scPDB - 5buk entry

Protein Data Bank Entry:

PDB ID : 5buk

Resolution :1.950 Å

Experimental Method : X-ray

Deposition Date : 2015-06-03

Activity from ChEMBL: What is pChEMBL ?

	Min	Mean	Median	Standard Deviation	Max	Count
pChEMBL:

List of CHEMBLId :

Binding Site :

Uniprot Annotation

Name:	FADH2-dependent halogenase
ID:	J7H1A1_9ACTN
AC:	J7H1A1
Organism:	Streptomyces sp. CNQ-418
Reign:	Bacteria
TaxID:	467194
EC Number:	/

Chains:

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

Ligand binding site composition:

B-Factor:	24.417
Number of residues:	73
Including
Standard Amino Acids:	67
Non Standard Amino Acids:	0
Water Molecules:	6
Cofactors:
Metals:

Cavity properties

Ligandability	Volume (Å3)
0.866	378.000

% Hydrophobic	% Polar
60.71	39.29
According to VolSite

Ligand :

HET Code:	FAD
Formula:	C27H31N9O15P2
Molecular weight:	783.534 g/mol
DrugBank ID:	DB03147
Buried Surface Area:	76.52 %
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
27.0218	72.3176	32.7061

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
O1P	N	ALA- 15	3.02	160.3	H-Bond (Protein Donor)	false
O3B	OE1	GLU- 34	2.79	175.4	H-Bond (Ligand Donor)	false
O3B	OE2	GLU- 34	3.25	125.69	H-Bond (Ligand Donor)	false
N3A	N	SER- 35	3.13	148.29	H-Bond (Protein Donor)	false
O3B	NE	ARG- 40	3.4	135.31	H-Bond (Protein Donor)	false
O3B	NH1	ARG- 40	2.9	157.17	H-Bond (Protein Donor)	false
O1A	NE2	HIS- 42	2.85	147.41	H-Bond (Protein Donor)	false
C6	CG2	VAL- 43	3.88	0	Hydrophobic	false
C7M	CG2	VAL- 43	3.87	0	Hydrophobic	false
C8	CG1	VAL- 43	3.56	0	Hydrophobic	false
N3	O	SER- 46	2.72	170.42	H-Bond (Ligand Donor)	false
O4	N	SER- 46	3.18	152.44	H-Bond (Protein Donor)	false
O2A	NH2	ARG- 122	2.89	128.23	H-Bond (Protein Donor)	false
O2'	NH1	ARG- 122	3.29	142.31	H-Bond (Protein Donor)	false
O4'	NH2	ARG- 122	3.22	145.26	H-Bond (Protein Donor)	false
O4'	NH1	ARG- 122	3.2	146.12	H-Bond (Protein Donor)	false
N6A	O	VAL- 146	2.82	168.63	H-Bond (Ligand Donor)	false
N1A	N	VAL- 146	3	175.49	H-Bond (Protein Donor)	false
C8M	CD	ARG- 180	4.45	0	Hydrophobic	false
N6A	OE1	GLN- 183	3.03	135.92	H-Bond (Ligand Donor)	false
C7M	CB	ALA- 201	3.49	0	Hydrophobic	false
C7M	CH2	TRP- 237	3.92	0	Hydrophobic	false
C7M	CB	ASP- 296	4.37	0	Hydrophobic	false
C8M	CB	ASP- 296	4.18	0	Hydrophobic	false
O3'	OD1	ASP- 314	2.75	170.48	H-Bond (Ligand Donor)	false
C5'	CB	ASP- 314	4.33	0	Hydrophobic	false
O2P	N	ASP- 314	3.06	160.79	H-Bond (Protein Donor)	false
C8M	CZ	PHE- 318	3.67	0	Hydrophobic	false
C1'	CE2	PHE- 318	4.12	0	Hydrophobic	false
C9A	CG	PRO- 321	3.51	0	Hydrophobic	false
O2	N	VAL- 327	2.76	167.96	H-Bond (Protein Donor)	false
C2'	CG2	VAL- 327	4.45	0	Hydrophobic	false
C4'	CG2	VAL- 327	4.35	0	Hydrophobic	false
C5'	CB	ALA- 330	4.01	0	Hydrophobic	false
O2B	O	HOH- 619	2.61	179.97	H-Bond (Protein Donor)	false
O2P	O	HOH- 632	2.68	179.96	H-Bond (Protein Donor)	false
O2	O	HOH- 661	2.76	179.98	H-Bond (Protein Donor)	false
O1P	O	HOH- 673	2.75	179.95	H-Bond (Protein Donor)	false
O1A	O	HOH- 692	2.78	179.98	H-Bond (Protein Donor)	false