scPDB - 1c23 entry

Protein Data Bank Entry:

PDB ID : 1c23

Resolution :2.000 Å

Experimental Method : X-ray

Deposition Date : 1999-07-22

Activity from ChEMBL: What is pChEMBL ?

	Min	Mean	Median	Standard Deviation	Max	Count
pChEMBL:

List of CHEMBLId :

Binding Site :

Uniprot Annotation

Name:	Methionine aminopeptidase
ID:	MAP1_ECOLI
AC:	P0AE18
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:	16.317
Number of residues:	23
Including
Standard Amino Acids:	23
Non Standard Amino Acids:	0
Water Molecules:	0
Cofactors:
Metals:

Cavity properties

Ligandability	Volume (Å3)
0.591	357.750

% Hydrophobic	% Polar
48.11	51.89
According to VolSite

Ligand :

HET Code:	MPH
Formula:	C4H11NO3PS
Molecular weight:	184.174 g/mol
DrugBank ID:	DB02151
Buried Surface Area:	75.07 %
Polar Surface area:	125.94 Å2

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

Mass center Coordinates

X	Y	Z
21.54	-13.8904	8.4722

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
CE	SG	CYS- 59	4.35	0	Hydrophobic	false
CG	SG	CYS- 59	3.92	0	Hydrophobic	false
SD	CD2	TYR- 62	4	0	Hydrophobic	false
CE	CD1	TYR- 65	3.5	0	Hydrophobic	false
CG	SG	CYS- 70	3.78	0	Hydrophobic	false
CE	SG	CYS- 70	3.8	0	Hydrophobic	false
O3	NE2	HIS- 79	3	159.67	H-Bond (Protein Donor)	false
SD	CE2	PHE- 177	3.92	0	Hydrophobic	false
CB	CZ	PHE- 177	3.5	0	Hydrophobic	false
CE	CZ3	TRP- 221	3.72	0	Hydrophobic	false