scPDB - 4ge4 entry

Protein Data Bank Entry:

PDB ID : 4ge4

Resolution :2.410 Å

Experimental Method : X-ray

Deposition Date : 2012-08-01

Activity from ChEMBL: What is pChEMBL ?

	Min	Mean	Median	Standard Deviation	Max	Count
pChEMBL:

List of CHEMBLId :

Binding Site :

Uniprot Annotation

Name:	Kynurenine/alpha-aminoadipate aminotransferase, mitochondrial
ID:	AADAT_HUMAN
AC:	Q8N5Z0
Organism:	Homo sapiens
Reign:	Eukaryota
TaxID:	9606
EC Number:	2.6.1.39

Chains:

Chain Name:	Percentage of Residues within binding site
A	70 %
B	30 %

Ligand binding site composition:

B-Factor:	39.903
Number of residues:	46
Including
Standard Amino Acids:	44
Non Standard Amino Acids:	0
Water Molecules:	2
Cofactors:
Metals:

Cavity properties

Ligandability	Volume (Å3)
1.209	894.375

% Hydrophobic	% Polar
52.83	47.17
According to VolSite

Ligand :

HET Code:	0KE
Formula:	C18H17N3O8P
Molecular weight:	434.317 g/mol
DrugBank ID:	-
Buried Surface Area:	74.55 %
Polar Surface area:	179.98 Å2

Number of
H-Bond Acceptors:	10
H-Bond Donors:	2
Rings:	3
Aromatic rings:	2
Anionic atoms:	3
Cationic atoms:	0
Rule of Five Violation:	1
Rotatable Bonds:	7

Mass center Coordinates

X	Y	Z
26.3012	-0.796733	-16.0799

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
C10	CG2	ILE- 19	3.53	0	Hydrophobic	false
C15	CG1	ILE- 19	3.62	0	Hydrophobic	false
N5	N	GLY- 39	3.18	153.74	H-Bond (Protein Donor)	false
O6	N	GLY- 39	2.64	160.8	H-Bond (Protein Donor)	false
C10	CD2	LEU- 40	3.97	0	Hydrophobic	false
C12	CD2	LEU- 40	3.57	0	Hydrophobic	false
C10	CB	TYR- 74	4.33	0	Hydrophobic	false
C14	CD2	TYR- 74	3.42	0	Hydrophobic	false
C13	CB	TYR- 74	3.83	0	Hydrophobic	false
O28	OH	TYR- 74	2.66	160.39	H-Bond (Protein Donor)	false
O29	OG	SER- 117	2.7	171.58	H-Bond (Protein Donor)	false
O29	N	SER- 117	2.85	153.44	H-Bond (Protein Donor)	false
C25	CB	GLN- 118	4.05	0	Hydrophobic	false
O30	N	GLN- 118	2.96	155.4	H-Bond (Protein Donor)	false
C24	CG	TYR- 142	3.77	0	Hydrophobic	false
C11	CZ	TYR- 142	3.8	0	Hydrophobic	false
C25	CZ	TYR- 142	4.11	0	Hydrophobic	false
DuAr	DuAr	TYR- 142	3.64	0	Aromatic Face/Face	false
C24	CG2	VAL- 197	3.71	0	Hydrophobic	false
C24	CB	ASN- 202	4.05	0	Hydrophobic	false
O7	ND2	ASN- 202	2.85	130.71	H-Bond (Protein Donor)	false
O23	ND2	ASN- 202	2.77	169.28	H-Bond (Protein Donor)	false
N20	OD2	ASP- 230	2.66	158.47	H-Bond (Ligand Donor)	false
N20	OD1	ASP- 230	3.18	138.33	H-Bond (Ligand Donor)	false
C18	CG	PRO- 232	4	0	Hydrophobic	false
C24	CG	PRO- 232	3.73	0	Hydrophobic	false
C24	CE1	TYR- 233	4.07	0	Hydrophobic	false
O29	OG	SER- 260	2.55	158.03	H-Bond (Protein Donor)	false
O28	OG	SER- 262	2.69	163.06	H-Bond (Protein Donor)	false
O30	NH2	ARG- 270	2.66	164.67	H-Bond (Protein Donor)	false
O28	NH1	ARG- 270	2.96	159.71	H-Bond (Protein Donor)	false
O30	CZ	ARG- 270	3.65	0	Ionic (Protein Cationic)	false
O28	CZ	ARG- 270	3.69	0	Ionic (Protein Cationic)	false
C14	CD1	LEU- 293	4.32	0	Hydrophobic	false
C25	CD1	LEU- 293	4.47	0	Hydrophobic	false
O7	NH1	ARG- 399	3.17	146.07	H-Bond (Protein Donor)	false
O6	NH2	ARG- 399	2.73	156.66	H-Bond (Protein Donor)	false