scPDB - 3fsu entry

Protein Data Bank Entry:

PDB ID : 3fsu

Resolution :1.700 Å

Experimental Method : X-ray

Deposition Date : 2009-01-12

Activity from ChEMBL: What is pChEMBL ?

	Min	Mean	Median	Standard Deviation	Max	Count
pChEMBL:

List of CHEMBLId :

Binding Site :

Uniprot Annotation

Name:	5,10-methylenetetrahydrofolate reductase
ID:	METF_ECOLI
AC:	P0AEZ1
Organism:	Escherichia coli
Reign:	Bacteria
TaxID:	83333
EC Number:	1.5.1.20

Chains:

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

Ligand binding site composition:

B-Factor:	35.251
Number of residues:	28
Including
Standard Amino Acids:	26
Non Standard Amino Acids:	1
Water Molecules:	1
Cofactors:	FAD
Metals:

Cavity properties

Ligandability	Volume (Å3)
1.161	486.000

% Hydrophobic	% Polar
63.89	36.11
According to VolSite

Ligand :

HET Code:	C2F
Formula:	C20H23N7O6
Molecular weight:	457.440 g/mol
DrugBank ID:	-
Buried Surface Area:	48.6 %
Polar Surface area:	204.14 Å2

Number of
H-Bond Acceptors:	11
H-Bond Donors:	5
Rings:	3
Aromatic rings:	1
Anionic atoms:	2
Cationic atoms:	0
Rule of Five Violation:	1
Rotatable Bonds:	9

Mass center Coordinates

X	Y	Z
-8.91548	18.9133	56.1271

Binding mode :

What is Poseview ?

2D View
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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
C11	CG2	THR- 59	3.83	0	Hydrophobic	false
NA2	OD1	ASP- 120	2.96	129.88	H-Bond (Ligand Donor)	false
N3	OD1	ASP- 120	3.39	120.14	H-Bond (Ligand Donor)	false
N3	OD2	ASP- 120	2.67	166.05	H-Bond (Ligand Donor)	false
N1	NE2	GLN- 183	2.94	174.91	H-Bond (Protein Donor)	false
N8	OE1	GLN- 183	2.57	168.67	H-Bond (Ligand Donor)	false
C9	CE2	PHE- 184	4.45	0	Hydrophobic	false
C13	CD2	LEU- 212	4.03	0	Hydrophobic	false
C14	CD1	LEU- 212	4.05	0	Hydrophobic	false
CB	CB	ASN- 216	4.44	0	Hydrophobic	false
CB	CG	GLN- 219	4.5	0	Hydrophobic	false
O2	NE2	GLN- 219	2.6	167.26	H-Bond (Protein Donor)	false
C9	CD2	LEU- 223	4.08	0	Hydrophobic	false
C16	CD2	LEU- 223	4.5	0	Hydrophobic	false
C13	CD2	LEU- 223	3.66	0	Hydrophobic	false
C14	CD2	LEU- 223	3.34	0	Hydrophobic	false
C9	CD1	TYR- 275	4.49	0	Hydrophobic	false
C7	CE1	TYR- 275	3.34	0	Hydrophobic	false
C16	CD2	LEU- 277	3.55	0	Hydrophobic	false
CG	CD1	LEU- 277	3.5	0	Hydrophobic	false
C15	CD2	LEU- 277	3.72	0	Hydrophobic	false
C12	CD2	LEU- 277	3.52	0	Hydrophobic	false
OE1	NE	ARG- 279	2.74	165.89	H-Bond (Protein Donor)	false
OE1	NH2	ARG- 279	3.29	131.94	H-Bond (Protein Donor)	false
OE1	CZ	ARG- 279	3.45	0	Ionic (Protein Cationic)	false
OE2	O	HOH- 336	2.85	179.98	H-Bond (Protein Donor)	false
C7	C8	FAD- 395	4.24	0	Hydrophobic	false
C11	C9A	FAD- 395	4.15	0	Hydrophobic	false