scPDB - 3ahe entry

Protein Data Bank Entry:

PDB ID : 3ahe

Resolution :2.100 Å

Experimental Method : X-ray

Deposition Date : 2010-04-22

Activity from ChEMBL: What is pChEMBL ?

	Min	Mean	Median	Standard Deviation	Max	Count
pChEMBL:

List of CHEMBLId :

Binding Site :

Uniprot Annotation

Name:	Probable phosphoketolase
ID:	D6PAH1_BIFBR
AC:	D6PAH1
Organism:	Bifidobacterium breve
Reign:	Bacteria
TaxID:	1685
EC Number:	/

Chains:

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

Ligand binding site composition:

B-Factor:	14.532
Number of residues:	37
Including
Standard Amino Acids:	32
Non Standard Amino Acids:	1
Water Molecules:	4
Cofactors:
Metals:	MG

Cavity properties

Ligandability	Volume (Å3)
0.597	239.625

% Hydrophobic	% Polar
67.61	32.39
According to VolSite

Ligand :

HET Code:	THD
Formula:	C14H19N4O9P2S
Molecular weight:	481.335 g/mol
DrugBank ID:	-
Buried Surface Area:	58.12 %
Polar Surface area:	262.2 Å2

Number of
H-Bond Acceptors:	14
H-Bond Donors:	3
Rings:	2
Aromatic rings:	1
Anionic atoms:	3
Cationic atoms:	0
Rule of Five Violation:	1
Rotatable Bonds:	9

Mass center Coordinates

X	Y	Z
62.7198	48.3532	11.0124

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
O2B	OG1	THR- 67	2.58	150.62	H-Bond (Protein Donor)	false
O3B	NE2	HIS- 97	2.73	171.92	H-Bond (Protein Donor)	false
C9	CB	HIS- 97	3.81	0	Hydrophobic	false
O10	NE2	HIS- 142	2.84	168.78	H-Bond (Protein Donor)	false
N4'	O	GLY- 155	2.77	143.09	H-Bond (Ligand Donor)	false
CM2	CG	GLU- 156	3.74	0	Hydrophobic	false
CM2	CB	LEU- 157	4.43	0	Hydrophobic	false
S1	CD1	LEU- 157	4.07	0	Hydrophobic	false
C7	CD1	LEU- 157	3.68	0	Hydrophobic	false
N3'	N	LEU- 157	3.02	164.57	H-Bond (Protein Donor)	false
O1A	N	GLY- 183	3.28	122.96	H-Bond (Protein Donor)	false
O2A	N	GLY- 183	2.75	146.36	H-Bond (Protein Donor)	false
O1A	N	GLU- 184	2.96	151.67	H-Bond (Protein Donor)	false
O1B	ND2	ASN- 215	3.14	144.56	H-Bond (Protein Donor)	false
O2B	ND2	ASN- 215	3.19	140.54	H-Bond (Protein Donor)	false
C6	CB	LYS- 218	3.84	0	Hydrophobic	false
S1	CG1	ILE- 219	4.24	0	Hydrophobic	false
CM4	CD1	ILE- 219	3.72	0	Hydrophobic	false
C6	CG1	ILE- 219	3.64	0	Hydrophobic	false
O1B	NZ	LYS- 300	2.67	158.05	H-Bond (Protein Donor)	false
O1B	NZ	LYS- 300	2.67	0	Ionic (Protein Cationic)	false
O3B	NZ	LYS- 300	3.18	0	Ionic (Protein Cationic)	false
O2A	MG	MG- 826	2.11	0	Metal Acceptor	false
O1B	MG	MG- 826	2.15	0	Metal Acceptor	false
O3B	O	HOH- 890	2.77	129.39	H-Bond (Protein Donor)	false
O2B	O	HOH- 1240	2.65	120.34	H-Bond (Protein Donor)	false