scPDB - 1u8x entry

Protein Data Bank Entry:

PDB ID : 1u8x

Resolution :2.050 Å

Experimental Method : X-ray

Deposition Date : 2004-08-09

Activity from ChEMBL: What is pChEMBL ?

	Min	Mean	Median	Standard Deviation	Max	Count
pChEMBL:

List of CHEMBLId :

Binding Site :

Uniprot Annotation

Name:	Maltose-6'-phosphate glucosidase
ID:	GLVA_BACSU
AC:	P54716
Organism:	Bacillus subtilis
Reign:	Bacteria
TaxID:	224308
EC Number:	3.2.1.122

Chains:

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

Ligand binding site composition:

B-Factor:	36.811
Number of residues:	52
Including
Standard Amino Acids:	49
Non Standard Amino Acids:	2
Water Molecules:	1
Cofactors:
Metals:	MN

Cavity properties

Ligandability	Volume (Å3)
0.071	864.000

% Hydrophobic	% Polar
35.94	64.06
According to VolSite

Ligand :

HET Code:	NAD
Formula:	C21H26N7O14P2
Molecular weight:	662.417 g/mol
DrugBank ID:	-
Buried Surface Area:	74.65 %
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
23.5708	81.4282	21.4806

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
O1A	OG	SER- 15	2.94	131.91	H-Bond (Protein Donor)	false
C4B	CB	SER- 15	3.54	0	Hydrophobic	false
O1A	N	THR- 16	2.92	147.87	H-Bond (Protein Donor)	false
O1A	OG1	THR- 16	3.13	165.07	H-Bond (Protein Donor)	false
O1N	N	PHE- 17	3.27	125.85	H-Bond (Protein Donor)	false
C5N	CE2	PHE- 17	3.36	0	Hydrophobic	false
O3B	OD2	ASP- 41	2.99	160.93	H-Bond (Ligand Donor)	false
O2B	OD2	ASP- 41	3.07	149.08	H-Bond (Ligand Donor)	false
O2B	OD1	ASP- 41	2.88	148.91	H-Bond (Ligand Donor)	false
C4D	CB	HIS- 86	3.54	0	Hydrophobic	false
C1B	CG2	ILE- 87	4.5	0	Hydrophobic	false
O3D	O	ILE- 87	2.84	139.8	H-Bond (Ligand Donor)	false
C5B	CB	ARG- 88	3.39	0	Hydrophobic	false
C3D	CG	ARG- 88	3.88	0	Hydrophobic	false
O4B	N	ARG- 88	3.32	149.8	H-Bond (Protein Donor)	false
O3	NE	ARG- 88	2.86	136.5	H-Bond (Protein Donor)	false
O2N	NH2	ARG- 88	2.98	164.23	H-Bond (Protein Donor)	false
O2N	CZ	ARG- 88	3.74	0	Ionic (Protein Cationic)	false
C2B	CD	LYS- 91	4.25	0	Hydrophobic	false
O2N	OH	TYR- 92	2.55	139.69	H-Bond (Protein Donor)	false
O2D	OE2	GLU- 111	2.73	160.58	H-Bond (Ligand Donor)	false
C3D	CZ	TYR- 120	4.47	0	Hydrophobic	false
C3N	CB	TYR- 147	4.21	0	Hydrophobic	false
N7N	O	TYR- 147	3.08	134.99	H-Bond (Ligand Donor)	false
O3D	N	ASN- 149	3.26	165.99	H-Bond (Protein Donor)	false
O2D	ND2	ASN- 149	3.37	139.2	H-Bond (Protein Donor)	false
C2D	CB	ASN- 149	4.43	0	Hydrophobic	false
N7N	O	ILE- 170	3.07	131.26	H-Bond (Ligand Donor)	false
O7N	N	ASP- 172	2.66	151.86	H-Bond (Protein Donor)	false