scPDB - 1qlt entry

Protein Data Bank Entry:

PDB ID : 1qlt

Resolution :2.200 Å

Experimental Method : X-ray

Deposition Date : 1999-09-16

Activity from ChEMBL: What is pChEMBL ?

	Min	Mean	Median	Standard Deviation	Max	Count
pChEMBL:

List of CHEMBLId :

Binding Site :

Uniprot Annotation

Name:	Vanillyl-alcohol oxidase
ID:	VAOX_PENSI
AC:	P56216
Organism:	Penicillium simplicissimum
Reign:	Eukaryota
TaxID:	69488
EC Number:	1.1.3.38

Chains:

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

Ligand binding site composition:

B-Factor:	29.523
Number of residues:	63
Including
Standard Amino Acids:	63
Non Standard Amino Acids:	0
Water Molecules:	0
Cofactors:
Metals:

Cavity properties

Ligandability	Volume (Å3)
1.123	982.125

% Hydrophobic	% Polar
45.70	54.30
According to VolSite

Ligand :

HET Code:	FAD
Formula:	C27H31N9O15P2
Molecular weight:	783.534 g/mol
DrugBank ID:	DB03147
Buried Surface Area:	71.5 %
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
91.0078	34.1113	38.4865

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
O2A	N	SER- 101	2.77	157.37	H-Bond (Protein Donor)	false
N7A	OG	SER- 101	2.71	159.31	H-Bond (Protein Donor)	false
O2A	N	ILE- 102	3.07	146.48	H-Bond (Protein Donor)	false
O2A	N	GLY- 103	3.03	158.64	H-Bond (Protein Donor)	false
O2'	O	ARG- 104	3.06	174.88	H-Bond (Ligand Donor)	false
O2P	N	ARG- 104	3.24	156.61	H-Bond (Protein Donor)	false
O1A	N	ASN- 105	3.48	120.2	H-Bond (Protein Donor)	false
C8M	CB	SER- 106	3.5	0	Hydrophobic	false
C1'	CE2	TYR- 108	4.09	0	Hydrophobic	false
O4	N	ASP- 170	2.87	152.24	H-Bond (Protein Donor)	false
C6	CB	ASP- 170	4.1	0	Hydrophobic	false
C6	CG	LEU- 171	3.82	0	Hydrophobic	false
C8M	CD1	LEU- 171	4.08	0	Hydrophobic	false
C7	CD1	LEU- 171	3.53	0	Hydrophobic	false
C7	CD1	LEU- 171	3.53	0	Hydrophobic	false
O1P	N	SER- 175	3.13	150.57	H-Bond (Protein Donor)	false
O2P	N	SER- 175	3.48	146.55	H-Bond (Protein Donor)	false
O2	ND2	ASN- 179	3.02	156.78	H-Bond (Protein Donor)	false
O4'	ND2	ASN- 179	3.18	159.94	H-Bond (Protein Donor)	false
C1B	CG2	VAL- 181	4.45	0	Hydrophobic	false
C4B	CG	GLU- 182	3.87	0	Hydrophobic	false
O2	N	VAL- 185	3.05	156.82	H-Bond (Protein Donor)	false
N3	O	VAL- 185	2.94	159.69	H-Bond (Ligand Donor)	false
O4	OH	TYR- 187	2.64	158.4	H-Bond (Protein Donor)	false
N6A	O	VAL- 262	2.74	137.49	H-Bond (Ligand Donor)	false
N1A	N	VAL- 262	2.92	146.52	H-Bond (Protein Donor)	false
C7M	CZ2	TRP- 413	3.6	0	Hydrophobic	false
C7M	CD1	ILE- 414	4.06	0	Hydrophobic	false
C8M	CD1	ILE- 414	3.86	0	Hydrophobic	false
C8M	CZ	PHE- 424	4.19	0	Hydrophobic	false
C1'	CE2	PHE- 424	4.3	0	Hydrophobic	false
N1	NH2	ARG- 504	3.39	137.65	H-Bond (Protein Donor)	false
O2	NH2	ARG- 504	3.09	132.12	H-Bond (Protein Donor)	false
O3'	NH1	ARG- 504	3.2	151.24	H-Bond (Protein Donor)	false
O3'	NH2	ARG- 504	3.47	138.74	H-Bond (Protein Donor)	false