scPDB - 1ozh entry

Protein Data Bank Entry:

PDB ID : 1ozh

Resolution :2.000 Å

Experimental Method : X-ray

Deposition Date : 2003-04-09

Activity from ChEMBL: What is pChEMBL ?

	Min	Mean	Median	Standard Deviation	Max	Count
pChEMBL:

List of CHEMBLId :

Binding Site :

Uniprot Annotation

Name:	Acetolactate synthase, catabolic
ID:	ILVB_KLEPN
AC:	P27696
Organism:	Klebsiella pneumoniae
Reign:	Bacteria
TaxID:	573
EC Number:	2.2.1.6

Chains:

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

Ligand binding site composition:

B-Factor:	20.869
Number of residues:	50
Including
Standard Amino Acids:	46
Non Standard Amino Acids:	1
Water Molecules:	3
Cofactors:
Metals:	MG

Cavity properties

Ligandability	Volume (Å3)
1.085	421.875

% Hydrophobic	% Polar
52.00	48.00
According to VolSite

Ligand :

HET Code:	HE3
Formula:	C14H20N4O8P2S
Molecular weight:	466.343 g/mol
DrugBank ID:	DB03361
Buried Surface Area:	81.41 %
Polar Surface area:	229.18 Å2

Number of
H-Bond Acceptors:	12
H-Bond Donors:	3
Rings:	3
Aromatic rings:	1
Anionic atoms:	3
Cationic atoms:	1
Rule of Five Violation:	1
Rotatable Bonds:	7

Mass center Coordinates

X	Y	Z
11.9989	8.39407	-0.156207

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
CM4	CG2	ILE- 32	3.73	0	Hydrophobic	false
C7'	CG2	THR- 80	4.01	0	Hydrophobic	false
CM2	CB	PRO- 83	3.72	0	Hydrophobic	false
S1	CG	MET- 394	3.51	0	Hydrophobic	false
C8	CG	MET- 394	4.07	0	Hydrophobic	false
O2B	N	SER- 396	2.74	174.14	H-Bond (Protein Donor)	false
C8	CB	GLN- 420	3.86	0	Hydrophobic	false
O9	OE1	GLN- 420	3.33	134.19	H-Bond (Ligand Donor)	false
CM2	CG2	THR- 421	4.27	0	Hydrophobic	false
N3'	N	MET- 422	3.31	158.95	H-Bond (Protein Donor)	false
CM2	CG	MET- 422	3.57	0	Hydrophobic	false
C5'	SD	MET- 422	4.25	0	Hydrophobic	false
CM4	SD	MET- 422	4.14	0	Hydrophobic	false
C6	CE	MET- 422	3.81	0	Hydrophobic	false
S1	CB	MET- 422	4.43	0	Hydrophobic	false
O2A	N	GLY- 448	2.74	156.86	H-Bond (Protein Donor)	false
O3A	N	GLY- 449	2.92	144.2	H-Bond (Protein Donor)	false
CM4	CG	TYR- 477	3.68	0	Hydrophobic	false
C7	CD2	TYR- 477	3.79	0	Hydrophobic	false
O3B	N	ASN- 478	2.82	150.77	H-Bond (Protein Donor)	false
C9	CE	MET- 479	3.49	0	Hydrophobic	false
O2B	N	MET- 479	2.89	142.8	H-Bond (Protein Donor)	false
C9	CG2	VAL- 480	4.34	0	Hydrophobic	false
C7'	CG2	VAL- 480	4.07	0	Hydrophobic	false
CM4	CG2	VAL- 480	3.56	0	Hydrophobic	false
O1B	OH	TYR- 543	2.64	151.51	H-Bond (Protein Donor)	false
O2A	MG	MG- 1412	2.09	0	Metal Acceptor	false
O3B	MG	MG- 1412	2.14	0	Metal Acceptor	false
O3A	O	HOH- 1446	2.7	157.53	H-Bond (Protein Donor)	false