scPDB - 4mo2 entry

Protein Data Bank Entry:

PDB ID : 4mo2

Resolution :2.000 Å

Experimental Method : X-ray

Deposition Date : 2013-09-11

Activity from ChEMBL: What is pChEMBL ?

	Min	Mean	Median	Standard Deviation	Max	Count
pChEMBL:

List of CHEMBLId :

Binding Site :

Uniprot Annotation

Name:	UDP-galactopyranose mutase
ID:	Q0P8H5_CAMJE
AC:	Q0P8H5
Organism:	Campylobacter jejuni subsp. jejuni serotype O:2
Reign:	Bacteria
TaxID:	192222
EC Number:	/

Chains:

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

Ligand binding site composition:

B-Factor:	17.219
Number of residues:	61
Including
Standard Amino Acids:	57
Non Standard Amino Acids:	0
Water Molecules:	4
Cofactors:
Metals:

Cavity properties

Ligandability	Volume (Å3)
0.729	988.875

% Hydrophobic	% Polar
34.47	65.53
According to VolSite

Ligand :

HET Code:	FDA
Formula:	C27H33N9O15P2
Molecular weight:	785.550 g/mol
DrugBank ID:	-
Buried Surface Area:	74.55 %
Polar Surface area:	381.04 Å2

Number of
H-Bond Acceptors:	21
H-Bond Donors:	9
Rings:	6
Aromatic rings:	3
Anionic atoms:	2
Cationic atoms:	0
Rule of Five Violation:	3
Rotatable Bonds:	13

Mass center Coordinates

X	Y	Z
10.4215	-13.2672	1.84138

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
O1P	N	PHE- 12	2.88	157.71	H-Bond (Protein Donor)	false
O3B	OE1	GLU- 31	2.83	156.94	H-Bond (Ligand Donor)	false
O2B	OE2	GLU- 31	2.62	164.08	H-Bond (Ligand Donor)	false
O2B	NE2	GLN- 32	3.49	149.96	H-Bond (Protein Donor)	false
N3A	N	GLN- 32	3.19	134.3	H-Bond (Protein Donor)	false
O2A	N	ASN- 39	3.09	166.48	H-Bond (Protein Donor)	false
C2'	SG	CYS- 40	4.34	0	Hydrophobic	false
C4'	SG	CYS- 40	4.16	0	Hydrophobic	false
O2'	NE2	HIS- 56	2.76	162.86	H-Bond (Protein Donor)	false
N3	O	ILE- 57	2.8	150.96	H-Bond (Ligand Donor)	false
O4	N	ILE- 57	2.8	169.22	H-Bond (Protein Donor)	false
N6A	OD1	ASP- 211	2.93	130.09	H-Bond (Ligand Donor)	false
N1A	N	PHE- 212	3.14	162.81	H-Bond (Protein Donor)	false
C7M	CD1	LEU- 248	3.64	0	Hydrophobic	false
C7M	CD2	TYR- 309	3.86	0	Hydrophobic	false
C8M	CD2	TYR- 309	3.73	0	Hydrophobic	false
C7M	CZ	TYR- 310	3.77	0	Hydrophobic	false
C8M	CE2	TYR- 310	4	0	Hydrophobic	false
O1A	NE	ARG- 339	2.61	145.07	H-Bond (Protein Donor)	false
O1A	NH2	ARG- 339	3.13	124.96	H-Bond (Protein Donor)	false
O2P	N	ARG- 339	2.92	162.05	H-Bond (Protein Donor)	false
O1A	CZ	ARG- 339	3.25	0	Ionic (Protein Cationic)	false
C5'	CD	ARG- 339	3.85	0	Hydrophobic	false
C5B	CD1	LEU- 340	4.33	0	Hydrophobic	false
C8M	CE1	TYR- 345	4.11	0	Hydrophobic	false
C1'	CZ	TYR- 345	4.24	0	Hydrophobic	false
O3'	O	TYR- 346	2.88	127.65	H-Bond (Ligand Donor)	false
N1	N	MET- 348	3.31	133.89	H-Bond (Protein Donor)	false
O2	N	MET- 348	2.67	159.47	H-Bond (Protein Donor)	false
C2'	CG	MET- 348	4.12	0	Hydrophobic	false
C5'	CG1	VAL- 351	4.26	0	Hydrophobic	false
O2A	O	HOH- 504	2.72	179.97	H-Bond (Protein Donor)	false
O3P	O	HOH- 542	3.2	167.99	H-Bond (Protein Donor)	false