scPDB - 3vqr entry

Protein Data Bank Entry:

PDB ID : 3vqr

Resolution :2.010 Å

Experimental Method : X-ray

Deposition Date : 2012-03-29

Activity from ChEMBL: What is pChEMBL ?

	Min	Mean	Median	Standard Deviation	Max	Count
pChEMBL:

List of CHEMBLId :

Binding Site :

Uniprot Annotation

Name:	Putative oxidoreductase
ID:	Q9YCJ0_AERPE
AC:	Q9YCJ0
Organism:	Aeropyrum pernix
Reign:	Archaea
TaxID:	272557
EC Number:	/

Chains:

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

Ligand binding site composition:

B-Factor:	25.491
Number of residues:	70
Including
Standard Amino Acids:	64
Non Standard Amino Acids:	0
Water Molecules:	6
Cofactors:
Metals:

Cavity properties

Ligandability	Volume (Å3)
0.614	1846.125

% Hydrophobic	% Polar
47.90	52.10
According to VolSite

Ligand :

HET Code:	FAD
Formula:	C27H31N9O15P2
Molecular weight:	783.534 g/mol
DrugBank ID:	DB03147
Buried Surface Area:	77.06 %
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
66.0236	52.0212	66.1041

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'	CG2	VAL- 13	4.19	0	Hydrophobic	false
O1P	N	VAL- 14	3.23	158.37	H-Bond (Protein Donor)	false
O3B	OD1	ASP- 34	3.1	127.93	H-Bond (Ligand Donor)	false
O3B	OD2	ASP- 34	2.61	164.35	H-Bond (Ligand Donor)	false
O2B	OD1	ASP- 34	2.64	151.87	H-Bond (Ligand Donor)	false
O2B	OD2	ASP- 34	3.46	149.43	H-Bond (Ligand Donor)	false
N3A	N	ALA- 35	3.12	130.38	H-Bond (Protein Donor)	false
O1A	N	ASP- 43	2.82	148.53	H-Bond (Protein Donor)	false
O2A	OG	SER- 44	2.68	155.08	H-Bond (Protein Donor)	false
O2A	N	SER- 44	2.75	159.12	H-Bond (Protein Donor)	false
O4'	OG	SER- 44	2.95	152.3	H-Bond (Ligand Donor)	false
C6	CB	SER- 47	4.07	0	Hydrophobic	false
C2'	CB	SER- 47	4.4	0	Hydrophobic	false
C9A	CB	SER- 47	3.34	0	Hydrophobic	false
N5	N	MET- 48	2.99	170.23	H-Bond (Protein Donor)	false
C6	CB	MET- 48	4.27	0	Hydrophobic	false
N3	O	ALA- 50	2.84	148.84	H-Bond (Ligand Donor)	false
O4	N	ALA- 50	3.14	148.58	H-Bond (Protein Donor)	false
N6A	O	VAL- 184	2.79	174.78	H-Bond (Ligand Donor)	false
N1A	N	VAL- 184	2.7	163.72	H-Bond (Protein Donor)	false
C5B	CZ3	TRP- 233	4.31	0	Hydrophobic	false
C2B	CZ3	TRP- 233	3.79	0	Hydrophobic	false
C8M	CB	ARG- 252	4.35	0	Hydrophobic	false
C7M	CB	ARG- 252	3.62	0	Hydrophobic	false
C7M	CG2	VAL- 254	3.81	0	Hydrophobic	false
C7M	CE1	TYR- 352	4.41	0	Hydrophobic	false
C8M	CD1	TYR- 352	3.88	0	Hydrophobic	false
C8	CE1	TYR- 352	3.38	0	Hydrophobic	false
C3'	CB	THR- 376	4.41	0	Hydrophobic	false
C5'	CG2	THR- 376	4.49	0	Hydrophobic	false
O3'	OG1	THR- 376	2.76	152.37	H-Bond (Ligand Donor)	false
O3'	N	GLY- 380	3.07	133.01	H-Bond (Protein Donor)	false
C2'	CG1	ILE- 381	4.29	0	Hydrophobic	false
C4'	CG1	ILE- 381	4.42	0	Hydrophobic	false
O2	N	MET- 382	2.77	155.03	H-Bond (Protein Donor)	false
O2P	O	HOH- 1109	2.77	162.84	H-Bond (Protein Donor)	false
O1P	O	HOH- 1110	2.54	158.25	H-Bond (Protein Donor)	false