scPDB - 2hq9 entry

Protein Data Bank Entry:

PDB ID : 2hq9

Resolution :1.950 Å

Experimental Method : X-ray

Deposition Date : 2006-07-18

Activity from ChEMBL: What is pChEMBL ?

	Min	Mean	Median	Standard Deviation	Max	Count
pChEMBL:

List of CHEMBLId :

Binding Site :

Uniprot Annotation

Name:	Mll6688 protein
ID:	Q988L5_RHILO
AC:	Q988L5
Organism:	Rhizobium loti
Reign:	Bacteria
TaxID:	266835
EC Number:	/

Chains:

Chain Name:	Percentage of Residues within binding site
A	63 %
B	37 %

Ligand binding site composition:

B-Factor:	32.433
Number of residues:	44
Including
Standard Amino Acids:	41
Non Standard Amino Acids:	0
Water Molecules:	3
Cofactors:
Metals:

Cavity properties

Ligandability	Volume (Å3)
0.310	749.250

% Hydrophobic	% Polar
44.14	55.86
According to VolSite

Ligand :

HET Code:	FAD
Formula:	C27H31N9O15P2
Molecular weight:	783.534 g/mol
DrugBank ID:	DB03147
Buried Surface Area:	63.52 %
Polar Surface area:	381.7 Å2

Number of
H-Bond Acceptors:	22
H-Bond Donors:	7
Rings:	6
Aromatic rings:	3
Anionic atoms:	2
Cationic atoms:	0
Rule of Five Violation:	3
Rotatable Bonds:	13

Mass center Coordinates

X	Y	Z
44.0346	49.5872	16.887

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
C7M	CG1	VAL- 20	4.35	0	Hydrophobic	false
C2B	CE1	TYR- 32	3.74	0	Hydrophobic	false
O1P	OH	TYR- 32	2.9	173.82	H-Bond (Protein Donor)	false
O3P	OH	TYR- 32	3.48	124.7	H-Bond (Protein Donor)	false
C2'	CB	VAL- 34	4.41	0	Hydrophobic	false
O2'	O	PRO- 35	2.82	140.71	H-Bond (Ligand Donor)	false
C7	CB	PRO- 35	4.13	0	Hydrophobic	false
C8	CG	PRO- 35	3.8	0	Hydrophobic	false
C9	CG	PRO- 35	3.69	0	Hydrophobic	false
O4	N	TYR- 37	3.11	147.17	H-Bond (Protein Donor)	false
N5	N	TYR- 37	3.23	137.61	H-Bond (Protein Donor)	false
C7M	CZ	TYR- 37	3.61	0	Hydrophobic	false
C6	CE2	TYR- 37	3.01	0	Hydrophobic	false
N3	O	PHE- 48	2.92	176	H-Bond (Ligand Donor)	false
O1A	N	LYS- 53	2.68	152.82	H-Bond (Protein Donor)	false
C5B	CB	LYS- 53	4.11	0	Hydrophobic	false
C3B	CD	LYS- 53	4.43	0	Hydrophobic	false
O4'	NZ	LYS- 54	2.6	139.24	H-Bond (Protein Donor)	false
O1P	N	LYS- 54	3.01	152.7	H-Bond (Protein Donor)	false
O2P	NZ	LYS- 54	3.85	0	Ionic (Protein Cationic)	false
C8M	CD2	TRP- 77	3.39	0	Hydrophobic	false
N6A	OG	SER- 79	3.05	134.11	H-Bond (Ligand Donor)	false
N1A	OG	SER- 79	2.73	122.21	H-Bond (Protein Donor)	false
C1'	CB	TRP- 113	4	0	Hydrophobic	false
C9A	CB	TRP- 113	3.56	0	Hydrophobic	false
O2B	OG	SER- 142	2.58	178.99	H-Bond (Ligand Donor)	false
N3A	OG	SER- 142	3.05	162.95	H-Bond (Protein Donor)	false
C1B	CB	SER- 142	3.84	0	Hydrophobic	false
O2A	CZ	ARG- 144	3.96	0	Ionic (Protein Cationic)	false
O2A	NH2	ARG- 144	3.03	168.13	H-Bond (Protein Donor)	false
O4	O	HOH- 202	2.68	179.98	H-Bond (Protein Donor)	false
O2P	O	HOH- 204	2.54	155.49	H-Bond (Protein Donor)	false