scPDB - 2fkn entry

Protein Data Bank Entry:

PDB ID : 2fkn

Resolution :2.200 Å

Experimental Method : X-ray

Deposition Date : 2006-01-05

Activity from ChEMBL: What is pChEMBL ?

	Min	Mean	Median	Standard Deviation	Max	Count
pChEMBL:

List of CHEMBLId :

Binding Site :

Uniprot Annotation

Name:	Urocanate hydratase
ID:	HUTU_BACSU
AC:	P25503
Organism:	Bacillus subtilis
Reign:	Bacteria
TaxID:	224308
EC Number:	4.2.1.49

Chains:

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

Ligand binding site composition:

B-Factor:	21.701
Number of residues:	65
Including
Standard Amino Acids:	63
Non Standard Amino Acids:	0
Water Molecules:	2
Cofactors:
Metals:

Cavity properties

Ligandability	Volume (Å3)
0.123	374.625

% Hydrophobic	% Polar
51.35	48.65
According to VolSite

Ligand :

HET Code:	NAD
Formula:	C21H26N7O14P2
Molecular weight:	662.417 g/mol
DrugBank ID:	-
Buried Surface Area:	83.36 %
Polar Surface area:	343.54 Å2

Number of
H-Bond Acceptors:	18
H-Bond Donors:	6
Rings:	5
Aromatic rings:	3
Anionic atoms:	2
Cationic atoms:	1
Rule of Five Violation:	3
Rotatable Bonds:	11

Mass center Coordinates

X	Y	Z
42.5618	28.8446	0.977682

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
O2N	N	GLY- 49	2.86	139.93	H-Bond (Protein Donor)	false
O2A	N	GLY- 50	2.73	147.71	H-Bond (Protein Donor)	false
O2D	NE2	GLN- 127	3.24	143.99	H-Bond (Protein Donor)	false
C4N	CD1	ILE- 141	3.38	0	Hydrophobic	false
O1A	N	GLY- 173	3.31	153.42	H-Bond (Protein Donor)	false
O1N	N	MET- 174	3.07	129.39	H-Bond (Protein Donor)	false
O2N	N	MET- 174	3.16	158.22	H-Bond (Protein Donor)	false
C5N	CG	MET- 174	3.56	0	Hydrophobic	false
O1N	N	GLY- 175	2.79	174.06	H-Bond (Protein Donor)	false
O3B	OE1	GLU- 193	2.85	170.61	H-Bond (Ligand Donor)	false
O3B	OE2	GLU- 193	3.16	125.16	H-Bond (Ligand Donor)	false
O2B	OE2	GLU- 193	2.61	168.73	H-Bond (Ligand Donor)	false
N3A	N	VAL- 194	3.42	156.5	H-Bond (Protein Donor)	false
O1A	NH1	ARG- 198	3.12	123.19	H-Bond (Protein Donor)	false
O1A	CZ	ARG- 198	3.88	0	Ionic (Protein Cationic)	false
C3B	CG	ARG- 198	4.26	0	Hydrophobic	false
N6A	OD1	ASN- 239	2.91	145.14	H-Bond (Ligand Donor)	false
N1A	N	ALA- 240	3.01	174.92	H-Bond (Protein Donor)	false
O4D	NE2	GLN- 260	3.05	170.12	H-Bond (Protein Donor)	false
C4D	CG	GLN- 260	4.13	0	Hydrophobic	false
O2A	OG	SER- 262	2.91	165.46	H-Bond (Protein Donor)	false
C5B	CB	SER- 262	3.93	0	Hydrophobic	false
C3D	CB	SER- 262	4.33	0	Hydrophobic	false
O3D	ND1	HIS- 264	2.8	167.86	H-Bond (Ligand Donor)	false
N7A	N	VAL- 271	3.01	167.32	H-Bond (Protein Donor)	false
N6A	O	VAL- 271	3.46	134.35	H-Bond (Ligand Donor)	false
N7N	O	TYR- 319	3.14	135.55	H-Bond (Ligand Donor)	false
C4D	CB	ASN- 321	4.04	0	Hydrophobic	false
O2D	O	GLY- 489	2.82	149.89	H-Bond (Ligand Donor)	false
O1N	O	HOH- 7602	2.72	179.93	H-Bond (Protein Donor)	false