scPDB - 2wes entry

Protein Data Bank Entry:

PDB ID : 2wes

Resolution :2.500 Å

Experimental Method : X-ray

Deposition Date : 2009-04-01

Activity from ChEMBL: What is pChEMBL ?

	Min	Mean	Median	Standard Deviation	Max	Count
pChEMBL:

List of CHEMBLId :

Binding Site :

Uniprot Annotation

Name:	Tryptophan 5-halogenase
ID:	A4D0H5_9ACTN
AC:	A4D0H5
Organism:	Streptomyces rugosporus
Reign:	Bacteria
TaxID:	295838
EC Number:	/

Chains:

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

Ligand binding site composition:

B-Factor:	35.717
Number of residues:	64
Including
Standard Amino Acids:	58
Non Standard Amino Acids:	1
Water Molecules:	5
Cofactors:
Metals:	CL

Cavity properties

Ligandability	Volume (Å3)
1.597	958.500

% Hydrophobic	% Polar
59.86	40.14
According to VolSite

Ligand :

HET Code:	FAD
Formula:	C27H31N9O15P2
Molecular weight:	783.534 g/mol
DrugBank ID:	DB03147
Buried Surface Area:	74.9 %
Polar Surface area:	381.7 Å2

Number of
H-Bond Acceptors:	22
H-Bond Donors:	7
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
-14.9632	33.5534	-25.3908

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
O3B	N	GLY- 10	3.08	148.45	H-Bond (Protein Donor)	false
C4'	CB	THR- 12	3.84	0	Hydrophobic	false
C5'	CB	ALA- 13	4.24	0	Hydrophobic	false
O1P	N	ALA- 13	3.12	156.01	H-Bond (Protein Donor)	false
C2B	CB	SER- 36	4.44	0	Hydrophobic	false
N3A	N	SER- 36	3.06	132.42	H-Bond (Protein Donor)	false
C2B	CB	VAL- 39	4.17	0	Hydrophobic	false
O2B	O	VAL- 39	2.72	163.13	H-Bond (Ligand Donor)	false
C3B	CB	ARG- 41	4.32	0	Hydrophobic	false
O2A	N	ILE- 42	2.86	156	H-Bond (Protein Donor)	false
C8M	CD1	ILE- 42	4.44	0	Hydrophobic	false
C8	CG2	ILE- 42	4.43	0	Hydrophobic	false
C6	CG2	VAL- 44	4.26	0	Hydrophobic	false
O4'	NE2	GLN- 46	3.34	160.24	H-Bond (Protein Donor)	false
N3	O	ALA- 47	2.58	163.84	H-Bond (Ligand Donor)	false
O4	N	ALA- 47	2.96	164.78	H-Bond (Protein Donor)	false
N6A	O	VAL- 195	3.03	166.54	H-Bond (Ligand Donor)	false
N1A	N	VAL- 195	2.8	167.89	H-Bond (Protein Donor)	false
C8M	CZ	PHE- 228	4.05	0	Hydrophobic	false
C7M	CB	ALA- 253	3.83	0	Hydrophobic	false
C7M	CH2	TRP- 281	3.76	0	Hydrophobic	false
C7M	CD1	ILE- 325	4.09	0	Hydrophobic	false
C8M	CG2	ILE- 325	4.24	0	Hydrophobic	false
C8M	CG	MET- 327	4.39	0	Hydrophobic	false
C5'	CG	LEU- 345	4.49	0	Hydrophobic	false
C3'	CD2	LEU- 345	3.87	0	Hydrophobic	false
O2P	N	LEU- 345	3.08	162.28	H-Bond (Protein Donor)	false
C8M	CZ	PHE- 349	4	0	Hydrophobic	false
C1'	CE1	PHE- 349	3.56	0	Hydrophobic	false
C9	CZ	PHE- 349	3.29	0	Hydrophobic	false
C6	CG	PRO- 352	3.72	0	Hydrophobic	false
O2	N	ILE- 358	2.73	157.55	H-Bond (Protein Donor)	false
C5'	CD1	ILE- 361	3.56	0	Hydrophobic	false
O3B	O	HOH- 2017	2.87	152.68	H-Bond (Ligand Donor)	false
O2P	O	HOH- 2186	2.88	163.52	H-Bond (Protein Donor)	false
O2	O	HOH- 2194	2.83	155.69	H-Bond (Protein Donor)	false
O1P	O	HOH- 2302	2.54	179.97	H-Bond (Protein Donor)	false