scPDB - 1nai entry

Protein Data Bank Entry:

PDB ID : 1nai

Resolution :2.000 Å

Experimental Method : X-ray

Deposition Date : 1995-11-22

Activity from ChEMBL: What is pChEMBL ?

	Min	Mean	Median	Standard Deviation	Max	Count
pChEMBL:

List of CHEMBLId :

Binding Site :

Uniprot Annotation

Name:	UDP-glucose 4-epimerase
ID:	GALE_ECOLI
AC:	P09147
Organism:	Escherichia coli
Reign:	Bacteria
TaxID:	83333
EC Number:	5.1.3.2

Chains:

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

Ligand binding site composition:

B-Factor:	22.739
Number of residues:	48
Including
Standard Amino Acids:	44
Non Standard Amino Acids:	0
Water Molecules:	4
Cofactors:
Metals:

Cavity properties

Ligandability	Volume (Å3)
1.050	1495.125

% Hydrophobic	% Polar
34.76	65.24
According to VolSite

Ligand :

HET Code:	NAD
Formula:	C21H26N7O14P2
Molecular weight:	662.417 g/mol
DrugBank ID:	-
Buried Surface Area:	77.95 %
Polar Surface area:	343.54 Å2

Number of
H-Bond Acceptors:	18
H-Bond Donors:	6
Rings:	5
Aromatic rings:	3
Anionic atoms:	2
Cationic atoms:	1
Rule of Five Violation:	3
Rotatable Bonds:	11

Mass center Coordinates

X	Y	Z
30.6815	2.90073	35.0845

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
O2A	N	TYR- 11	2.85	165.57	H-Bond (Protein Donor)	false
O2N	N	ILE- 12	3.06	150.88	H-Bond (Protein Donor)	false
C3N	CD1	ILE- 12	4.29	0	Hydrophobic	false
O3B	OD2	ASP- 31	2.74	154.76	H-Bond (Ligand Donor)	false
O2B	OD1	ASP- 31	2.84	165.1	H-Bond (Ligand Donor)	false
N3A	N	ASN- 32	3.18	140.76	H-Bond (Protein Donor)	false
C2B	SG	CYS- 34	3.63	0	Hydrophobic	false
O1A	ND2	ASN- 35	2.77	169.25	H-Bond (Protein Donor)	false
O2B	N	ASN- 35	2.78	151.91	H-Bond (Protein Donor)	false
C2B	CB	ASN- 35	3.88	0	Hydrophobic	false
C3B	CB	SER- 36	4.32	0	Hydrophobic	false
O3B	OG	SER- 36	2.62	164.11	H-Bond (Protein Donor)	false
N6A	OD1	ASP- 58	2.97	149.75	H-Bond (Ligand Donor)	false
N1A	N	ILE- 59	3.12	167.79	H-Bond (Protein Donor)	false
C5D	CB	PHE- 80	3.95	0	Hydrophobic	false
O3	NZ	LYS- 84	3.12	128.49	H-Bond (Protein Donor)	false
O1N	NZ	LYS- 84	3.15	164.66	H-Bond (Protein Donor)	false
C2D	CB	LYS- 84	3.76	0	Hydrophobic	false
C3N	CD	LYS- 84	4.26	0	Hydrophobic	false
N6A	OD1	ASN- 99	2.85	151.58	H-Bond (Ligand Donor)	false
C4D	CB	SER- 122	4.04	0	Hydrophobic	false
C5N	CB	SER- 124	4.22	0	Hydrophobic	false
O2D	OH	TYR- 149	2.68	158.18	H-Bond (Ligand Donor)	false
O2D	NZ	LYS- 153	3.1	154.96	H-Bond (Protein Donor)	false
C5N	CE1	TYR- 177	3.31	0	Hydrophobic	false
C3N	CG	PRO- 180	4.11	0	Hydrophobic	false
O5B	O	HOH- 354	3.13	161.21	H-Bond (Protein Donor)	false