scPDB - 4b1b entry

Protein Data Bank Entry:

PDB ID : 4b1b

Resolution :2.900 Å

Experimental Method : X-ray

Deposition Date : 2012-07-09

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:	TRXR_PLAF5
AC:	Q25861
Organism:	Plasmodium falciparum
Reign:	Eukaryota
TaxID:	132416
EC Number:	1.8.1.9

Chains:

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

Ligand binding site composition:

B-Factor:	22.221
Number of residues:	65
Including
Standard Amino Acids:	64
Non Standard Amino Acids:	0
Water Molecules:	1
Cofactors:
Metals:

Cavity properties

Ligandability	Volume (Å3)
1.082	867.375

% Hydrophobic	% Polar
46.69	53.31
According to VolSite

Ligand :

HET Code:	FAD
Formula:	C27H31N9O15P2
Molecular weight:	783.534 g/mol
DrugBank ID:	DB03147
Buried Surface Area:	73.97 %
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
-25.7012	6.5397	-24.4985

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
C4'	CG	PRO- 51	3.76	0	Hydrophobic	false
O1P	N	GLY- 52	2.98	147.74	H-Bond (Protein Donor)	false
O3B	OD1	ASP- 71	3.37	160.18	H-Bond (Ligand Donor)	false
O2B	O	TYR- 72	3.41	147.1	H-Bond (Ligand Donor)	false
N3A	N	TYR- 72	3.18	151.37	H-Bond (Protein Donor)	false
O1A	OG1	THR- 87	2.68	159.74	H-Bond (Protein Donor)	false
O2A	N	THR- 87	2.98	157.56	H-Bond (Protein Donor)	false
C8M	CG2	THR- 87	3.93	0	Hydrophobic	false
C2'	CB	CYS- 88	4.08	0	Hydrophobic	false
C4'	CB	CYS- 88	4.31	0	Hydrophobic	false
O4'	N	CYS- 88	3.38	146.52	H-Bond (Protein Donor)	false
C9A	SG	CYS- 93	4.32	0	Hydrophobic	false
C2'	SG	CYS- 93	4.11	0	Hydrophobic	false
N5	NZ	LYS- 96	3.18	121.39	H-Bond (Protein Donor)	false
C6	CB	LYS- 96	4.34	0	Hydrophobic	false
N6A	O	ALA- 161	3.08	164.57	H-Bond (Ligand Donor)	false
N1A	N	ALA- 161	2.75	162.03	H-Bond (Protein Donor)	false
C7M	CB	SER- 212	4.22	0	Hydrophobic	false
C7M	CE2	PHE- 216	4.4	0	Hydrophobic	false
C7M	CG1	VAL- 233	3.75	0	Hydrophobic	false
C7	CG2	VAL- 233	3.96	0	Hydrophobic	false
C8M	CD	ARG- 316	4.07	0	Hydrophobic	false
O3'	OD1	ASP- 357	3.04	156.88	H-Bond (Ligand Donor)	false
O3'	OD2	ASP- 357	3	138.5	H-Bond (Ligand Donor)	false
O2P	N	ASP- 357	2.98	121.16	H-Bond (Protein Donor)	false
N1	N	ALA- 366	3.42	154.95	H-Bond (Protein Donor)	false
O2	N	ALA- 366	3.08	138.09	H-Bond (Protein Donor)	false
C4'	CB	ALA- 366	4.19	0	Hydrophobic	false
C5'	CB	ALA- 369	3.98	0	Hydrophobic	false
O2P	O	HOH- 2002	2.87	136.81	H-Bond (Protein Donor)	false