scPDB - 2fut entry

Protein Data Bank Entry:

PDB ID : 2fut

Resolution :2.300 Å

Experimental Method : X-ray

Deposition Date : 2006-01-27

Activity from ChEMBL: What is pChEMBL ?

	Min	Mean	Median	Standard Deviation	Max	Count
pChEMBL:

List of CHEMBLId :

Binding Site :

Uniprot Annotation

Name:	Heparin and heparin-sulfate lyase
ID:	HEPB_PEDHD
AC:	C6XZB6
Organism:	Pedobacter heparinus
Reign:	Bacteria
TaxID:	485917
EC Number:	/

Chains:

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

Ligand binding site composition:

B-Factor:	32.222
Number of residues:	35
Including
Standard Amino Acids:	33
Non Standard Amino Acids:	0
Water Molecules:	2
Cofactors:
Metals:

Cavity properties

Ligandability	Volume (Å3)
0.290	475.875

% Hydrophobic	% Polar
33.33	66.67
According to VolSite

Ligand :

HET Code:	H1S
Formula:	C12H15NO19S3
Molecular weight:	573.438 g/mol
DrugBank ID:	DB02322
Buried Surface Area:	57.73 %
Polar Surface area:	355.74 Å2

Number of
H-Bond Acceptors:	19
H-Bond Donors:	4
Rings:	2
Aromatic rings:	0
Anionic atoms:	4
Cationic atoms:	0
Rule of Five Violation:	2
Rotatable Bonds:	10

Mass center Coordinates

X	Y	Z
0.0811714	104.31	38.1958

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
O25	OD1	ASP- 145	2.76	146.66	H-Bond (Ligand Donor)	false
O25	OD2	ASP- 145	3.08	141.49	H-Bond (Ligand Donor)	false
O3	NE2	HIS- 202	3.46	125.46	H-Bond (Protein Donor)	false
O25	NE2	HIS- 202	3.22	164.7	H-Bond (Protein Donor)	false
O34	OE2	GLU- 205	3.17	155.74	H-Bond (Protein Donor)	false
O35	OE2	GLU- 205	2.61	136.26	H-Bond (Protein Donor)	false
O34	NH2	ARG- 261	2.82	144.58	H-Bond (Protein Donor)	false
O34	CZ	ARG- 261	3.94	0	Ionic (Protein Cationic)	false
O9	ND2	ASN- 405	2.74	160.93	H-Bond (Protein Donor)	false
O34	NE2	HIS- 406	2.77	171.88	H-Bond (Protein Donor)	false
O13	OH	TYR- 429	3.22	121.85	H-Bond (Protein Donor)	false
O18	OH	TYR- 429	2.89	124.77	H-Bond (Protein Donor)	false
C1	CG	TYR- 436	4	0	Hydrophobic	false
C2	CD2	TYR- 436	4.13	0	Hydrophobic	false
C6	CB	TYR- 436	3.8	0	Hydrophobic	false
C7	CB	TYR- 436	4.2	0	Hydrophobic	false
C10	CE2	TYR- 436	4.21	0	Hydrophobic	false
C8	CZ	TYR- 436	3.88	0	Hydrophobic	false
O32	N	TYR- 436	3.35	155.75	H-Bond (Protein Donor)	false
O21	ND2	ASN- 437	2.73	131.71	H-Bond (Protein Donor)	false
O21	N	GLY- 470	2.87	139.95	H-Bond (Protein Donor)	false
O15	O	HOH- 873	3.11	179.94	H-Bond (Protein Donor)	false
O28	O	HOH- 1007	3.07	179.96	H-Bond (Protein Donor)	false