scPDB - 4opt entry

Protein Data Bank Entry:

PDB ID : 4opt

Resolution :2.600 Å

Experimental Method : X-ray

Deposition Date : 2014-02-06

Activity from ChEMBL: What is pChEMBL ?

	Min	Mean	Median	Standard Deviation	Max	Count
pChEMBL:

List of CHEMBLId :

Binding Site :

Uniprot Annotation

Name:	Conserved Archaeal protein
ID:	Q4JA33_SULAC
AC:	Q4JA33
Organism:	Sulfolobus acidocaldarius
Reign:	Archaea
TaxID:	330779
EC Number:	/

Chains:

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

Ligand binding site composition:

B-Factor:	44.053
Number of residues:	66
Including
Standard Amino Acids:	64
Non Standard Amino Acids:	0
Water Molecules:	2
Cofactors:
Metals:

Cavity properties

Ligandability	Volume (Å3)
0.266	2379.375

% Hydrophobic	% Polar
58.30	41.70
According to VolSite

Ligand :

HET Code:	FDA
Formula:	C27H33N9O15P2
Molecular weight:	785.550 g/mol
DrugBank ID:	-
Buried Surface Area:	70.67 %
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
-11.9636	23.4706	-8.67653

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- 16	3.28	168.89	H-Bond (Protein Donor)	false
O3B	OD1	ASP- 35	2.56	147.33	H-Bond (Ligand Donor)	false
O2B	OD2	ASP- 35	3.04	176.48	H-Bond (Ligand Donor)	false
N3A	N	SER- 36	3.1	138.85	H-Bond (Protein Donor)	false
O2'	NZ	LYS- 45	2.81	168.17	H-Bond (Protein Donor)	false
C6	CB	CYS- 47	4.44	0	Hydrophobic	false
C9A	SG	CYS- 47	3.76	0	Hydrophobic	false
C2'	SG	CYS- 47	3.97	0	Hydrophobic	false
N5	N	GLY- 48	2.97	149.78	H-Bond (Protein Donor)	false
N3	O	ALA- 50	2.89	129.29	H-Bond (Ligand Donor)	false
O4	N	ALA- 50	3.25	153.6	H-Bond (Protein Donor)	false
N6A	O	ALA- 122	3.3	159.26	H-Bond (Ligand Donor)	false
N1A	N	ALA- 122	3.06	158.83	H-Bond (Protein Donor)	false
N7A	OG	SER- 162	3.23	130.65	H-Bond (Protein Donor)	false
N6A	OG	SER- 162	3.17	164.72	H-Bond (Ligand Donor)	false
C7M	CB	ALA- 185	3.55	0	Hydrophobic	false
C7M	CG	ARG- 187	4.32	0	Hydrophobic	false
C7M	CH2	TRP- 217	4.13	0	Hydrophobic	false
C8M	CB	ALA- 267	3.66	0	Hydrophobic	false
C9	CG2	VAL- 269	3.53	0	Hydrophobic	false
O3'	OD1	ASP- 288	2.63	158.2	H-Bond (Ligand Donor)	false
O3'	OD2	ASP- 288	3.25	139.42	H-Bond (Ligand Donor)	false
C5'	CB	ASP- 288	4.44	0	Hydrophobic	false
O2P	N	ASP- 288	3.1	163.45	H-Bond (Protein Donor)	false
N1	N	GLY- 300	3.14	174.51	H-Bond (Protein Donor)	false
O2	N	GLY- 300	3.19	126.87	H-Bond (Protein Donor)	false
O2	N	LYS- 301	2.99	160.31	H-Bond (Protein Donor)	false
O4'	NZ	LYS- 301	2.93	151.52	H-Bond (Protein Donor)	false
C4'	CG	LYS- 301	3.68	0	Hydrophobic	false
C5'	CB	ALA- 304	4.29	0	Hydrophobic	false
O3B	O	HOH- 605	2.67	179.96	H-Bond (Protein Donor)	false