scPDB - 4mrt entry

Protein Data Bank Entry:

PDB ID : 4mrt

Resolution :2.000 Å

Experimental Method : X-ray

Deposition Date : 2013-09-17

Activity from ChEMBL: What is pChEMBL ?

	Min	Mean	Median	Standard Deviation	Max	Count
pChEMBL:

List of CHEMBLId :

Binding Site :

Uniprot Annotation

Name:	4'-phosphopantetheinyl transferase sfp
ID:	SFP_BACSU
AC:	P39135
Organism:	Bacillus subtilis
Reign:	Bacteria
TaxID:	224308
EC Number:	2.7.8

Chains:

Chain Name:	Percentage of Residues within binding site
C	20 %
A	80 %

Ligand binding site composition:

B-Factor:	21.907
Number of residues:	53
Including
Standard Amino Acids:	49
Non Standard Amino Acids:	2
Water Molecules:	2
Cofactors:
Metals:	MG MG

Cavity properties

Ligandability	Volume (Å3)
0.974	1117.125

% Hydrophobic	% Polar
43.81	56.19
According to VolSite

Ligand :

HET Code:	COA
Formula:	C21H32N7O16P3S
Molecular weight:	763.502 g/mol
DrugBank ID:	DB01992
Buried Surface Area:	64.8 %
Polar Surface area:	426.11 Å2

Number of
H-Bond Acceptors:	21
H-Bond Donors:	6
Rings:	3
Aromatic rings:	2
Anionic atoms:	4
Cationic atoms:	0
Rule of Five Violation:	3
Rotatable Bonds:	18

Mass center Coordinates

X	Y	Z
18.6764	-2.71335	17.6006

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
O8A	NZ	LYS- 31	3.48	0	Ionic (Protein Cationic)	false
O9A	NZ	LYS- 31	3.75	0	Ionic (Protein Cationic)	false
O7A	OG1	THR- 44	2.79	172.22	H-Bond (Protein Donor)	false
O5A	N	ALA- 45	2.87	155.36	H-Bond (Protein Donor)	false
CDP	CB	ALA- 45	4.19	0	Hydrophobic	false
CAP	CE1	PHE- 69	3.88	0	Hydrophobic	false
C6P	CG	PHE- 69	3.25	0	Hydrophobic	false
C2P	CB	ALA- 70	3.97	0	Hydrophobic	false
N6A	O	TYR- 73	2.94	142.96	H-Bond (Ligand Donor)	false
C2B	CG	PRO- 76	3.56	0	Hydrophobic	false
N3A	ND2	ASN- 87	3.02	156.79	H-Bond (Protein Donor)	false
O2A	OG	SER- 89	2.93	167.19	H-Bond (Protein Donor)	false
O7A	NE2	HIS- 90	2.72	174.41	H-Bond (Protein Donor)	false
O1A	N	HIS- 90	2.94	169.51	H-Bond (Protein Donor)	false
CDP	CG	GLU- 151	3.71	0	Hydrophobic	false
CDP	CD1	ILE- 154	4.32	0	Hydrophobic	false
O2A	NZ	LYS- 155	2.99	149.2	H-Bond (Protein Donor)	false
O2A	NZ	LYS- 155	2.99	0	Ionic (Protein Cationic)	false
CDP	CG	LYS- 155	4.41	0	Hydrophobic	false
CEP	CG	LYS- 155	3.71	0	Hydrophobic	false
CBP	CD	LYS- 155	4.09	0	Hydrophobic	false
N6A	O	GLY- 158	3.15	145.7	H-Bond (Ligand Donor)	false
CDP	CG	LEU- 161	4.26	0	Hydrophobic	false
O9P	N	LEU- 161	2.72	156.65	H-Bond (Protein Donor)	false
O5P	OG	SER- 162	2.72	161.23	H-Bond (Protein Donor)	false
O2A	MG	MG- 301	1.94	0	Metal Acceptor	false
O4A	MG	MG- 301	2.05	0	Metal Acceptor	false
O1A	MG	MG- 304	2.1	0	Metal Acceptor	false
O4A	O	HOH- 414	2.84	141.14	H-Bond (Protein Donor)	false