scPDB - 1tde entry

Protein Data Bank Entry:

PDB ID : 1tde

Resolution :2.100 Å

Experimental Method : X-ray

Deposition Date : 1994-01-14

Activity from ChEMBL: What is pChEMBL ?

	Min	Mean	Median	Standard Deviation	Max	Count
pChEMBL:

List of CHEMBLId :

Binding Site :

Uniprot Annotation

Name:	Thioredoxin reductase
ID:	TRXB_ECOLI
AC:	P0A9P4
Organism:	Escherichia coli
Reign:	Bacteria
TaxID:	83333
EC Number:	1.8.1.9

Chains:

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

Ligand binding site composition:

B-Factor:	18.654
Number of residues:	68
Including
Standard Amino Acids:	62
Non Standard Amino Acids:	0
Water Molecules:	6
Cofactors:
Metals:

Cavity properties

Ligandability	Volume (Å3)
1.301	1231.875

% Hydrophobic	% Polar
38.90	61.10
According to VolSite

Ligand :

HET Code:	FAD
Formula:	C27H31N9O15P2
Molecular weight:	783.534 g/mol
DrugBank ID:	DB03147
Buried Surface Area:	72.9 %
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
26.4371	31.1576	-12.0532

Binding mode :

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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
O3B	N	SER- 13	2.99	156.16	H-Bond (Protein Donor)	false
C4'	CG	PRO- 15	3.77	0	Hydrophobic	false
O1P	N	ALA- 16	3.1	154.09	H-Bond (Protein Donor)	false
O3B	O	THR- 35	3	150.14	H-Bond (Ligand Donor)	false
O2B	O	THR- 35	3.04	169	H-Bond (Ligand Donor)	false
O2B	N	GLU- 38	3.07	137.56	H-Bond (Protein Donor)	false
C2B	CB	GLU- 38	4.26	0	Hydrophobic	false
O2A	N	GLN- 42	3.03	148.69	H-Bond (Protein Donor)	false
C9A	CD1	LEU- 43	4.25	0	Hydrophobic	false
C2'	CD1	LEU- 43	3.67	0	Hydrophobic	false
C6	CB	THR- 46	3.67	0	Hydrophobic	false
N3	OD1	ASN- 51	2.7	139.8	H-Bond (Ligand Donor)	false
N6A	O	ILE- 84	2.94	151.25	H-Bond (Ligand Donor)	false
N1A	N	ILE- 84	3.01	170.65	H-Bond (Protein Donor)	false
C8M	CB	ALA- 116	4.02	0	Hydrophobic	false
C7M	CB	ALA- 134	4.04	0	Hydrophobic	false
C8M	CB	ALA- 134	4.37	0	Hydrophobic	false
C9A	CB	CYS- 135	4.21	0	Hydrophobic	false
C6	SG	CYS- 138	4.44	0	Hydrophobic	false
C9A	SG	CYS- 138	3.72	0	Hydrophobic	false
C1'	SG	CYS- 138	4.41	0	Hydrophobic	false
O3'	OD2	ASP- 286	3.02	139.79	H-Bond (Ligand Donor)	false
O3'	OD1	ASP- 286	3.1	160.73	H-Bond (Ligand Donor)	false
C5'	CB	ASP- 286	4.15	0	Hydrophobic	false
O2P	N	ASP- 286	2.96	155.2	H-Bond (Protein Donor)	false
N1	N	ALA- 295	3.43	142.15	H-Bond (Protein Donor)	false
O2	N	ALA- 295	2.92	160.06	H-Bond (Protein Donor)	false
C5'	CB	SER- 298	4.09	0	Hydrophobic	false
O2P	O	HOH- 602	2.6	172.47	H-Bond (Protein Donor)	false
O1P	O	HOH- 607	2.59	179.95	H-Bond (Protein Donor)	false
O2A	O	HOH- 615	2.83	168.17	H-Bond (Protein Donor)	false
O1A	O	HOH- 617	2.69	139.54	H-Bond (Protein Donor)	false