354.82 Å2

Number of
H-Bond Acceptors:	19
H-Bond Donors:	6
Rings:	3
Aromatic rings:	0
Anionic atoms:	3
Cationic atoms:	0
Rule of Five Violation:	3
Rotatable Bonds:	13

Mass center Coordinates

X	Y	Z
10.8919	20.4291	13.7024

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
C4	CB	ALA- 124	4.08	0	Hydrophobic	false
C6	CB	ALA- 124	4.18	0	Hydrophobic	false
C6	CZ	TYR- 125	3.89	0	Hydrophobic	false
O6	N	TYR- 125	2.8	161.49	H-Bond (Protein Donor)	false
C8	CZ	TYR- 158	4.34	0	Hydrophobic	false
O3	NH2	ARG- 159	3.1	127.76	H-Bond (Protein Donor)	false
O2E	NE	ARG- 159	3.25	138.31	H-Bond (Protein Donor)	false
O2E	NH2	ARG- 159	2.88	152.99	H-Bond (Protein Donor)	false
C6	CZ	TYR- 190	3.9	0	Hydrophobic	false
C8	CB	ALA- 229	3.75	0	Hydrophobic	false
O1E	N	ALA- 229	2.84	144.48	H-Bond (Protein Donor)	false
O1B	ND2	ASN- 233	2.76	156.77	H-Bond (Protein Donor)	false
C1D	CG	PRO- 252	4.47	0	Hydrophobic	false
C3D	CG	PRO- 252	4.38	0	Hydrophobic	false
C4D	CB	PRO- 252	4.07	0	Hydrophobic	false
C4D	CB	ALA- 264	3.6	0	Hydrophobic	false
C1D	CB	TRP- 267	4.06	0	Hydrophobic	false
N3U	OD2	ASP- 270	2.88	178.01	H-Bond (Ligand Donor)	false
O2A	NE2	GLN- 288	2.76	129.05	H-Bond (Protein Donor)	false
O2B	NE2	GLN- 288	2.74	147.42	H-Bond (Protein Donor)	false
O4U	N	ALA- 289	2.85	166.51	H-Bond (Protein Donor)	false
C8	CD2	LEU- 290	3.74	0	Hydrophobic	false
O2E	OE2	GLU- 325	2.69	152.74	H-Bond (Ligand Donor)	false
O4	O4	FAD- 401	2.91	170.13	H-Bond (Ligand Donor)	false
O2B	O	HOH- 694	2.58	179.96	H-Bond (Protein Donor)	false