scPDB - 2wuf entry

Protein Data Bank Entry:

PDB ID : 2wuf

Resolution :1.900 Å

Experimental Method : X-ray

Deposition Date : 2009-10-02

Activity from ChEMBL: What is pChEMBL ?

	Min	Mean	Median	Standard Deviation	Max	Count
pChEMBL:

List of CHEMBLId :

Binding Site :

Uniprot Annotation

Name:	4,5:9,10-diseco-3-hydroxy-5,9,17-trioxoandrosta-1(10),2-diene-4-oate hydrolase
ID:	HSAD_MYCTU
AC:	P9WNH5
Organism:	Mycobacterium tuberculosis
Reign:	Bacteria
TaxID:	83332
EC Number:	3.7.1.17

Chains:

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

Ligand binding site composition:

B-Factor:	31.580
Number of residues:	36
Including
Standard Amino Acids:	35
Non Standard Amino Acids:	0
Water Molecules:	1
Cofactors:
Metals:

Cavity properties

Ligandability	Volume (Å3)
1.322	806.625

% Hydrophobic	% Polar
49.79	50.21
According to VolSite

Ligand :

HET Code:	KEM
Formula:	C19H25O6
Molecular weight:	349.398 g/mol
DrugBank ID:	-
Buried Surface Area:	61.29 %
Polar Surface area:	111.57 Å2

Number of
H-Bond Acceptors:	6
H-Bond Donors:	1
Rings:	2
Aromatic rings:	0
Anionic atoms:	1
Cationic atoms:	0
Rule of Five Violation:	0
Rotatable Bonds:	7

Mass center Coordinates

X	Y	Z
11.9546	-40.6136	8.52384

Binding mode :

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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
O11	N	GLY- 45	2.87	134.35	H-Bond (Protein Donor)	false
C02	CB	ALA- 114	4.04	0	Hydrophobic	false
O11	N	LEU- 115	2.94	149.43	H-Bond (Protein Donor)	false
C12	CB	LEU- 115	4.16	0	Hydrophobic	false
C23	CD1	LEU- 115	4.26	0	Hydrophobic	false
C17	CG1	VAL- 155	4.07	0	Hydrophobic	false
C01	CD2	LEU- 158	3.67	0	Hydrophobic	false
C16	CD2	LEU- 158	4.09	0	Hydrophobic	false
C13	CD2	LEU- 158	3.83	0	Hydrophobic	false
C01	CZ	PHE- 173	3.78	0	Hydrophobic	false
C12	CE	MET- 208	4.44	0	Hydrophobic	false
C14	CE	MET- 208	4.01	0	Hydrophobic	false
C16	CE	MET- 208	4.42	0	Hydrophobic	false
C22	SD	MET- 208	3.77	0	Hydrophobic	false
C23	CE2	PHE- 212	3.48	0	Hydrophobic	false
C22	CD2	PHE- 212	3.31	0	Hydrophobic	false
C02	CG1	VAL- 243	4.05	0	Hydrophobic	false