scPDB - 2o2q entry

Protein Data Bank Entry:

PDB ID : 2o2q

Resolution :2.000 Å

Experimental Method : X-ray

Deposition Date : 2006-11-30

Activity from ChEMBL: What is pChEMBL ?

	Min	Mean	Median	Standard Deviation	Max	Count
pChEMBL:

List of CHEMBLId :

Binding Site :

Uniprot Annotation

Name:	Cytosolic 10-formyltetrahydrofolate dehydrogenase
ID:	AL1L1_RAT
AC:	P28037
Organism:	Rattus norvegicus
Reign:	Eukaryota
TaxID:	10116
EC Number:	1.5.1.6

Chains:

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

Ligand binding site composition:

B-Factor:	18.256
Number of residues:	57
Including
Standard Amino Acids:	54
Non Standard Amino Acids:	1
Water Molecules:	2
Cofactors:
Metals:	MG

Cavity properties

Ligandability	Volume (Å3)
0.434	739.125

% Hydrophobic	% Polar
52.05	47.95
According to VolSite

Ligand :

HET Code:	NAP
Formula:	C21H25N7O17P3
Molecular weight:	740.381 g/mol
DrugBank ID:	DB03461
Buried Surface Area:	71.11 %
Polar Surface area:	405.54 Å2

Number of
H-Bond Acceptors:	21
H-Bond Donors:	5
Rings:	5
Aromatic rings:	3
Anionic atoms:	4
Cationic atoms:	1
Rule of Five Violation:	2
Rotatable Bonds:	13

Mass center Coordinates

X	Y	Z
59.1874	28.1304	56.4211

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
C1B	CG1	VAL- 570	3.62	0	Hydrophobic	false
C4B	CG1	VAL- 570	3.66	0	Hydrophobic	false
O3B	O	ILE- 571	2.85	175.71	H-Bond (Ligand Donor)	false
C5B	CB	PRO- 572	4.37	0	Hydrophobic	false
C5N	CG	PRO- 572	3.93	0	Hydrophobic	false
C5D	CZ2	TRP- 573	4.26	0	Hydrophobic	false
C4N	SD	MET- 579	4.04	0	Hydrophobic	false
O2B	NZ	LYS- 597	2.94	170.83	H-Bond (Protein Donor)	false
O2X	NZ	LYS- 597	3	0	Ionic (Protein Cationic)	false
O2X	N	GLN- 600	2.69	179.01	H-Bond (Protein Donor)	false
O3X	N	GLY- 630	2.73	176.29	H-Bond (Protein Donor)	false
N6A	OE1	GLN- 635	3.18	162.9	H-Bond (Ligand Donor)	false
C1B	CE1	PHE- 648	4.3	0	Hydrophobic	false
C4B	CE1	PHE- 648	3.76	0	Hydrophobic	false
C4N	CG2	THR- 649	3.32	0	Hydrophobic	false
O1A	N	SER- 651	2.72	165.55	H-Bond (Protein Donor)	false
O1A	OG	SER- 651	2.71	161.96	H-Bond (Protein Donor)	false
O3	N	SER- 651	3.46	128.66	H-Bond (Protein Donor)	false
C1B	CG1	VAL- 654	4.26	0	Hydrophobic	false
N7N	OE1	GLU- 673	3.48	147.32	H-Bond (Ligand Donor)	false
N7N	O	LEU- 674	2.98	169.65	H-Bond (Ligand Donor)	false
C2D	CB	CYS- 707	4.31	0	Hydrophobic	false
C5N	SG	CYS- 707	3.46	0	Hydrophobic	false
O3D	OE1	GLU- 804	2.69	164.4	H-Bond (Ligand Donor)	false
O2D	OE2	GLU- 804	2.63	147.83	H-Bond (Ligand Donor)	false
O2D	OE1	GLU- 804	3.27	147.76	H-Bond (Ligand Donor)	false
C5D	CE2	PHE- 806	3.7	0	Hydrophobic	false
C2D	CE1	PHE- 806	3.33	0	Hydrophobic	false
O2A	MG	MG- 2004	2.51	0	Metal Acceptor	false
O1N	MG	MG- 2004	2.72	0	Metal Acceptor	false
O2N	MG	MG- 2004	2.17	0	Metal Acceptor	false