scPDB - 4a0s entry

Protein Data Bank Entry:

PDB ID : 4a0s

Resolution :1.900 Å

Experimental Method : X-ray

Deposition Date : 2011-09-12

Activity from ChEMBL: What is pChEMBL ?

	Min	Mean	Median	Standard Deviation	Max	Count
pChEMBL:

List of CHEMBLId :

Binding Site :

Uniprot Annotation

Name:	Octenoyl-CoA reductase/carboxylase
ID:	F0V3Z3_9ACTN
AC:	F0V3Z3
Organism:	Streptomyces sp. JS360
Reign:	Bacteria
TaxID:	319633
EC Number:	/

Chains:

Chain Name:	Percentage of Residues within binding site
A	20 %
D	80 %

Ligand binding site composition:

B-Factor:	25.444
Number of residues:	50
Including
Standard Amino Acids:	45
Non Standard Amino Acids:	1
Water Molecules:	4
Cofactors:	NAP
Metals:

Cavity properties

Ligandability	Volume (Å3)
0.775	867.375

% Hydrophobic	% Polar
54.86	45.14
According to VolSite

Ligand :

HET Code:	CO8
Formula:	C29H46N7O17P3S
Molecular weight:	889.699 g/mol
DrugBank ID:	DB02910
Buried Surface Area:	52.83 %
Polar Surface area:	429.68 Å2

Number of
H-Bond Acceptors:	22
H-Bond Donors:	5
Rings:	3
Aromatic rings:	2
Anionic atoms:	4
Cationic atoms:	0
Rule of Five Violation:	2
Rotatable Bonds:	26

Mass center Coordinates

X	Y	Z
-2.94128	19.0483	52.5981

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
C2P	CB	ASN- 77	3.91	0	Hydrophobic	false
C1B	CG2	ILE- 87	4.26	0	Hydrophobic	false
C5B	CD1	ILE- 87	3.84	0	Hydrophobic	false
CAP	CD1	ILE- 87	3.79	0	Hydrophobic	false
O2A	NE2	HIS- 91	2.7	168.79	H-Bond (Protein Donor)	false
O2A	NE2	GLN- 95	2.71	121.76	H-Bond (Protein Donor)	false
C6'	CG	PRO- 141	3.49	0	Hydrophobic	false
C8'	CB	ALA- 142	3.83	0	Hydrophobic	false
C7'	CE	MET- 156	4.06	0	Hydrophobic	false
C8'	SD	MET- 156	3.64	0	Hydrophobic	false
C7'	CB	ALA- 163	3.82	0	Hydrophobic	false
C2P	CE2	PHE- 166	3.72	0	Hydrophobic	false
O7A	NH2	ARG- 286	3.11	155.6	H-Bond (Protein Donor)	false
O8A	NH1	ARG- 286	3.5	162.06	H-Bond (Protein Donor)	false
O8A	CZ	ARG- 293	3.17	0	Ionic (Protein Cationic)	false
O9A	CZ	ARG- 293	3.43	0	Ionic (Protein Cationic)	false
O4A	CZ	ARG- 293	3.69	0	Ionic (Protein Cationic)	false
O8A	NH1	ARG- 293	2.86	136.52	H-Bond (Protein Donor)	false
O8A	NH2	ARG- 293	2.65	149.36	H-Bond (Protein Donor)	false
O3A	NH2	ARG- 293	3.3	128.06	H-Bond (Protein Donor)	false
O4A	NH2	ARG- 293	3.03	127.98	H-Bond (Protein Donor)	false
CDP	CB	ARG- 348	3.74	0	Hydrophobic	false
CEP	CB	ARG- 348	4.16	0	Hydrophobic	false
O9P	NH1	ARG- 348	2.98	123.12	H-Bond (Protein Donor)	false
O4A	OH	TYR- 349	2.99	155.91	H-Bond (Protein Donor)	false
CCP	CE1	TYR- 349	4.15	0	Hydrophobic	false
CDP	CZ	TYR- 349	3.85	0	Hydrophobic	false
C6P	CZ2	TRP- 351	4.42	0	Hydrophobic	false
S1P	CZ2	TRP- 351	3.77	0	Hydrophobic	false
CEP	CG	MET- 352	3.67	0	Hydrophobic	false
C6P	SD	MET- 352	3.75	0	Hydrophobic	false
S1P	SD	MET- 352	4.47	0	Hydrophobic	false
O5A	NZ	LYS- 353	3.3	157.74	H-Bond (Protein Donor)	false
O5A	NZ	LYS- 353	3.3	0	Ionic (Protein Cationic)	false
S1P	C3N	NAP- 1445	4.42	0	Hydrophobic	false
C5'	C3N	NAP- 1445	4.49	0	Hydrophobic	false
O1'	O2D	NAP- 1445	2.89	168.65	H-Bond (Protein Donor)	false