scPDB - 2pia entry

Protein Data Bank Entry:

PDB ID : 2pia

Resolution :2.000 Å

Experimental Method : X-ray

Deposition Date : 1993-02-15

Activity from ChEMBL: What is pChEMBL ?

	Min	Mean	Median	Standard Deviation	Max	Count
pChEMBL:

List of CHEMBLId :

Binding Site :

Uniprot Annotation

Name:	Phthalate dioxygenase reductase
ID:	PDR_BURCE
AC:	P33164
Organism:	Burkholderia cepacia
Reign:	Bacteria
TaxID:	292
EC Number:	/

Chains:

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

Ligand binding site composition:

B-Factor:	19.780
Number of residues:	45
Including
Standard Amino Acids:	39
Non Standard Amino Acids:	0
Water Molecules:	6
Cofactors:
Metals:

Cavity properties

Ligandability	Volume (Å3)
0.623	823.500

% Hydrophobic	% Polar
36.07	63.93
According to VolSite

Ligand :

HET Code:	FMN
Formula:	C17H19N4O9P
Molecular weight:	454.328 g/mol
DrugBank ID:	DB03247
Buried Surface Area:	76.92 %
Polar Surface area:	217.05 Å2

Number of
H-Bond Acceptors:	12
H-Bond Donors:	4
Rings:	3
Aromatic rings:	1
Anionic atoms:	2
Cationic atoms:	0
Rule of Five Violation:	1
Rotatable Bonds:	7

Mass center Coordinates

X	Y	Z
0.290194	33.6418	7.95532

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
C3'	CD	ARG- 55	4.08	0	Hydrophobic	false
O3P	CZ	ARG- 55	3.53	0	Ionic (Protein Cationic)	false
O3P	NH2	ARG- 55	3.24	139.24	H-Bond (Protein Donor)	false
O3P	NE	ARG- 55	2.93	157.5	H-Bond (Protein Donor)	false
C8	CG2	THR- 56	4.13	0	Hydrophobic	false
C9	CB	THR- 56	4.5	0	Hydrophobic	false
C7	CG2	THR- 56	3.8	0	Hydrophobic	false
O2'	N	THR- 56	3.4	129.47	H-Bond (Protein Donor)	false
O2'	O	THR- 56	2.75	168.78	H-Bond (Ligand Donor)	false
C2'	CE1	TYR- 57	3.78	0	Hydrophobic	false
O4	N	SER- 58	3.29	157.25	H-Bond (Protein Donor)	false
N5	N	SER- 58	3.34	135.04	H-Bond (Protein Donor)	false
N3	O	ALA- 72	2.86	152.66	H-Bond (Ligand Donor)	false
O2	N	LYS- 74	3	162.31	H-Bond (Protein Donor)	false
O1P	CZ	ARG- 80	3.86	0	Ionic (Protein Cationic)	false
O1P	N	ARG- 80	2.73	174.09	H-Bond (Protein Donor)	false
O1P	NE	ARG- 80	3	173.21	H-Bond (Protein Donor)	false
O3P	N	GLY- 82	2.78	129.22	H-Bond (Protein Donor)	false
O2P	N	SER- 83	3.24	157.9	H-Bond (Protein Donor)	false
O2P	OG	SER- 83	2.79	162.12	H-Bond (Protein Donor)	false
O3P	N	SER- 83	3.43	138.58	H-Bond (Protein Donor)	false
C7M	CG	GLU- 223	4.24	0	Hydrophobic	false
C7M	CD1	PHE- 225	4.44	0	Hydrophobic	false
C1'	CB	PHE- 225	4.26	0	Hydrophobic	false
C9	CB	PHE- 225	3.85	0	Hydrophobic	false
DuAr	DuAr	PHE- 225	3.92	0	Aromatic Face/Face	false
C8M	CB	CYS- 272	4.08	0	Hydrophobic	false
C8M	CB	SER- 274	4.03	0	Hydrophobic	false
O3'	OG	SER- 274	3.21	148.25	H-Bond (Protein Donor)	false
O2P	O	HOH- 327	2.62	171.24	H-Bond (Protein Donor)	false
O4	O	HOH- 329	2.61	161.12	H-Bond (Protein Donor)	false
O2'	O	HOH- 332	2.73	149.95	H-Bond (Protein Donor)	false