scPDB - 3jrx entry

Protein Data Bank Entry:

PDB ID : 3jrx

Resolution :2.500 Å

Experimental Method : X-ray

Deposition Date : 2009-09-09

Activity from ChEMBL: What is pChEMBL ?

	Min	Mean	Median	Standard Deviation	Max	Count
pChEMBL:

List of CHEMBLId :

Binding Site :

Uniprot Annotation

Name:	Acetyl-CoA carboxylase 2
ID:	ACACB_HUMAN
AC:	O00763
Organism:	Homo sapiens
Reign:	Eukaryota
TaxID:	9606
EC Number:	/

Chains:

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

Ligand binding site composition:

B-Factor:	31.462
Number of residues:	36
Including
Standard Amino Acids:	36
Non Standard Amino Acids:	0
Water Molecules:	0
Cofactors:
Metals:

Cavity properties

Ligandability	Volume (Å3)
1.119	536.625

% Hydrophobic	% Polar
62.89	37.11
According to VolSite

Ligand :

HET Code:	S1A
Formula:	C29H44O8
Molecular weight:	520.655 g/mol
DrugBank ID:	DB02859
Buried Surface Area:	64.74 %
Polar Surface area:	103.68 Å2

Number of
H-Bond Acceptors:	8
H-Bond Donors:	2
Rings:	3
Aromatic rings:	1
Anionic atoms:	0
Cationic atoms:	0
Rule of Five Violation:	1
Rotatable Bonds:	4

Mass center Coordinates

X	Y	Z
-44.8614	23.6436	-16.9366

Binding mode :

What is Poseview ?

2D View
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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
C24	CD1	ILE- 270	3.99	0	Hydrophobic	false
C24	CG1	VAL- 273	3.75	0	Hydrophobic	false
C13	CD	LYS- 274	3.77	0	Hydrophobic	false
C24	CD	LYS- 274	4.09	0	Hydrophobic	false
O5	NZ	LYS- 274	3.09	138.01	H-Bond (Protein Donor)	false
C22	CB	ARG- 277	4.17	0	Hydrophobic	false
O11	NE	ARG- 277	3.21	127.85	H-Bond (Protein Donor)	false
O11	NH2	ARG- 277	3.17	126.9	H-Bond (Protein Donor)	false
O12	NE	ARG- 277	3.27	145.17	H-Bond (Protein Donor)	false
O12	NH2	ARG- 277	3.42	137.78	H-Bond (Protein Donor)	false
O5	OG	SER- 278	2.66	170.33	H-Bond (Protein Donor)	false
C6	CB	SER- 278	4.38	0	Hydrophobic	false
C21	CG	ARG- 281	3.97	0	Hydrophobic	false
C22	CB	ARG- 281	4.2	0	Hydrophobic	false
C26	CB	PRO- 590	4.38	0	Hydrophobic	false
C16	CB	PRO- 590	3.73	0	Hydrophobic	false
C4	CB	GLU- 593	4.05	0	Hydrophobic	false
C19	CB	GLU- 593	3.53	0	Hydrophobic	false
C20	CB	GLU- 593	3.91	0	Hydrophobic	false
O5	OE2	GLU- 593	2.79	165.82	H-Bond (Ligand Donor)	false
C2	CE	MET- 594	4.24	0	Hydrophobic	false
C19	CB	MET- 594	3.88	0	Hydrophobic	false
C25	CE	MET- 594	3.68	0	Hydrophobic	false
C5	CB	ASN- 599	4.19	0	Hydrophobic	false
C27	CG2	VAL- 648	4.18	0	Hydrophobic	false
C12	CZ2	TRP- 681	3.78	0	Hydrophobic	false
C13	CH2	TRP- 681	4.06	0	Hydrophobic	false
C24	CZ2	TRP- 681	3.9	0	Hydrophobic	false
C30	CB	TRP- 681	3.89	0	Hydrophobic	false
C16	CE3	TRP- 681	3.72	0	Hydrophobic	false
C16	CD2	PHE- 704	4.28	0	Hydrophobic	false
C28	CB	PHE- 704	3.61	0	Hydrophobic	false
C28	CB	TRP- 706	3.91	0	Hydrophobic	false