scPDB - 1pz1 entry

Protein Data Bank Entry:

PDB ID : 1pz1

Resolution :2.200 Å

Experimental Method : X-ray

Deposition Date : 2003-07-09

Activity from ChEMBL: What is pChEMBL ?

	Min	Mean	Median	Standard Deviation	Max	Count
pChEMBL:

List of CHEMBLId :

Binding Site :

Uniprot Annotation

Name:	General stress protein 69
ID:	GS69_BACSU
AC:	P80874
Organism:	Bacillus subtilis
Reign:	Bacteria
TaxID:	224308
EC Number:	/

Chains:

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

Ligand binding site composition:

B-Factor:	15.916
Number of residues:	45
Including
Standard Amino Acids:	45
Non Standard Amino Acids:	0
Water Molecules:	0
Cofactors:
Metals:

Cavity properties

Ligandability	Volume (Å3)
1.284	1275.750

% Hydrophobic	% Polar
55.29	44.71
According to VolSite

Ligand :

HET Code:	NAP
Formula:	C21H25N7O17P3
Molecular weight:	740.381 g/mol
DrugBank ID:	DB03461
Buried Surface Area:	68.69 %
Polar Surface area:	405.54 Å2

Number of
H-Bond Acceptors:	21
H-Bond Donors:	5
Rings:	5
Aromatic rings:	3
Anionic atoms:	4
Cationic atoms:	1
Rule of Five Violation:	2
Rotatable Bonds:	13

Mass center Coordinates

X	Y	Z
33.085	-8.42417	31.7831

Binding mode :

What is Poseview ?

2D View
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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
O3D	N	TRP- 21	3.16	164.49	H-Bond (Protein Donor)	false
C3D	CB	TRP- 21	3.94	0	Hydrophobic	false
C4B	CH2	TRP- 28	4.34	0	Hydrophobic	false
C3B	CZ3	TRP- 28	4.29	0	Hydrophobic	false
O2D	OD2	ASP- 52	3.07	163.32	H-Bond (Ligand Donor)	false
C2D	CZ	TYR- 57	4.28	0	Hydrophobic	false
N7N	OG	SER- 155	3.41	136.04	H-Bond (Ligand Donor)	false
O7N	ND2	ASN- 156	3.47	163.43	H-Bond (Protein Donor)	false
DuAr	DuAr	TYR- 203	3.96	0	Aromatic Face/Face	false
C3N	CB	TYR- 203	4.13	0	Hydrophobic	false
O5D	N	GLY- 204	3.19	125.07	H-Bond (Protein Donor)	false
O1A	N	LEU- 206	3.11	136.19	H-Bond (Protein Donor)	false
C5B	CD1	LEU- 206	3.97	0	Hydrophobic	false
O1A	N	ARG- 208	3.03	133.5	H-Bond (Protein Donor)	false
N3A	NZ	LYS- 214	3.24	156.42	H-Bond (Protein Donor)	false
O3X	NZ	LYS- 214	2.84	150.53	H-Bond (Protein Donor)	false
O1X	NZ	LYS- 214	3.52	0	Ionic (Protein Cationic)	false
O3X	NZ	LYS- 214	2.84	0	Ionic (Protein Cationic)	false
O2X	CZ	ARG- 227	3.88	0	Ionic (Protein Cationic)	false
O3X	CZ	ARG- 227	3.91	0	Ionic (Protein Cationic)	false
O2X	NH2	ARG- 227	3.05	160.81	H-Bond (Protein Donor)	false
O3X	NH1	ARG- 227	3.07	168.53	H-Bond (Protein Donor)	false
C4D	CB	LEU- 278	4.22	0	Hydrophobic	false
O2A	N	GLY- 280	3.23	162.64	H-Bond (Protein Donor)	false
C2B	CD	ARG- 282	4.39	0	Hydrophobic	false
O2X	NH1	ARG- 282	3	151.95	H-Bond (Protein Donor)	false
N6A	O	GLN- 286	3.18	142.75	H-Bond (Ligand Donor)	false
O1X	NE2	GLN- 286	3.12	151.3	H-Bond (Protein Donor)	false
C4N	SD	MET- 323	4.26	0	Hydrophobic	false