scPDB - 2e7f entry

Protein Data Bank Entry:

PDB ID : 2e7f

Resolution :2.200 Å

Experimental Method : X-ray

Deposition Date : 2007-01-09

Activity from ChEMBL: What is pChEMBL ?

	Min	Mean	Median	Standard Deviation	Max	Count
pChEMBL:

List of CHEMBLId :

Binding Site :

Uniprot Annotation

Name:	5-methyltetrahydrofolate:corrinoid/iron-sulfur protein co-methyltransferase
ID:	ACSE_MOOTH
AC:	Q46389
Organism:	Moorella thermoacetica
Reign:	Bacteria
TaxID:	1525
EC Number:	2.1.1.258

Chains:

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

Ligand binding site composition:

B-Factor:	13.107
Number of residues:	31
Including
Standard Amino Acids:	28
Non Standard Amino Acids:	0
Water Molecules:	3
Cofactors:
Metals:

Cavity properties

Ligandability	Volume (Å3)
0.002	384.750

% Hydrophobic	% Polar
42.98	57.02
According to VolSite

Ligand :

HET Code:	C2F
Formula:	C20H23N7O6
Molecular weight:	457.440 g/mol
DrugBank ID:	-
Buried Surface Area:	50.98 %
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
-10.1743	70.1193	116.722

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
C14	CB	GLU- 6	4.07	0	Hydrophobic	false
C12	SD	MET- 11	4.13	0	Hydrophobic	false
CB	SD	MET- 11	3.62	0	Hydrophobic	false
C13	CE	MET- 11	3.71	0	Hydrophobic	false
CG	CE1	PHE- 12	3.38	0	Hydrophobic	false
N8	OD1	ASP- 75	3.05	145.27	H-Bond (Ligand Donor)	false
N1	ND2	ASN- 96	3	157.09	H-Bond (Protein Donor)	false
NA2	OD1	ASN- 96	2.83	147.98	H-Bond (Ligand Donor)	false
NA2	OD2	ASP- 160	2.9	132.18	H-Bond (Ligand Donor)	false
N3	OD2	ASP- 160	2.58	150.47	H-Bond (Ligand Donor)	false
C17	CB	SER- 198	3.49	0	Hydrophobic	false
O1	NE2	GLN- 202	2.56	166.59	H-Bond (Protein Donor)	false
O2	NE2	GLN- 202	3.3	131.65	H-Bond (Protein Donor)	false
O	NH2	ARG- 207	3.12	128.12	H-Bond (Protein Donor)	false
O	NH1	ARG- 207	2.86	136.31	H-Bond (Protein Donor)	false
O2	NH2	ARG- 207	3	126.33	H-Bond (Protein Donor)	false
C9	CG2	ILE- 227	3.89	0	Hydrophobic	false
O4	O	HOH- 3002	2.84	152.38	H-Bond (Protein Donor)	false
N10	O	HOH- 3005	3.25	155.64	H-Bond (Ligand Donor)	false