scPDB - 1q6y entry

Protein Data Bank Entry:

PDB ID : 1q6y

Resolution :1.990 Å

Experimental Method : X-ray

Deposition Date : 2003-08-14

Activity from ChEMBL: What is pChEMBL ?

	Min	Mean	Median	Standard Deviation	Max	Count
pChEMBL:

List of CHEMBLId :

Binding Site :

Uniprot Annotation

Name:	Formyl-CoA:oxalate CoA-transferase
ID:	FCTA_ECOLI
AC:	P69902
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:	31.279
Number of residues:	42
Including
Standard Amino Acids:	41
Non Standard Amino Acids:	0
Water Molecules:	1
Cofactors:
Metals:

Cavity properties

Ligandability	Volume (Å3)
0.532	357.750

% Hydrophobic	% Polar
52.83	47.17
According to VolSite

Ligand :

HET Code:	COA
Formula:	C21H32N7O16P3S
Molecular weight:	763.502 g/mol
DrugBank ID:	DB01992
Buried Surface Area:	61.19 %
Polar Surface area:	426.11 Å2

Number of
H-Bond Acceptors:	21
H-Bond Donors:	6
Rings:	3
Aromatic rings:	2
Anionic atoms:	4
Cationic atoms:	0
Rule of Five Violation:	3
Rotatable Bonds:	18

Mass center Coordinates

X	Y	Z
40.1125	-3.31094	22.2114

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
CDP	CG2	VAL- 18	4.26	0	Hydrophobic	false
S1P	CG1	VAL- 18	3.45	0	Hydrophobic	false
S1P	CB	GLN- 19	3.73	0	Hydrophobic	false
O5P	OG	SER- 20	2.75	137.35	H-Bond (Protein Donor)	false
C2P	CB	SER- 20	4	0	Hydrophobic	false
O1A	NH2	ARG- 40	3.08	140.18	H-Bond (Protein Donor)	false
N6A	O	LEU- 74	2.8	159.72	H-Bond (Ligand Donor)	false
N1A	N	THR- 76	3.17	151.36	H-Bond (Protein Donor)	false
O3B	NZ	LYS- 77	3.23	127.94	H-Bond (Protein Donor)	false
O8A	NZ	LYS- 77	2.71	161.18	H-Bond (Protein Donor)	false
O8A	NZ	LYS- 77	2.71	0	Ionic (Protein Cationic)	false
N8P	O	ASN- 98	2.87	146.47	H-Bond (Ligand Donor)	false
O5P	ND2	ASN- 98	3.12	136.32	H-Bond (Protein Donor)	false
O7A	NE2	HIS- 100	3.12	121.67	H-Bond (Protein Donor)	false
O9A	NE2	HIS- 100	3.14	169.79	H-Bond (Protein Donor)	false
O2A	N	HIS- 100	2.94	159.13	H-Bond (Protein Donor)	false
CAP	CB	HIS- 100	3.85	0	Hydrophobic	false
C2B	CB	ALA- 103	4.06	0	Hydrophobic	false
C1B	CE	MET- 107	4.21	0	Hydrophobic	false
C6P	CG2	ILE- 126	4.46	0	Hydrophobic	false
O5A	NZ	LYS- 139	3.29	0	Ionic (Protein Cationic)	false
CEP	CG	LYS- 139	3.46	0	Hydrophobic	false
O9P	N	ALA- 140	3.38	174.52	H-Bond (Protein Donor)	false
N4P	O	ALA- 140	2.93	161.13	H-Bond (Ligand Donor)	false
CEP	CE1	TYR- 141	3.84	0	Hydrophobic	false
CDP	CZ	TYR- 141	4.08	0	Hydrophobic	false
S1P	CB	ASP- 171	4.03	0	Hydrophobic	false
C6P	SD	MET- 202	3.61	0	Hydrophobic	false
C2P	CE	MET- 202	3.72	0	Hydrophobic	false
O9P	O	HOH- 1211	2.77	157.77	H-Bond (Protein Donor)	false