scPDB - 2r59 entry

Protein Data Bank Entry:

PDB ID : 2r59

Resolution :1.890 Å

Experimental Method : X-ray

Deposition Date : 2007-09-03

Activity from ChEMBL: What is pChEMBL ?

	Min	Mean	Median	Standard Deviation	Max	Count
pChEMBL:

List of CHEMBLId :

Binding Site :

Uniprot Annotation

Name:	Leukotriene A-4 hydrolase
ID:	LKHA4_HUMAN
AC:	P09960
Organism:	Homo sapiens
Reign:	Eukaryota
TaxID:	9606
EC Number:	3.3.2.6

Chains:

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

Ligand binding site composition:

B-Factor:	20.870
Number of residues:	44
Including
Standard Amino Acids:	43
Non Standard Amino Acids:	1
Water Molecules:	0
Cofactors:
Metals:	ZN

Cavity properties

Ligandability	Volume (Å3)
0.137	2642.625

% Hydrophobic	% Polar
38.70	61.30
According to VolSite

Ligand :

HET Code:	PH0
Formula:	C27H30N2O5P
Molecular weight:	493.511 g/mol
DrugBank ID:	-
Buried Surface Area:	73.13 %
Polar Surface area:	146.81 Å2

Number of
H-Bond Acceptors:	5
H-Bond Donors:	2
Rings:	3
Aromatic rings:	3
Anionic atoms:	2
Cationic atoms:	1
Rule of Five Violation:	0
Rotatable Bonds:	12

Mass center Coordinates

X	Y	Z
33.4245	6.59251	1.38886

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
N2	OE1	GLN- 136	2.91	161.52	H-Bond (Ligand Donor)	false
C7	CG	GLN- 136	4.03	0	Hydrophobic	false
C4	CB	GLN- 136	3.78	0	Hydrophobic	false
C6	CG	GLN- 136	3.64	0	Hydrophobic	false
C9	CD2	TYR- 267	4.39	0	Hydrophobic	false
C4	CZ	TYR- 267	3.25	0	Hydrophobic	false
O2	N	GLY- 268	2.75	136.2	H-Bond (Protein Donor)	false
C3	SD	MET- 270	4.26	0	Hydrophobic	false
N2	OE2	GLU- 271	3.05	0	Ionic (Ligand Cationic)	false
N2	OE1	GLU- 271	2.66	0	Ionic (Ligand Cationic)	false
N2	OE1	GLU- 271	2.66	170.53	H-Bond (Ligand Donor)	false
C24	CG2	VAL- 292	3.98	0	Hydrophobic	false
DuAr	DuAr	HIS- 295	3.84	0	Aromatic Face/Face	false
C24	CB	HIS- 295	3.76	0	Hydrophobic	false
C1	CZ	PHE- 314	4.37	0	Hydrophobic	false
N2	OE2	GLU- 318	3.2	172.38	H-Bond (Ligand Donor)	false
N2	OE2	GLU- 318	3.2	0	Ionic (Ligand Cationic)	false
C1	CE1	TYR- 378	4.05	0	Hydrophobic	false
C18	CE2	TYR- 378	3.37	0	Hydrophobic	false
C17	CB	SER- 380	4.31	0	Hydrophobic	false
O1	OH	TYR- 383	2.71	156.63	H-Bond (Protein Donor)	false
C10	CE2	TYR- 383	4.41	0	Hydrophobic	false
C17	CE1	TYR- 383	3.46	0	Hydrophobic	false
O3	CZ	ARG- 563	3.57	0	Ionic (Protein Cationic)	false
O4	CZ	ARG- 563	3.56	0	Ionic (Protein Cationic)	false
O3	NH2	ARG- 563	2.7	176.01	H-Bond (Protein Donor)	false
O4	NE	ARG- 563	2.72	175.41	H-Bond (Protein Donor)	false
O4	NH2	ARG- 563	3.5	129.42	H-Bond (Protein Donor)	false
C13	CD	LYS- 565	3.96	0	Hydrophobic	false
O1	ZN	ZN- 701	1.93	0	Metal Acceptor	false