scPDB - 2hw2 entry

Protein Data Bank Entry:

PDB ID : 2hw2

Resolution :1.450 Å

Experimental Method : X-ray

Deposition Date : 2006-07-31

Activity from ChEMBL: What is pChEMBL ?

	Min	Mean	Median	Standard Deviation	Max	Count
pChEMBL:

List of CHEMBLId :

Binding Site :

Uniprot Annotation

Name:	Rifampin ADP-ribosyl transferase
ID:	A0QRS5_MYCS2
AC:	A0QRS5
Organism:	Mycobacterium smegmatis 155)
Reign:	Bacteria
TaxID:	246196
EC Number:	/

Chains:

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

Ligand binding site composition:

B-Factor:	25.381
Number of residues:	46
Including
Standard Amino Acids:	43
Non Standard Amino Acids:	0
Water Molecules:	3
Cofactors:
Metals:

Cavity properties

Ligandability	Volume (Å3)
1.455	985.500

% Hydrophobic	% Polar
54.11	45.89
According to VolSite

Ligand :

HET Code:	RFP
Formula:	C43H59N4O12
Molecular weight:	823.948 g/mol
DrugBank ID:	DB01045
Buried Surface Area:	58.43 %
Polar Surface area:	221.34 Å2

Number of
H-Bond Acceptors:	14
H-Bond Donors:	7
Rings:	5
Aromatic rings:	2
Anionic atoms:	0
Cationic atoms:	1
Rule of Five Violation:	3
Rotatable Bonds:	5

Mass center Coordinates

X	Y	Z
-12.9446	7.79447	-18.3629

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
C12	CE2	PHE- 9	4.48	0	Hydrophobic	false
C13	CZ	PHE- 9	3.88	0	Hydrophobic	false
C23	CZ	PHE- 39	4.13	0	Hydrophobic	false
C31	CD2	PHE- 39	4.15	0	Hydrophobic	false
C33	CE2	PHE- 39	3.78	0	Hydrophobic	false
C36	CZ	PHE- 39	4.2	0	Hydrophobic	false
C32	CD1	PHE- 39	3.58	0	Hydrophobic	false
C37	CB	ALA- 56	3.68	0	Hydrophobic	false
C27	CB	TRP- 59	4.38	0	Hydrophobic	false
C36	CB	TRP- 59	4.04	0	Hydrophobic	false
C33	CD1	LEU- 63	3.96	0	Hydrophobic	false
C36	CD1	LEU- 63	4.34	0	Hydrophobic	false
C25	CG1	VAL- 87	4.43	0	Hydrophobic	false
C34	CG1	VAL- 87	4.1	0	Hydrophobic	false
C37	CG1	VAL- 87	4.34	0	Hydrophobic	false
C14	CB	VAL- 87	4.28	0	Hydrophobic	false
C8	CG1	VAL- 87	3.99	0	Hydrophobic	false
O2	N	LYS- 91	3.33	163.36	H-Bond (Protein Donor)	false
C1	CG	LYS- 91	3.63	0	Hydrophobic	false
C8	CB	LYS- 91	3.68	0	Hydrophobic	false
C10	CD	LYS- 91	4.08	0	Hydrophobic	false
C14	CD1	LEU- 92	4.12	0	Hydrophobic	false
C14	CG	PRO- 96	4.47	0	Hydrophobic	false
C14	CG2	THR- 97	4.27	0	Hydrophobic	false
C37	CB	THR- 97	4.23	0	Hydrophobic	false
C26	CE	MET- 126	4.33	0	Hydrophobic	false
C41	SD	MET- 126	3.83	0	Hydrophobic	false
C31	CD2	LEU- 130	3.87	0	Hydrophobic	false
C33	CD2	LEU- 130	4.02	0	Hydrophobic	false
C41	CD2	LEU- 130	3.63	0	Hydrophobic	false
C30	CD2	LEU- 133	4.24	0	Hydrophobic	false
C40	CD1	LEU- 133	3.57	0	Hydrophobic	false
C41	CD1	LEU- 133	3.81	0	Hydrophobic	false
C31	CB	ALA- 139	4.47	0	Hydrophobic	false
C31	CD1	ILE- 141	4.16	0	Hydrophobic	false
C23	CA	GLY- 144	4.31	0	Hydrophobic	false
C36	CA	GLY- 144	4.17	0	Hydrophobic	false
O9	N	GLY- 144	2.79	174.37	H-Bond (Protein Donor)	false
O2	O	HOH- 1226	3.07	168.13	H-Bond (Protein Donor)	false