scPDB - 1cqx entry

Protein Data Bank Entry:

PDB ID : 1cqx

Resolution :1.750 Å

Experimental Method : X-ray

Deposition Date : 1999-08-12

Activity from ChEMBL: What is pChEMBL ?

	Min	Mean	Median	Standard Deviation	Max	Count
pChEMBL:

List of CHEMBLId :

Binding Site :

Uniprot Annotation

Name:	Flavohemoprotein
ID:	HMP_CUPNH
AC:	P39662
Organism:	Cupriavidus necator
Reign:	Bacteria
TaxID:	381666
EC Number:	/

Chains:

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

Ligand binding site composition:

B-Factor:	27.103
Number of residues:	44
Including
Standard Amino Acids:	42
Non Standard Amino Acids:	1
Water Molecules:	1
Cofactors:
Metals:

Cavity properties

Ligandability	Volume (Å3)
0.877	624.375

% Hydrophobic	% Polar
38.92	61.08
According to VolSite

Ligand :

HET Code:	FAD
Formula:	C27H31N9O15P2
Molecular weight:	783.534 g/mol
DrugBank ID:	DB03147
Buried Surface Area:	63.32 %
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
20.6881	-9.6637	88.4306

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
O1A	ND2	ASN- 44	3.47	162.83	H-Bond (Protein Donor)	false
C7M	CD2	TYR- 190	3.49	0	Hydrophobic	false
O1A	NH1	ARG- 206	3.22	130.68	H-Bond (Protein Donor)	false
O1A	NE	ARG- 206	3.34	129.88	H-Bond (Protein Donor)	false
O5'	NE	ARG- 206	3.49	136.66	H-Bond (Protein Donor)	false
O1P	NE	ARG- 206	2.92	131.32	H-Bond (Protein Donor)	false
O1A	CZ	ARG- 206	3.66	0	Ionic (Protein Cationic)	false
O1P	CZ	ARG- 206	3.6	0	Ionic (Protein Cationic)	false
C3'	CD	ARG- 206	4	0	Hydrophobic	false
O2'	O	GLN- 207	2.67	176.26	H-Bond (Ligand Donor)	false
C7	CB	GLN- 207	3.82	0	Hydrophobic	false
C8	CB	GLN- 207	3.9	0	Hydrophobic	false
O4'	OH	TYR- 208	2.87	140.87	H-Bond (Protein Donor)	false
C2'	CE2	TYR- 208	3.84	0	Hydrophobic	false
O4	N	SER- 209	3.23	144.44	H-Bond (Protein Donor)	false
N5	N	SER- 209	3.25	141.59	H-Bond (Protein Donor)	false
N3	O	SER- 222	2.81	143.95	H-Bond (Ligand Donor)	false
O2	N	LYS- 224	2.9	171.96	H-Bond (Protein Donor)	false
C3B	CB	GLU- 226	4.4	0	Hydrophobic	false
C5'	CG	GLU- 226	3.81	0	Hydrophobic	false
O3B	OE1	GLU- 226	3.34	150.84	H-Bond (Ligand Donor)	false
O2A	N	TYR- 235	2.87	166.69	H-Bond (Protein Donor)	false
O1P	N	VAL- 236	2.9	142.27	H-Bond (Protein Donor)	false
O2P	OG	SER- 237	2.69	153.28	H-Bond (Protein Donor)	false
O2P	N	SER- 237	2.93	157.19	H-Bond (Protein Donor)	false
C7M	CG	GLU- 394	3.9	0	Hydrophobic	false
C6	CG1	VAL- 395	3.99	0	Hydrophobic	false
C8M	CG2	VAL- 395	4.25	0	Hydrophobic	false
C9A	CG1	VAL- 395	3.69	0	Hydrophobic	false
C7	CB	VAL- 395	3.79	0	Hydrophobic	false
O4	O	HOH- 1526	2.71	179.97	H-Bond (Protein Donor)	false