scPDB - 3r95 entry

Protein Data Bank Entry:

PDB ID : 3r95

Resolution :1.600 Å

Experimental Method : X-ray

Deposition Date : 2011-03-24

Activity from ChEMBL: What is pChEMBL ?

	Min	Mean	Median	Standard Deviation	Max	Count
pChEMBL:

List of CHEMBLId :

Binding Site :

Uniprot Annotation

Name:	MccE protein
ID:	Q47510_ECOLX
AC:	Q47510
Organism:	Escherichia coli
Reign:	Bacteria
TaxID:	562
EC Number:	/

Chains:

Chain Name:	Percentage of Residues within binding site
A	14 %
B	86 %

Ligand binding site composition:

B-Factor:	14.964
Number of residues:	45
Including
Standard Amino Acids:	41
Non Standard Amino Acids:	1
Water Molecules:	3
Cofactors:	ACO
Metals:

Cavity properties

Ligandability	Volume (Å3)
1.100	1461.375

% Hydrophobic	% Polar
42.26	57.74
According to VolSite

Ligand :

HET Code:	ACO
Formula:	C23H34N7O17P3S
Molecular weight:	805.539 g/mol
DrugBank ID:	-
Buried Surface Area:	62.03 %
Polar Surface area:	429.68 Å2

Number of
H-Bond Acceptors:	22
H-Bond Donors:	5
Rings:	3
Aromatic rings:	2
Anionic atoms:	4
Cationic atoms:	0
Rule of Five Violation:	2
Rotatable Bonds:	20

Mass center Coordinates

X	Y	Z
42.9031	7.8028	-14.1147

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
C6P	CB	SER- 45	4.31	0	Hydrophobic	false
C6P	CE	MET- 46	3.64	0	Hydrophobic	false
C2P	CG	MET- 46	4.42	0	Hydrophobic	false
CDP	CE1	TYR- 105	3.8	0	Hydrophobic	false
CH3	CZ	TYR- 105	3.72	0	Hydrophobic	false
CEP	CD1	TYR- 105	3.73	0	Hydrophobic	false
N4P	O	TYR- 105	2.99	137.22	H-Bond (Ligand Donor)	false
O	N	TYR- 105	3.15	152.21	H-Bond (Protein Donor)	false
C6P	CB	TRP- 106	4.05	0	Hydrophobic	false
CEP	CG	LEU- 107	4.2	0	Hydrophobic	false
O9P	N	LEU- 107	2.83	163.49	H-Bond (Protein Donor)	false
CAP	CG	GLN- 112	4	0	Hydrophobic	false
OAP	OE1	GLN- 112	3.09	125.45	H-Bond (Ligand Donor)	false
O4A	N	GLY- 113	2.82	155.7	H-Bond (Protein Donor)	false
O4B	N	GLY- 115	3.04	121.4	H-Bond (Protein Donor)	false
O5B	N	GLY- 115	3.29	125.92	H-Bond (Protein Donor)	false
CEP	CG2	VAL- 117	3.97	0	Hydrophobic	false
O1A	OG1	THR- 118	2.85	145.25	H-Bond (Protein Donor)	false
O2A	N	THR- 118	2.8	172.19	H-Bond (Protein Donor)	false
O2A	OG1	THR- 118	3.47	142.47	H-Bond (Protein Donor)	false
CH3	CG2	ILE- 139	3.65	0	Hydrophobic	false
S1P	CB	CYS- 141	3.91	0	Hydrophobic	false
O5P	ND2	ASN- 145	2.9	170.09	H-Bond (Protein Donor)	false
O8A	NZ	LYS- 147	3.81	0	Ionic (Protein Cationic)	false
CCP	CB	LYS- 147	4.3	0	Hydrophobic	false
CDP	CB	LYS- 147	4.27	0	Hydrophobic	false
CDP	CB	SER- 148	4.31	0	Hydrophobic	false
S1P	CB	SER- 148	4	0	Hydrophobic	false
O1A	OG1	THR- 151	2.92	167.97	H-Bond (Protein Donor)	false
C5B	CD	ARG- 154	3.82	0	Hydrophobic	false
O1A	NH1	ARG- 154	2.86	132.7	H-Bond (Protein Donor)	false
O1A	CZ	ARG- 154	3.85	0	Ionic (Protein Cationic)	false
O4A	O	HOH- 185	2.74	179.97	H-Bond (Protein Donor)	false
O5A	O	HOH- 190	2.67	139.82	H-Bond (Protein Donor)	false