scPDB - 3ahn entry

Protein Data Bank Entry:

PDB ID : 3ahn

Resolution :1.800 Å

Experimental Method : X-ray

Deposition Date : 2010-04-25

Activity from ChEMBL: What is pChEMBL ?

	Min	Mean	Median	Standard Deviation	Max	Count
pChEMBL:

List of CHEMBLId :

Binding Site :

Uniprot Annotation

Name:	Oligopeptidase
ID:	Q4W803_9BACI
AC:	Q4W803
Organism:	Geobacillus sp. MO-1
Reign:	Bacteria
TaxID:	295930
EC Number:	/

Chains:

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

Ligand binding site composition:

B-Factor:	12.671
Number of residues:	44
Including
Standard Amino Acids:	41
Non Standard Amino Acids:	1
Water Molecules:	2
Cofactors:
Metals:	ZN

Cavity properties

Ligandability	Volume (Å3)
0.188	2575.125

% Hydrophobic	% Polar
36.44	63.56
According to VolSite

Ligand :

HET Code:	3A1
Formula:	C29H40N4O8P
Molecular weight:	603.624 g/mol
DrugBank ID:	-
Buried Surface Area:	53.91 %
Polar Surface area:	225.23 Å2

Number of
H-Bond Acceptors:	8
H-Bond Donors:	5
Rings:	2
Aromatic rings:	2
Anionic atoms:	2
Cationic atoms:	1
Rule of Five Violation:	2
Rotatable Bonds:	18

Mass center Coordinates

X	Y	Z
14.8734	-1.98343	1.60957

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
C18	CB	TYR- 328	3.64	0	Hydrophobic	false
O12	N	CYS- 329	2.92	160.37	H-Bond (Protein Donor)	false
C40	CG2	VAL- 353	4.39	0	Hydrophobic	false
OP3	OE1	GLU- 357	2.79	157.54	H-Bond (Protein Donor)	false
C3	CB	HIS- 360	3.97	0	Hydrophobic	false
C4	CG2	VAL- 364	3.72	0	Hydrophobic	false
C4	CB	TRP- 377	3.89	0	Hydrophobic	false
C7	CD2	LEU- 380	4.06	0	Hydrophobic	false
C2	CB	CYS- 383	3.92	0	Hydrophobic	false
C3	SG	CYS- 383	3.6	0	Hydrophobic	false
C54	CE	MET- 388	4.11	0	Hydrophobic	false
C54	CE1	PHE- 420	3.55	0	Hydrophobic	false
C53	CE1	PHE- 420	3.71	0	Hydrophobic	false
O80	NH2	ARG- 476	2.81	162.23	H-Bond (Protein Donor)	false
O80	NH1	ARG- 476	3.27	134.77	H-Bond (Protein Donor)	false
O80	CZ	ARG- 476	3.48	0	Ionic (Protein Cationic)	false
O68	NE2	GLN- 477	2.93	135.79	H-Bond (Protein Donor)	false
O81	NE2	GLN- 477	3.32	132.07	H-Bond (Protein Donor)	false
O46	NE2	HIS- 479	2.95	124.95	H-Bond (Protein Donor)	false
C21	CB	THR- 483	4.41	0	Hydrophobic	false
N13	OH	TYR- 486	3.01	165.44	H-Bond (Ligand Donor)	false
C16	CE2	TYR- 486	4.18	0	Hydrophobic	false
C22	CE2	TYR- 486	3.26	0	Hydrophobic	false
O68	OH	TYR- 487	2.61	126.56	H-Bond (Ligand Donor)	false
C52	CZ	TYR- 487	4.22	0	Hydrophobic	false
O36	OH	TYR- 490	2.55	165.7	H-Bond (Protein Donor)	false
C52	CD1	TYR- 490	3.56	0	Hydrophobic	false
O36	ZN	ZN- 566	2.16	0	Metal Acceptor	false
OP3	ZN	ZN- 566	2.58	0	Metal Acceptor	false
O80	O	HOH- 582	2.95	157.34	H-Bond (Protein Donor)	false