scPDB - 3cty entry

Protein Data Bank Entry:

PDB ID : 3cty

Resolution :2.350 Å

Experimental Method : X-ray

Deposition Date : 2008-04-14

Activity from ChEMBL: What is pChEMBL ?

	Min	Mean	Median	Standard Deviation	Max	Count
pChEMBL:

List of CHEMBLId :

Binding Site :

Uniprot Annotation

Name:	Probable thioredoxin reductase
ID:	Q9HJI4_THEAC
AC:	Q9HJI4
Organism:	Thermoplasma acidophilum
Reign:	Archaea
TaxID:	273075
EC Number:	/

Chains:

Chain Name:	Percentage of Residues within binding site
A	97 %
B	3 %

Ligand binding site composition:

B-Factor:	50.288
Number of residues:	73
Including
Standard Amino Acids:	65
Non Standard Amino Acids:	0
Water Molecules:	8
Cofactors:
Metals:

Cavity properties

Ligandability	Volume (Å3)
1.313	1157.625

% Hydrophobic	% Polar
40.52	59.48
According to VolSite

Ligand :

HET Code:	FAD
Formula:	C27H31N9O15P2
Molecular weight:	783.534 g/mol
DrugBank ID:	DB03147
Buried Surface Area:	74.39 %
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
72.287	35.685	29.96

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- 27	2.91	148.83	H-Bond (Protein Donor)	false
O3B	OD2	ASP- 46	2.52	178.68	H-Bond (Ligand Donor)	false
O3B	OD1	ASP- 46	3.43	127.01	H-Bond (Ligand Donor)	false
O2B	OD1	ASP- 46	2.84	164.33	H-Bond (Ligand Donor)	false
C1B	CG	LYS- 47	4.49	0	Hydrophobic	false
N3A	N	LYS- 47	3.03	147.92	H-Bond (Protein Donor)	false
O1A	N	LEU- 53	2.84	145.79	H-Bond (Protein Donor)	false
C3'	CB	LEU- 53	4.38	0	Hydrophobic	false
C8M	CG	LEU- 53	3.72	0	Hydrophobic	false
C6	CB	ALA- 57	3.87	0	Hydrophobic	false
C9A	CB	ALA- 57	4.12	0	Hydrophobic	false
C7M	CG	PRO- 58	4.37	0	Hydrophobic	false
N3	OD1	ASN- 62	2.88	162.61	H-Bond (Ligand Donor)	false
N6A	O	VAL- 94	3.26	166.76	H-Bond (Ligand Donor)	false
N1A	N	VAL- 94	3	171.65	H-Bond (Protein Donor)	false
C7	CB	SER- 166	3.96	0	Hydrophobic	false
C8	CB	SER- 166	4.12	0	Hydrophobic	false
C6	CG2	ILE- 169	3.75	0	Hydrophobic	false
C7M	CE1	TYR- 247	3.74	0	Hydrophobic	false
C8M	CE1	TYR- 247	4.15	0	Hydrophobic	false
O3'	OD1	ASP- 288	2.94	148.26	H-Bond (Ligand Donor)	false
O3'	OD2	ASP- 288	3.16	148.5	H-Bond (Ligand Donor)	false
C5'	CB	ASP- 288	4.05	0	Hydrophobic	false
O2P	N	ASP- 288	2.87	149.84	H-Bond (Protein Donor)	false
O2	N	ILE- 297	2.77	167.04	H-Bond (Protein Donor)	false
C2'	CG1	ILE- 297	3.85	0	Hydrophobic	false
C4'	CG1	ILE- 297	4.42	0	Hydrophobic	false
C5'	CB	ALA- 300	4.46	0	Hydrophobic	false
O2P	O	HOH- 1002	2.52	165.88	H-Bond (Protein Donor)	false
O2	O	HOH- 1003	2.85	134.85	H-Bond (Protein Donor)	false
O1A	O	HOH- 1006	2.75	179.98	H-Bond (Protein Donor)	false
O1P	O	HOH- 1046	2.73	176.26	H-Bond (Protein Donor)	false