scPDB - 4em3 entry

Protein Data Bank Entry:

PDB ID : 4em3

Resolution :1.980 Å

Experimental Method : X-ray

Deposition Date : 2012-04-11

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:	CDR_STAA3
AC:	Q2FIA5
Organism:	Staphylococcus aureus
Reign:	Bacteria
TaxID:	367830
EC Number:	/

Chains:

Chain Name:	Percentage of Residues within binding site
A	93 %
B	7 %

Ligand binding site composition:

B-Factor:	31.437
Number of residues:	60
Including
Standard Amino Acids:	54
Non Standard Amino Acids:	1
Water Molecules:	5
Cofactors:
Metals:

Cavity properties

Ligandability	Volume (Å3)
1.471	1120.500

% Hydrophobic	% Polar
55.12	44.88
According to VolSite

Ligand :

HET Code:	FAD
Formula:	C27H31N9O15P2
Molecular weight:	783.534 g/mol
DrugBank ID:	DB03147
Buried Surface Area:	75.63 %
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
11.6675	10.2079	33.7911

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
C4B	CG2	VAL- 10	4.18	0	Hydrophobic	false
O2A	N	ALA- 11	3.24	163.97	H-Bond (Protein Donor)	false
C4'	CB	ALA- 11	3.58	0	Hydrophobic	false
O1P	N	GLY- 12	2.94	160.72	H-Bond (Protein Donor)	false
O3B	OE1	GLU- 33	2.59	164.43	H-Bond (Ligand Donor)	false
O3B	OE2	GLU- 33	3.1	125.46	H-Bond (Ligand Donor)	false
O2B	OE2	GLU- 33	2.67	140.94	H-Bond (Ligand Donor)	false
O2B	NZ	LYS- 34	3.05	142.78	H-Bond (Protein Donor)	false
N3A	N	LYS- 34	3.13	134.31	H-Bond (Protein Donor)	false
C2B	CG	LYS- 34	4.37	0	Hydrophobic	false
O2A	ND2	ASN- 42	3.03	148.41	H-Bond (Protein Donor)	false
C8	CB	ASN- 42	3.96	0	Hydrophobic	false
C9A	SG	CYS- 43	3.99	0	Hydrophobic	false
C2'	SG	CYS- 43	4.4	0	Hydrophobic	false
C7M	CB	LEU- 45	4.4	0	Hydrophobic	false
C7M	CG	PRO- 46	4.18	0	Hydrophobic	false
N6A	O	VAL- 81	2.91	163.35	H-Bond (Ligand Donor)	false
N1A	N	VAL- 81	2.97	156.7	H-Bond (Protein Donor)	false
O1P	OG	SER- 112	2.64	127.83	H-Bond (Protein Donor)	false
C7M	CD2	LEU- 130	4.1	0	Hydrophobic	false
C8M	CD	ARG- 131	4.07	0	Hydrophobic	false
N1	OH	TYR- 158	3.48	125.68	H-Bond (Protein Donor)	false
C6	CG2	VAL- 159	4.13	0	Hydrophobic	false
C7M	CG1	VAL- 159	3.54	0	Hydrophobic	false
O3'	OD2	ASP- 277	3.49	136.12	H-Bond (Ligand Donor)	false
O3'	OD1	ASP- 277	2.94	167.31	H-Bond (Ligand Donor)	false
C5'	CB	ASP- 277	4.46	0	Hydrophobic	false
O2P	N	ASP- 277	2.88	159.51	H-Bond (Protein Donor)	false
N1	N	ALA- 295	3.49	136.36	H-Bond (Protein Donor)	false
O2	N	ALA- 295	2.93	167.86	H-Bond (Protein Donor)	false
C5'	CB	ALA- 298	4.11	0	Hydrophobic	false
N3	O	TYR- 419	2.93	166.18	H-Bond (Ligand Donor)	false
O1A	O	HOH- 727	2.9	143.84	H-Bond (Protein Donor)	false
O1P	O	HOH- 834	2.81	133.91	H-Bond (Protein Donor)	false
O2P	O	HOH- 835	2.63	179.96	H-Bond (Protein Donor)	false