scPDB - 4ava entry

Protein Data Bank Entry:

PDB ID : 4ava

Resolution :1.700 Å

Experimental Method : X-ray

Deposition Date : 2012-05-24

Activity from ChEMBL: What is pChEMBL ?

	Min	Mean	Median	Standard Deviation	Max	Count
pChEMBL:

List of CHEMBLId :

Binding Site :

Uniprot Annotation

Name:	Acetyltransferase Pat
ID:	PAT_MYCTU
AC:	O05581
Organism:	Mycobacterium tuberculosis
Reign:	Bacteria
TaxID:	83332
EC Number:	2.3.1

Chains:

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

Ligand binding site composition:

B-Factor:	28.920
Number of residues:	35
Including
Standard Amino Acids:	31
Non Standard Amino Acids:	0
Water Molecules:	4
Cofactors:
Metals:

Cavity properties

Ligandability	Volume (Å3)
0.432	270.000

% Hydrophobic	% Polar
52.50	47.50
According to VolSite

Ligand :

HET Code:	ACO
Formula:	C23H34N7O17P3S
Molecular weight:	805.539 g/mol
DrugBank ID:	-
Buried Surface Area:	51.29 %
Polar Surface area:	429.68 Å2

Number of
H-Bond Acceptors:	22
H-Bond Donors:	5
Rings:	3
Aromatic rings:	2
Anionic atoms:	4
Cationic atoms:	0
Rule of Five Violation:	2
Rotatable Bonds:	20

Mass center Coordinates

X	Y	Z
62.6973	65.8981	22.6527

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
CDP	CB	PHE- 238	3.61	0	Hydrophobic	false
CH3	CD1	PHE- 238	4.38	0	Hydrophobic	false
N4P	O	PHE- 238	2.91	143.57	H-Bond (Ligand Donor)	false
O	N	PHE- 238	3.03	143.84	H-Bond (Protein Donor)	false
CDP	CG2	VAL- 240	4.18	0	Hydrophobic	false
CAP	CB	VAL- 240	4.05	0	Hydrophobic	false
O9P	N	VAL- 240	2.82	152.1	H-Bond (Protein Donor)	false
CAP	CG	GLN- 245	3.98	0	Hydrophobic	false
O5A	N	GLY- 246	2.94	157.49	H-Bond (Protein Donor)	false
O2A	N	GLY- 248	2.77	144.17	H-Bond (Protein Donor)	false
O4A	N	GLY- 250	2.79	165.56	H-Bond (Protein Donor)	false
O1A	N	SER- 251	2.83	151.95	H-Bond (Protein Donor)	false
O1A	OG	SER- 251	2.61	164.37	H-Bond (Protein Donor)	false
CH3	CB	ALA- 271	4.02	0	Hydrophobic	false
S1P	CB	MET- 273	3.78	0	Hydrophobic	false
CH3	CE	MET- 273	4.07	0	Hydrophobic	false
O5P	ND2	ASN- 277	2.91	138.37	H-Bond (Protein Donor)	false
C5B	CB	PRO- 279	4.32	0	Hydrophobic	false
CCP	CB	PRO- 279	3.91	0	Hydrophobic	false
CEP	CB	PRO- 279	4.2	0	Hydrophobic	false
CDP	SD	MET- 280	4.26	0	Hydrophobic	false
CEP	CB	MET- 280	3.88	0	Hydrophobic	false
S1P	CG	MET- 280	3.71	0	Hydrophobic	false
CH3	SD	MET- 280	3.97	0	Hydrophobic	false
C1B	CG2	THR- 282	4.19	0	Hydrophobic	false
C4B	CG2	THR- 282	3.82	0	Hydrophobic	false
CCP	CD1	ILE- 283	3.91	0	Hydrophobic	false
C5B	CG1	ILE- 283	3.48	0	Hydrophobic	false
O7A	NE	ARG- 286	3.01	177.69	H-Bond (Protein Donor)	false
O8A	NH2	ARG- 286	2.92	166.58	H-Bond (Protein Donor)	false
O7A	CZ	ARG- 286	3.82	0	Ionic (Protein Cationic)	false
O8A	CZ	ARG- 286	3.82	0	Ionic (Protein Cationic)	false
O4A	O	HOH- 2172	2.56	150.73	H-Bond (Protein Donor)	false