scPDB - 3rha entry

Protein Data Bank Entry:

PDB ID : 3rha

Resolution :2.050 Å

Experimental Method : X-ray

Deposition Date : 2011-04-11

Activity from ChEMBL: What is pChEMBL ?

	Min	Mean	Median	Standard Deviation	Max	Count
pChEMBL:

List of CHEMBLId :

Binding Site :

Uniprot Annotation

Name:	Putrescine oxidase
ID:	A1R0W1_ARTAT
AC:	A1R0W1
Organism:	Arthrobacter aurescens
Reign:	Bacteria
TaxID:	290340
EC Number:	/

Chains:

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

Ligand binding site composition:

B-Factor:	12.316
Number of residues:	77
Including
Standard Amino Acids:	68
Non Standard Amino Acids:	0
Water Molecules:	9
Cofactors:
Metals:

Cavity properties

Ligandability	Volume (Å3)
1.251	560.250

% Hydrophobic	% Polar
62.65	37.35
According to VolSite

Ligand :

HET Code:	FDA
Formula:	C27H33N9O15P2
Molecular weight:	785.550 g/mol
DrugBank ID:	-
Buried Surface Area:	81.05 %
Polar Surface area:	381.04 Å2

Number of
H-Bond Acceptors:	21
H-Bond Donors:	9
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
17.7911	2.36345	-30.5961

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
C4'	CG	PRO- 17	3.97	0	Hydrophobic	false
O1P	N	SER- 18	2.83	155.26	H-Bond (Protein Donor)	false
O3B	OE1	GLU- 37	2.76	171.34	H-Bond (Ligand Donor)	false
O2B	OE2	GLU- 37	2.61	174.71	H-Bond (Ligand Donor)	false
N3A	N	ALA- 38	3.03	137.56	H-Bond (Protein Donor)	false
O2B	NH1	ARG- 39	2.94	123.25	H-Bond (Protein Donor)	false
O1A	CZ	ARG- 45	3.51	0	Ionic (Protein Cationic)	false
O1A	NE	ARG- 45	2.76	157.96	H-Bond (Protein Donor)	false
O1A	NH2	ARG- 45	3.42	127.78	H-Bond (Protein Donor)	false
O2A	N	ARG- 45	2.81	173.59	H-Bond (Protein Donor)	false
O3P	NH2	ARG- 45	2.94	149.24	H-Bond (Protein Donor)	false
C8M	CB	ARG- 45	3.96	0	Hydrophobic	false
C9	CB	ARG- 45	3.93	0	Hydrophobic	false
C3'	CB	ARG- 45	4.05	0	Hydrophobic	false
O4	N	GLN- 61	3.11	160.32	H-Bond (Protein Donor)	false
N3	O	TRP- 62	3.15	161.42	H-Bond (Ligand Donor)	false
O4	N	TRP- 62	2.75	163.13	H-Bond (Protein Donor)	false
N6A	O	VAL- 237	3.16	168.97	H-Bond (Ligand Donor)	false
N1A	N	VAL- 237	2.82	167.23	H-Bond (Protein Donor)	false
C1B	CG1	VAL- 265	4.29	0	Hydrophobic	false
C6	CD	LYS- 297	4.29	0	Hydrophobic	false
C7M	CD	LYS- 297	4.04	0	Hydrophobic	false
C7M	CB	SER- 384	4.42	0	Hydrophobic	false
C7M	CE2	TRP- 386	4.15	0	Hydrophobic	false
C8	CE2	TRP- 386	4.46	0	Hydrophobic	false
C8M	CD2	TRP- 386	3.32	0	Hydrophobic	false
C2B	CB	TRP- 391	4.04	0	Hydrophobic	false
C8M	CB	ALA- 395	4.03	0	Hydrophobic	false
C8	CB	ALA- 395	3.97	0	Hydrophobic	false
C1'	CB	TYR- 396	4.27	0	Hydrophobic	false
C7	CD1	TYR- 396	3.21	0	Hydrophobic	false
C8	CD1	TYR- 396	3.66	0	Hydrophobic	false
O3'	OG	SER- 424	2.58	165.73	H-Bond (Protein Donor)	false
O2P	N	SER- 424	2.9	151.62	H-Bond (Protein Donor)	false
C5'	CB	SER- 424	3.89	0	Hydrophobic	false
N1	N	VAL- 434	3.46	142.18	H-Bond (Protein Donor)	false
O2	N	VAL- 434	2.65	149.6	H-Bond (Protein Donor)	false
C4'	CG2	VAL- 434	4.31	0	Hydrophobic	false
C5'	CB	ALA- 437	4	0	Hydrophobic	false
O1A	O	HOH- 535	2.58	127.94	H-Bond (Protein Donor)	false
O3B	O	HOH- 604	2.83	162.69	H-Bond (Protein Donor)	false
O1P	O	HOH- 940	2.55	172.52	H-Bond (Protein Donor)	false