scPDB - 3ea4 entry

Protein Data Bank Entry:

PDB ID : 3ea4

Resolution :2.800 Å

Experimental Method : X-ray

Deposition Date : 2008-08-24

Activity from ChEMBL: What is pChEMBL ?

	Min	Mean	Median	Standard Deviation	Max	Count
pChEMBL:

List of CHEMBLId :

Binding Site :

Uniprot Annotation

Name:	Acetolactate synthase, chloroplastic
ID:	ILVB_ARATH
AC:	P17597
Organism:	Arabidopsis thaliana
Reign:	Eukaryota
TaxID:	3702
EC Number:	2.2.1.6

Chains:

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

Ligand binding site composition:

B-Factor:	49.628
Number of residues:	63
Including
Standard Amino Acids:	57
Non Standard Amino Acids:	2
Water Molecules:	4
Cofactors:
Metals:

Cavity properties

Ligandability	Volume (Å3)
1.247	975.375

% Hydrophobic	% Polar
47.06	52.94
According to VolSite

Ligand :

HET Code:	FAB
Formula:	C31H38N9O16P2
Molecular weight:	854.632 g/mol
DrugBank ID:	DB03531
Buried Surface Area:	74.85 %
Polar Surface area:	389.42 Å2

Number of
H-Bond Acceptors:	22
H-Bond Donors:	7
Rings:	6
Aromatic rings:	3
Anionic atoms:	2
Cationic atoms:	1
Rule of Five Violation:	3
Rotatable Bonds:	14

Mass center Coordinates

X	Y	Z
59.6584	67.7897	53.6525

Binding mode :

What is Poseview ?

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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
C2B	CG	ARG- 246	3.84	0	Hydrophobic	false
O1A	N	GLY- 308	3.37	120.17	H-Bond (Protein Donor)	false
O2P	N	GLY- 308	2.79	159.19	H-Bond (Protein Donor)	false
C4D	CB	THR- 331	4.41	0	Hydrophobic	false
O5'	OG1	THR- 331	3.45	131.81	H-Bond (Protein Donor)	false
O2P	OG1	THR- 331	2.78	163.6	H-Bond (Protein Donor)	false
O2	N	LEU- 332	2.86	144.83	H-Bond (Protein Donor)	false
C1'	CB	LEU- 332	4.05	0	Hydrophobic	false
C9A	CD1	LEU- 332	4.16	0	Hydrophobic	false
C5D	CG	MET- 333	3.78	0	Hydrophobic	false
N3	O	LEU- 349	2.88	163.53	H-Bond (Ligand Donor)	false
O4	N	HIS- 352	2.8	171.19	H-Bond (Protein Donor)	false
O2A	CZ	ARG- 373	3.8	0	Ionic (Protein Cationic)	false
O2A	NE	ARG- 373	2.77	156.13	H-Bond (Protein Donor)	false
O1P	N	ARG- 373	3.19	163.58	H-Bond (Protein Donor)	false
C3B	CB	ARG- 373	4.36	0	Hydrophobic	false
C5D	CG	ARG- 373	4.43	0	Hydrophobic	false
O2'	OD1	ASP- 375	3.32	156.68	H-Bond (Ligand Donor)	false
C9A	CG	ARG- 377	3.9	0	Hydrophobic	false
C2D	CB	ARG- 377	3.84	0	Hydrophobic	false
O3B	OD2	ASP- 395	2.78	166.3	H-Bond (Ligand Donor)	false
O2B	OD1	ASP- 395	2.62	165.48	H-Bond (Ligand Donor)	false
C1B	CG2	ILE- 396	4.34	0	Hydrophobic	false
N3A	N	ILE- 396	3.19	138.72	H-Bond (Protein Donor)	false
N6A	OD1	ASP- 414	2.99	168.14	H-Bond (Ligand Donor)	false
N1A	N	VAL- 415	2.86	165.02	H-Bond (Protein Donor)	false
C7M	CG1	VAL- 485	4.31	0	Hydrophobic	false
C8M	CG1	VAL- 485	3.87	0	Hydrophobic	false
C6	SD	MET- 490	3.54	0	Hydrophobic	false
C7	CE	MET- 490	3.66	0	Hydrophobic	false
C7	CE	MET- 490	3.66	0	Hydrophobic	false
C7M	CE	MET- 570	3.88	0	Hydrophobic	false
O2A	O	HOH- 704	2.72	179.97	H-Bond (Protein Donor)	false