scPDB - 2x6t entry

Protein Data Bank Entry:

PDB ID : 2x6t

Resolution :2.360 Å

Experimental Method : X-ray

Deposition Date : 2010-02-21

Activity from ChEMBL: What is pChEMBL ?

	Min	Mean	Median	Standard Deviation	Max	Count
pChEMBL:

List of CHEMBLId :

Binding Site :

Uniprot Annotation

Name:	ADP-L-glycero-D-manno-heptose-6-epimerase
ID:	HLDD_ECOLI
AC:	P67910
Organism:	Escherichia coli
Reign:	Bacteria
TaxID:	83333
EC Number:	/

Chains:

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

Ligand binding site composition:

B-Factor:	28.628
Number of residues:	57
Including
Standard Amino Acids:	52
Non Standard Amino Acids:	1
Water Molecules:	4
Cofactors:
Metals:

Cavity properties

Ligandability	Volume (Å3)
1.087	1468.125

% Hydrophobic	% Polar
41.15	58.85
According to VolSite

Ligand :

HET Code:	NAP
Formula:	C21H25N7O17P3
Molecular weight:	740.381 g/mol
DrugBank ID:	DB03461
Buried Surface Area:	74.31 %
Polar Surface area:	405.54 Å2

Number of
H-Bond Acceptors:	21
H-Bond Donors:	5
Rings:	5
Aromatic rings:	3
Anionic atoms:	4
Cationic atoms:	1
Rule of Five Violation:	2
Rotatable Bonds:	13

Mass center Coordinates

X	Y	Z
69.3796	-21.7308	-64.7444

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
O1A	N	PHE- 10	3.02	166.46	H-Bond (Protein Donor)	false
O2N	N	ILE- 11	2.86	169	H-Bond (Protein Donor)	false
C3N	CD1	ILE- 11	4.2	0	Hydrophobic	false
C5D	CD1	ILE- 11	4.11	0	Hydrophobic	false
O3B	OD1	ASP- 31	2.66	158.06	H-Bond (Ligand Donor)	false
O3B	OD2	ASP- 31	3.44	135.13	H-Bond (Ligand Donor)	false
O2X	ND2	ASN- 32	2.95	173.81	H-Bond (Protein Donor)	false
O3B	NZ	LYS- 38	2.66	171.69	H-Bond (Protein Donor)	false
O1X	NZ	LYS- 38	3.86	0	Ionic (Protein Cationic)	false
O2X	NZ	LYS- 53	2.86	149.16	H-Bond (Protein Donor)	false
O2X	NZ	LYS- 53	2.86	0	Ionic (Protein Cationic)	false
C5D	CB	GLU- 75	4.21	0	Hydrophobic	false
C3D	CB	ALA- 77	3.88	0	Hydrophobic	false
O2A	OG	SER- 79	2.66	155.44	H-Bond (Protein Donor)	false
O3	OG	SER- 79	3.37	136.75	H-Bond (Protein Donor)	false
C2D	CB	SER- 79	3.98	0	Hydrophobic	false
N7A	ND2	ASN- 92	2.83	156.56	H-Bond (Protein Donor)	false
N6A	O	ASN- 92	3.26	130.46	H-Bond (Ligand Donor)	false
C4D	CB	ALA- 114	3.62	0	Hydrophobic	false
C5N	CB	SER- 116	3.76	0	Hydrophobic	false
C2D	CZ	PHE- 140	4.41	0	Hydrophobic	false
O3D	NZ	LYS- 144	2.77	144.43	H-Bond (Protein Donor)	false
C5N	CB	TYR- 167	3.46	0	Hydrophobic	false
O7N	N	VAL- 170	3.14	147.13	H-Bond (Protein Donor)	false
C3N	CG2	VAL- 170	4.3	0	Hydrophobic	false
O1A	NE2	HIS- 177	2.77	155.63	H-Bond (Protein Donor)	false
O1N	NZ	LYS- 178	2.7	155.68	H-Bond (Protein Donor)	false
O1N	NZ	LYS- 178	2.7	0	Ionic (Protein Cationic)	false
O5B	O	HOH- 2002	3.16	164.77	H-Bond (Protein Donor)	false
N7N	O	HOH- 2085	3.45	149.06	H-Bond (Ligand Donor)	false