scPDB - 4n8i entry

Protein Data Bank Entry:

PDB ID : 4n8i

Resolution :2.010 Å

Experimental Method : X-ray

Deposition Date : 2013-10-17

Activity from ChEMBL: What is pChEMBL ?

	Min	Mean	Median	Standard Deviation	Max	Count
pChEMBL:

List of CHEMBLId :

Binding Site :

Uniprot Annotation

Name:	Putative 4-hydroxybutyrate coenzyme A transferase
ID:	Q9ZC36_YERPE
AC:	Q9ZC36
Organism:	Yersinia pestis
Reign:	Bacteria
TaxID:	632
EC Number:	/

Chains:

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

Ligand binding site composition:

B-Factor:	27.256
Number of residues:	53
Including
Standard Amino Acids:	49
Non Standard Amino Acids:	0
Water Molecules:	4
Cofactors:
Metals:

Cavity properties

Ligandability	Volume (Å3)
0.904	1063.125

% Hydrophobic	% Polar
44.13	55.87
According to VolSite

Ligand :

HET Code:	COA
Formula:	C21H32N7O16P3S
Molecular weight:	763.502 g/mol
DrugBank ID:	DB01992
Buried Surface Area:	56.79 %
Polar Surface area:	426.11 Å2

Number of
H-Bond Acceptors:	21
H-Bond Donors:	6
Rings:	3
Aromatic rings:	2
Anionic atoms:	4
Cationic atoms:	0
Rule of Five Violation:	3
Rotatable Bonds:	18

Mass center Coordinates

X	Y	Z
-20.945	5.48792	-0.407583

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
C6P	CE2	PHE- 85	4.06	0	Hydrophobic	false
O1A	NH2	ARG- 200	2.93	141.72	H-Bond (Protein Donor)	false
O4A	NH1	ARG- 200	2.76	164.22	H-Bond (Protein Donor)	false
O4A	CZ	ARG- 200	3.62	0	Ionic (Protein Cationic)	false
CAP	CG2	VAL- 227	4.36	0	Hydrophobic	false
C6P	CG2	VAL- 227	3.94	0	Hydrophobic	false
S1P	CG1	VAL- 227	3.83	0	Hydrophobic	false
OAP	O	VAL- 227	2.68	158.73	H-Bond (Ligand Donor)	false
O5A	N	ALA- 229	2.91	167.17	H-Bond (Protein Donor)	false
S1P	CB	GLU- 249	4.37	0	Hydrophobic	false
S1P	CG2	VAL- 250	3.75	0	Hydrophobic	false
CCP	CB	ALA- 322	4.2	0	Hydrophobic	false
CEP	CB	ALA- 322	4.27	0	Hydrophobic	false
N6A	O	LEU- 324	2.93	177.78	H-Bond (Ligand Donor)	false
CEP	CG	LEU- 324	4.02	0	Hydrophobic	false
CDP	CD2	LEU- 324	3.89	0	Hydrophobic	false
CEP	CB	SER- 334	4.1	0	Hydrophobic	false
C1B	CE	MET- 337	4.23	0	Hydrophobic	false
C4B	CE	MET- 337	4.18	0	Hydrophobic	false
C5B	CZ	TYR- 342	4.37	0	Hydrophobic	false
CDP	CE2	TYR- 342	3.81	0	Hydrophobic	false
CDP	CB	SER- 343	4.39	0	Hydrophobic	false
O9P	OG	SER- 343	2.85	141.11	H-Bond (Protein Donor)	false
C6P	CB	GLN- 348	4.41	0	Hydrophobic	false
O5P	NE2	GLN- 348	2.77	145.47	H-Bond (Protein Donor)	false
C2B	CB	ALA- 371	4.16	0	Hydrophobic	false
O2A	NH1	ARG- 378	3.02	141.82	H-Bond (Protein Donor)	false
O2A	NH2	ARG- 378	2.89	149.64	H-Bond (Protein Donor)	false
O2A	CZ	ARG- 378	3.39	0	Ionic (Protein Cationic)	false
O5P	O	HOH- 630	2.95	157.28	H-Bond (Protein Donor)	false
N6A	O	HOH- 649	2.82	147.23	H-Bond (Ligand Donor)	false