scPDB - 3cgd entry

Protein Data Bank Entry:

PDB ID : 3cgd

Resolution :2.250 Å

Experimental Method : X-ray

Deposition Date : 2008-03-05

Activity from ChEMBL: What is pChEMBL ?

	Min	Mean	Median	Standard Deviation	Max	Count
pChEMBL:

List of CHEMBLId :

Binding Site :

Uniprot Annotation

Name:	Coenzyme A disulfide reductase
ID:	Q81TK8_BACAN
AC:	Q81TK8
Organism:	Bacillus anthracis
Reign:	Bacteria
TaxID:	1392
EC Number:	/

Chains:

Chain Name:	Percentage of Residues within binding site
A	91 %
B	9 %

Ligand binding site composition:

B-Factor:	47.072
Number of residues:	64
Including
Standard Amino Acids:	55
Non Standard Amino Acids:	2
Water Molecules:	7
Cofactors:	COA NAD
Metals:

Cavity properties

Ligandability	Volume (Å3)
0.900	911.250

% Hydrophobic	% Polar
46.67	53.33
According to VolSite

Ligand :

HET Code:	FAD
Formula:	C27H31N9O15P2
Molecular weight:	783.534 g/mol
DrugBank ID:	DB03147
Buried Surface Area:	78.99 %
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
50.0438	48.2841	22.5022

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	OD2	ASP- 9	2.54	167.73	H-Bond (Protein Donor)	false
C5B	CB	ASP- 9	4.25	0	Hydrophobic	false
C4'	CB	ALA- 10	4.49	0	Hydrophobic	false
O1P	N	ALA- 11	2.74	165.8	H-Bond (Protein Donor)	false
O3B	OE1	GLU- 32	2.95	173.83	H-Bond (Ligand Donor)	false
O3B	OE2	GLU- 32	3.37	127.62	H-Bond (Ligand Donor)	false
O2B	OE1	GLU- 32	3.39	154.47	H-Bond (Ligand Donor)	false
O2B	OE2	GLU- 32	2.61	144.33	H-Bond (Ligand Donor)	false
N3A	N	LYS- 33	3.38	131	H-Bond (Protein Donor)	false
O1A	NE2	GLN- 41	3.26	146.55	H-Bond (Protein Donor)	false
O2'	OE1	GLN- 41	2.98	164.6	H-Bond (Ligand Donor)	false
C9	CB	GLN- 41	3.73	0	Hydrophobic	false
C7M	CD1	LEU- 44	4.4	0	Hydrophobic	false
C7M	CG	PRO- 45	3.92	0	Hydrophobic	false
N6A	O	VAL- 80	3.1	167.02	H-Bond (Ligand Donor)	false
N1A	N	VAL- 80	3.04	162.2	H-Bond (Protein Donor)	false
C7M	CD2	LEU- 132	3.95	0	Hydrophobic	false
C8M	CD	LYS- 133	3.88	0	Hydrophobic	false
C7M	CD1	ILE- 161	4.32	0	Hydrophobic	false
C8M	CD1	ILE- 161	3.9	0	Hydrophobic	false
O3'	OD1	ASP- 282	3.19	135.65	H-Bond (Ligand Donor)	false
O3'	OD2	ASP- 282	2.86	163.42	H-Bond (Ligand Donor)	false
C5'	CB	ASP- 282	4.37	0	Hydrophobic	false
O2P	N	ASP- 282	2.85	164.57	H-Bond (Protein Donor)	false
N1	N	GLY- 300	3.24	151.49	H-Bond (Protein Donor)	false
O2	N	GLY- 300	3.14	128.72	H-Bond (Protein Donor)	false
O2	N	THR- 301	3.47	144.47	H-Bond (Protein Donor)	false
C5'	CB	ALA- 303	3.58	0	Hydrophobic	false
N3	O	TYR- 425	2.93	152.27	H-Bond (Ligand Donor)	false
C2'	S1P	COA- 445	3.57	0	Hydrophobic	false
C7M	C5N	NAD- 818	4.4	0	Hydrophobic	false
O1P	O	HOH- 829	2.75	179.99	H-Bond (Protein Donor)	false
O2P	O	HOH- 844	2.66	179.96	H-Bond (Protein Donor)	false
O4	O	HOH- 873	3.2	179.99	H-Bond (Protein Donor)	false