scPDB - 3fg2 entry

Protein Data Bank Entry:

PDB ID : 3fg2

Resolution :2.200 Å

Experimental Method : X-ray

Deposition Date : 2008-12-04

Activity from ChEMBL: What is pChEMBL ?

	Min	Mean	Median	Standard Deviation	Max	Count
pChEMBL:

List of CHEMBLId :

Binding Site :

Uniprot Annotation

Name:	Putative rubredoxin reductase
ID:	Q6N3B2_RHOPA
AC:	Q6N3B2
Organism:	Rhodopseudomonas palustris
Reign:	Bacteria
TaxID:	258594
EC Number:	/

Chains:

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

Ligand binding site composition:

B-Factor:	27.192
Number of residues:	62
Including
Standard Amino Acids:	53
Non Standard Amino Acids:	0
Water Molecules:	9
Cofactors:
Metals:

Cavity properties

Ligandability	Volume (Å3)
0.008	654.750

% Hydrophobic	% Polar
36.08	63.92
According to VolSite

Ligand :

HET Code:	FAD
Formula:	C27H31N9O15P2
Molecular weight:	783.534 g/mol
DrugBank ID:	DB03147
Buried Surface Area:	72.59 %
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
115.272	150.072	82.1164

Binding mode :

What is Poseview ?

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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
O2A	N	HIS- 11	3.41	151.35	H-Bond (Protein Donor)	false
C4'	CB	HIS- 11	4.22	0	Hydrophobic	false
O1P	N	ALA- 12	2.63	140.12	H-Bond (Protein Donor)	false
O2B	OD2	ASP- 34	2.57	160.92	H-Bond (Ligand Donor)	false
O3B	OE1	GLU- 35	2.59	155.24	H-Bond (Ligand Donor)	false
O2A	CZ	ARG- 42	3.64	0	Ionic (Protein Cationic)	false
C8M	CG	ARG- 42	4.26	0	Hydrophobic	false
C2'	CB	ARG- 42	4.36	0	Hydrophobic	false
C9	CB	ARG- 42	3.94	0	Hydrophobic	false
C7M	CB	LEU- 45	3.71	0	Hydrophobic	false
C7M	CB	SER- 46	3.83	0	Hydrophobic	false
O4	NZ	LYS- 47	2.96	151.23	H-Bond (Protein Donor)	false
N5	NZ	LYS- 47	3.14	130.22	H-Bond (Protein Donor)	false
N6A	O	MET- 79	3.07	145.99	H-Bond (Ligand Donor)	false
N1A	N	MET- 79	3.12	157.7	H-Bond (Protein Donor)	false
C8M	CB	ARG- 127	3.83	0	Hydrophobic	false
C6	CG1	ILE- 153	4.23	0	Hydrophobic	false
C8M	CD1	ILE- 153	3.87	0	Hydrophobic	false
C7	CD1	ILE- 153	3.73	0	Hydrophobic	false
C8	CD1	ILE- 153	3.67	0	Hydrophobic	false
O3'	OD1	ASP- 275	2.93	161.95	H-Bond (Ligand Donor)	false
O3'	OD2	ASP- 275	3.47	134.84	H-Bond (Ligand Donor)	false
C5'	CB	ASP- 275	4.12	0	Hydrophobic	false
O2P	N	ASP- 275	3.05	150.8	H-Bond (Protein Donor)	false
O2	N	VAL- 293	3.19	167.77	H-Bond (Protein Donor)	false
C2'	CG2	VAL- 293	4.19	0	Hydrophobic	false
C5'	CB	ALA- 296	4.07	0	Hydrophobic	false
O2	O	HOH- 407	2.95	179.98	H-Bond (Protein Donor)	false
O2P	O	HOH- 408	2.52	164.97	H-Bond (Protein Donor)	false
O1P	O	HOH- 412	2.7	170.66	H-Bond (Protein Donor)	false
O1A	O	HOH- 416	2.72	179.93	H-Bond (Protein Donor)	false
O3B	O	HOH- 445	2.86	179.95	H-Bond (Protein Donor)	false