scPDB - 2ywl entry

Protein Data Bank Entry:

PDB ID : 2ywl

Resolution :1.600 Å

Experimental Method : X-ray

Deposition Date : 2007-04-20

Activity from ChEMBL: What is pChEMBL ?

	Min	Mean	Median	Standard Deviation	Max	Count
pChEMBL:

List of CHEMBLId :

Binding Site :

Uniprot Annotation

Name:	Thioredoxin reductase related protein
ID:	Q5SLC3_THET8
AC:	Q5SLC3
Organism:	Thermus thermophilus
Reign:	Bacteria
TaxID:	300852
EC Number:	/

Chains:

Chain Name:	Percentage of Residues within binding site
A	89 %
B	11 %

Ligand binding site composition:

B-Factor:	11.166
Number of residues:	61
Including
Standard Amino Acids:	56
Non Standard Amino Acids:	0
Water Molecules:	5
Cofactors:
Metals:

Cavity properties

Ligandability	Volume (Å3)
1.044	864.000

% Hydrophobic	% Polar
47.66	52.34
According to VolSite

Ligand :

HET Code:	FAD
Formula:	C27H31N9O15P2
Molecular weight:	783.534 g/mol
DrugBank ID:	DB03147
Buried Surface Area:	72.68 %
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
-10.2916	-16.5425	25.8086

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- 11	4.37	0	Hydrophobic	false
O1P	N	SER- 12	2.96	159.24	H-Bond (Protein Donor)	false
O1P	OG	SER- 12	2.65	164.59	H-Bond (Protein Donor)	false
N3A	N	GLY- 32	2.9	129.44	H-Bond (Protein Donor)	false
C2B	CB	ARG- 34	4.19	0	Hydrophobic	false
O2B	N	ARG- 34	2.9	149.36	H-Bond (Protein Donor)	false
O1A	OG	SER- 35	2.71	175.07	H-Bond (Protein Donor)	false
C3B	CB	SER- 35	4.22	0	Hydrophobic	false
O2A	N	LYS- 36	3.03	169.53	H-Bond (Protein Donor)	false
C8M	CB	LYS- 36	4.13	0	Hydrophobic	false
C9	CB	LYS- 36	4.11	0	Hydrophobic	false
C3'	CB	LYS- 36	4.35	0	Hydrophobic	false
C2'	CB	VAL- 37	4.21	0	Hydrophobic	false
C6	CG2	VAL- 40	3.79	0	Hydrophobic	false
C9A	CG2	VAL- 40	4.44	0	Hydrophobic	false
N3	OD1	ASN- 45	2.91	166.2	H-Bond (Ligand Donor)	false
N6A	O	VAL- 78	3.22	161.45	H-Bond (Ligand Donor)	false
N1A	N	VAL- 78	2.9	156.47	H-Bond (Protein Donor)	false
C5B	CB	HIS- 107	3.77	0	Hydrophobic	false
C5'	CG2	VAL- 143	3.99	0	Hydrophobic	false
O2P	N	VAL- 143	3.24	161.9	H-Bond (Protein Donor)	false
N1	N	ALA- 152	3.49	145.86	H-Bond (Protein Donor)	false
O2	N	ALA- 152	2.78	152.28	H-Bond (Protein Donor)	false
C5'	CB	SER- 155	3.92	0	Hydrophobic	false
O5'	OG	SER- 155	3.22	124.95	H-Bond (Protein Donor)	false
O2P	OG	SER- 155	2.8	166.59	H-Bond (Protein Donor)	false
C6	CB	HIS- 178	3.79	0	Hydrophobic	false
C9A	CB	HIS- 178	4.13	0	Hydrophobic	false
O4	N	ALA- 179	3.14	135.68	H-Bond (Protein Donor)	false
N5	N	ALA- 179	3.19	146.19	H-Bond (Protein Donor)	false
O2P	O	HOH- 1002	2.78	179.97	H-Bond (Protein Donor)	false
O1P	O	HOH- 1008	2.78	173.5	H-Bond (Protein Donor)	false