scPDB - 2cul entry

Protein Data Bank Entry:

PDB ID : 2cul

Resolution :1.650 Å

Experimental Method : X-ray

Deposition Date : 2005-05-26

Activity from ChEMBL: What is pChEMBL ?

	Min	Mean	Median	Standard Deviation	Max	Count
pChEMBL:

List of CHEMBLId :

Binding Site :

Uniprot Annotation

Name:	GidA-related protein
ID:	Q5SH33_THET8
AC:	Q5SH33
Organism:	Thermus thermophilus
Reign:	Bacteria
TaxID:	300852
EC Number:	/

Chains:

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

Ligand binding site composition:

B-Factor:	11.628
Number of residues:	62
Including
Standard Amino Acids:	58
Non Standard Amino Acids:	0
Water Molecules:	4
Cofactors:
Metals:

Cavity properties

Ligandability	Volume (Å3)
1.149	769.500

% Hydrophobic	% Polar
53.51	46.49
According to VolSite

Ligand :

HET Code:	FAD
Formula:	C27H31N9O15P2
Molecular weight:	783.534 g/mol
DrugBank ID:	DB03147
Buried Surface Area:	75.15 %
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
54.3755	33.3879	2.29226

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
O2A	N	PHE- 13	3.23	154.19	H-Bond (Protein Donor)	false
C4'	CD2	PHE- 13	4.09	0	Hydrophobic	false
O1P	OG	SER- 14	2.76	175.77	H-Bond (Protein Donor)	false
O1P	N	SER- 14	2.82	169.96	H-Bond (Protein Donor)	false
N3A	N	GLN- 34	3.06	143.19	H-Bond (Protein Donor)	false
C2B	CG	GLN- 34	4.23	0	Hydrophobic	false
C6	CB	PHE- 43	4.16	0	Hydrophobic	false
C7M	CE1	PHE- 43	3.63	0	Hydrophobic	false
C8M	CZ	PHE- 43	4.33	0	Hydrophobic	false
C3'	CE2	PHE- 43	3.91	0	Hydrophobic	false
DuAr	DuAr	PHE- 43	3.62	0	Aromatic Face/Face	false
O4	N	LEU- 44	3.37	147.2	H-Bond (Protein Donor)	false
N6A	O	ALA- 91	2.91	167.56	H-Bond (Ligand Donor)	false
N1A	N	ALA- 91	2.91	144.57	H-Bond (Protein Donor)	false
C8M	CB	SER- 123	3.92	0	Hydrophobic	false
C5B	CE2	PHE- 124	4.23	0	Hydrophobic	false
C2B	CE2	PHE- 124	3.8	0	Hydrophobic	false
O1A	NH2	ARG- 140	3.46	128.38	H-Bond (Protein Donor)	false
O1A	NH1	ARG- 140	2.98	143.84	H-Bond (Protein Donor)	false
O1A	CZ	ARG- 140	3.64	0	Ionic (Protein Cationic)	false
C6	CG2	VAL- 167	3.76	0	Hydrophobic	false
C7M	CG2	VAL- 167	4.28	0	Hydrophobic	false
C7M	CE1	TYR- 176	4.43	0	Hydrophobic	false
C7M	CB	VAL- 178	3.63	0	Hydrophobic	false
C8M	CB	VAL- 178	4.33	0	Hydrophobic	false
C8M	CE2	TYR- 180	3.77	0	Hydrophobic	false
C8M	CD2	LEU- 206	3.96	0	Hydrophobic	false
C9	CD2	LEU- 206	4.12	0	Hydrophobic	false
C5'	CB	LEU- 206	3.93	0	Hydrophobic	false
C2'	CD1	LEU- 206	4.24	0	Hydrophobic	false
O2P	N	LEU- 206	2.9	149.23	H-Bond (Protein Donor)	false
O2	N	TYR- 213	2.92	160.89	H-Bond (Protein Donor)	false
C3'	CE1	TYR- 213	4.49	0	Hydrophobic	false
C4'	CD1	TYR- 213	4.49	0	Hydrophobic	false
C2'	CG	MET- 216	4.16	0	Hydrophobic	false
C5'	CG	MET- 216	3.47	0	Hydrophobic	false
O2P	O	HOH- 302	2.63	152.88	H-Bond (Protein Donor)	false
O2B	O	HOH- 306	2.95	159.82	H-Bond (Ligand Donor)	false
O1P	O	HOH- 310	2.76	179.99	H-Bond (Protein Donor)	false