scPDB - 4cry entry

Protein Data Bank Entry:

PDB ID : 4cry

Resolution :1.610 Å

Experimental Method : X-ray

Deposition Date : 2014-03-02

Activity from ChEMBL: What is pChEMBL ?

	Min	Mean	Median	Standard Deviation	Max	Count
pChEMBL:

List of CHEMBLId :

Binding Site :

Uniprot Annotation

Name:	PanD regulatory factor
ID:	PANM_ECOLI
AC:	P37613
Organism:	Escherichia coli
Reign:	Bacteria
TaxID:	83333
EC Number:	/

Chains:

Chain Name:	Percentage of Residues within binding site
B	97 %
G	3 %

Ligand binding site composition:

B-Factor:	28.836
Number of residues:	36
Including
Standard Amino Acids:	34
Non Standard Amino Acids:	1
Water Molecules:	1
Cofactors:
Metals:	MG

Cavity properties

Ligandability	Volume (Å3)
0.700	432.000

% Hydrophobic	% Polar
64.84	35.16
According to VolSite

Ligand :

HET Code:	ACO
Formula:	C23H34N7O17P3S
Molecular weight:	805.539 g/mol
DrugBank ID:	-
Buried Surface Area:	62.4 %
Polar Surface area:	429.68 Å2

Number of
H-Bond Acceptors:	22
H-Bond Donors:	5
Rings:	3
Aromatic rings:	2
Anionic atoms:	4
Cationic atoms:	0
Rule of Five Violation:	2
Rotatable Bonds:	20

Mass center Coordinates

X	Y	Z
30.8492	-18.2068	-13.3737

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
CH3	CG	GLU- 25	3.77	0	Hydrophobic	false
CH3	CZ	TYR- 26	3.8	0	Hydrophobic	false
CH3	CB	SER- 65	4.19	0	Hydrophobic	false
CDP	CD2	LEU- 66	3.98	0	Hydrophobic	false
N4P	O	LEU- 66	2.85	175.93	H-Bond (Ligand Donor)	false
CDP	CG2	VAL- 68	4.02	0	Hydrophobic	false
CAP	CB	VAL- 68	4.37	0	Hydrophobic	false
O9P	N	VAL- 68	2.75	176.85	H-Bond (Protein Donor)	false
CAP	CD	ARG- 73	3.9	0	Hydrophobic	false
O7A	NE	ARG- 74	2.8	161.36	H-Bond (Protein Donor)	false
O8A	NH2	ARG- 74	2.77	175.13	H-Bond (Protein Donor)	false
O4A	N	ARG- 74	2.86	177.37	H-Bond (Protein Donor)	false
O7A	CZ	ARG- 74	3.58	0	Ionic (Protein Cationic)	false
O8A	CZ	ARG- 74	3.64	0	Ionic (Protein Cationic)	false
DuAr	CZ	ARG- 74	3.85	167.53	Pi/Cation	false
O1A	N	GLY- 76	2.79	150.87	H-Bond (Protein Donor)	false
O5A	N	GLY- 78	2.84	158.8	H-Bond (Protein Donor)	false
C5B	CB	GLN- 79	4.02	0	Hydrophobic	false
O2A	N	GLN- 79	2.8	150.82	H-Bond (Protein Donor)	false
O7A	NH2	ARG- 102	2.84	147.78	H-Bond (Protein Donor)	false
O7A	CZ	ARG- 102	3.67	0	Ionic (Protein Cationic)	false
O5P	N	GLU- 103	2.83	160.48	H-Bond (Protein Donor)	false
CEP	CG1	VAL- 107	4.1	0	Hydrophobic	false
CEP	CE	MET- 108	3.93	0	Hydrophobic	false
C6P	CE	MET- 108	3.65	0	Hydrophobic	false
C1B	CB	PHE- 111	4.23	0	Hydrophobic	false
CCP	CD1	PHE- 111	3.63	0	Hydrophobic	false
CDP	CE2	PHE- 111	4.38	0	Hydrophobic	false
CEP	CG	PHE- 111	4.15	0	Hydrophobic	false
C5B	CD1	PHE- 111	3.88	0	Hydrophobic	false
C4B	CB	ALA- 114	4.17	0	Hydrophobic	false
O5A	MG	MG- 1129	2.65	0	Metal Acceptor	false
O5P	O	HOH- 2032	2.71	179.99	H-Bond (Protein Donor)	false