scPDB - 1a2n entry

Protein Data Bank Entry:

PDB ID : 1a2n

Resolution :2.800 Å

Experimental Method : X-ray

Deposition Date : 1998-01-06

Activity from ChEMBL: What is pChEMBL ?

	Min	Mean	Median	Standard Deviation	Max	Count
pChEMBL:

List of CHEMBLId :

Binding Site :

Uniprot Annotation

Name:	UDP-N-acetylglucosamine 1-carboxyvinyltransferase
ID:	MURA_ECOLI
AC:	P0A749
Organism:	Escherichia coli
Reign:	Bacteria
TaxID:	83333
EC Number:	/

Chains:

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

Ligand binding site composition:

B-Factor:	16.640
Number of residues:	52
Including
Standard Amino Acids:	45
Non Standard Amino Acids:	0
Water Molecules:	7
Cofactors:
Metals:

Cavity properties

Ligandability	Volume (Å3)
0.638	1134.000

% Hydrophobic	% Polar
36.61	63.39
According to VolSite

Ligand :

HET Code:	TET
Formula:	C20H26FN3O23P3
Molecular weight:	788.346 g/mol
DrugBank ID:	-
Buried Surface Area:	68.68 %
Polar Surface area:	437.05 Å2

Number of
H-Bond Acceptors:	23
H-Bond Donors:	6
Rings:	3
Aromatic rings:	0
Anionic atoms:	5
Cationic atoms:	0
Rule of Five Violation:	3
Rotatable Bonds:	16

Mass center Coordinates

X	Y	Z
43.6644	21.6316	41.1837

Binding mode :

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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
O13	NZ	LYS- 22	2.86	123.8	H-Bond (Protein Donor)	false
O15	NZ	LYS- 22	2.9	160.34	H-Bond (Protein Donor)	false
O18	NZ	LYS- 22	3.26	156.09	H-Bond (Protein Donor)	false
O15	NZ	LYS- 22	2.9	0	Ionic (Protein Cationic)	false
O18	NZ	LYS- 22	3.26	0	Ionic (Protein Cationic)	false
O21	ND2	ASN- 23	2.94	134.31	H-Bond (Protein Donor)	false
C8	CB	ASN- 23	4.49	0	Hydrophobic	false
C8	CD1	LEU- 26	4.06	0	Hydrophobic	false
O9	CZ	ARG- 91	3.86	0	Ionic (Protein Cationic)	false
O10	CZ	ARG- 91	3.53	0	Ionic (Protein Cationic)	false
C8	CH2	TRP- 95	3.87	0	Hydrophobic	false
F1	CD1	ILE- 117	3.73	0	Hydrophobic	false
O10	CZ	ARG- 120	3.83	0	Ionic (Protein Cationic)	false
O16	CZ	ARG- 120	3.78	0	Ionic (Protein Cationic)	false
O16	NH2	ARG- 120	2.74	153.16	H-Bond (Protein Donor)	false
N1	OD1	ASP- 123	2.99	164.09	H-Bond (Ligand Donor)	false
O1	N	LEU- 124	2.72	155.42	H-Bond (Protein Donor)	false
O6	OG	SER- 162	2.82	153.4	H-Bond (Protein Donor)	false
O5	N	VAL- 163	2.82	148.55	H-Bond (Protein Donor)	false
C10	CG1	VAL- 163	4.05	0	Hydrophobic	false
O6	N	GLY- 164	3.37	142.63	H-Bond (Protein Donor)	false
O9	N	GLY- 164	2.91	127.26	H-Bond (Protein Donor)	false
C17	CG2	THR- 304	4.11	0	Hydrophobic	false
O22	OD1	ASP- 305	2.65	173.55	H-Bond (Ligand Donor)	false
C12	CG1	VAL- 327	4.35	0	Hydrophobic	false
C17	CG1	VAL- 327	4.29	0	Hydrophobic	false
O14	O	VAL- 327	2.82	159.08	H-Bond (Ligand Donor)	false
C20	CE2	PHE- 328	4.23	0	Hydrophobic	false
C16	CZ	PHE- 328	3.99	0	Hydrophobic	false
C17	CE2	PHE- 328	3.82	0	Hydrophobic	false
F1	CZ	PHE- 328	3.82	0	Hydrophobic	false
C15	CE1	PHE- 328	3.97	0	Hydrophobic	false
O19	NH2	ARG- 331	2.84	120.34	H-Bond (Protein Donor)	false
O18	CZ	ARG- 371	3.1	0	Ionic (Protein Cationic)	false
O19	NE	ARG- 371	3.04	128.41	H-Bond (Protein Donor)	false
O15	NH2	ARG- 397	2.93	140.51	H-Bond (Protein Donor)	false
O15	CZ	ARG- 397	3.63	0	Ionic (Protein Cationic)	false
O24	O	HOH- 511	2.86	152.74	H-Bond (Ligand Donor)	false
O11	O	HOH- 518	2.96	164.95	H-Bond (Ligand Donor)	false