scPDB - 1bxr entry

Protein Data Bank Entry:

PDB ID : 1bxr

Resolution :2.100 Å

Experimental Method : X-ray

Deposition Date : 1998-10-08

Activity from ChEMBL: What is pChEMBL ?

	Min	Mean	Median	Standard Deviation	Max	Count
pChEMBL:

List of CHEMBLId :

Binding Site :

Uniprot Annotation

Name:	Carbamoyl-phosphate synthase large chain
ID:	CARB_ECOLI
AC:	P00968
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:	38.987
Number of residues:	51
Including
Standard Amino Acids:	46
Non Standard Amino Acids:	3
Water Molecules:	2
Cofactors:
Metals:	MN K K

Cavity properties

Ligandability	Volume (Å3)
0.223	394.875

% Hydrophobic	% Polar
50.43	49.57
According to VolSite

Ligand :

HET Code:	ANP
Formula:	C10H13N6O12P3
Molecular weight:	502.164 g/mol
DrugBank ID:	-
Buried Surface Area:	82.14 %
Polar Surface area:	322.68 Å2

Number of
H-Bond Acceptors:	16
H-Bond Donors:	4
Rings:	3
Aromatic rings:	2
Anionic atoms:	4
Cationic atoms:	0
Rule of Five Violation:	2
Rotatable Bonds:	8

Mass center Coordinates

X	Y	Z
15.3547	33.3864	69.7818

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
O2B	CZ	ARG- 129	3.58	0	Ionic (Protein Cationic)	false
O1A	CZ	ARG- 129	3.88	0	Ionic (Protein Cationic)	false
O2B	NH2	ARG- 129	2.5	156.11	H-Bond (Protein Donor)	false
O1A	NH1	ARG- 129	3.2	126.57	H-Bond (Protein Donor)	false
O1A	NH1	ARG- 169	3.06	148.31	H-Bond (Protein Donor)	false
O1B	N	GLY- 176	2.59	148.7	H-Bond (Protein Donor)	false
N6	O	GLU- 208	3.19	132.62	H-Bond (Ligand Donor)	false
N1	N	LEU- 210	3.1	157.97	H-Bond (Protein Donor)	false
O3'	OE2	GLU- 215	2.56	162.35	H-Bond (Ligand Donor)	false
O2'	OE1	GLU- 215	2.65	163.48	H-Bond (Ligand Donor)	false
O2'	OE2	GLU- 215	3.39	121.22	H-Bond (Ligand Donor)	false
C2'	CE	MET- 240	4.02	0	Hydrophobic	false
O2'	N	GLY- 241	3.04	167.03	H-Bond (Protein Donor)	false
O1G	NE2	HIS- 243	3.35	131.21	H-Bond (Protein Donor)	false
C4'	CB	HIS- 243	4.46	0	Hydrophobic	false
O3'	N	THR- 244	3.23	141.38	H-Bond (Protein Donor)	false
O3G	NH2	ARG- 303	3.23	142.4	H-Bond (Protein Donor)	false
O1G	NH2	ARG- 306	2.84	170.97	H-Bond (Protein Donor)	false
O2G	NH1	ARG- 306	3.14	164.02	H-Bond (Protein Donor)	false
O1G	CZ	ARG- 306	3.71	0	Ionic (Protein Cationic)	false
O2G	CZ	ARG- 306	3.94	0	Ionic (Protein Cationic)	false
C4'	CB	THR- 376	4.06	0	Hydrophobic	false
C1'	CG2	THR- 376	3.58	0	Hydrophobic	false
O3G	MN	MN- 1074	2.41	0	Metal Acceptor	false
O2B	MN	MN- 1074	2.4	0	Metal Acceptor	false