scPDB - 2oc2 entry

Protein Data Bank Entry:

PDB ID : 2oc2

Resolution :2.250 Å

Experimental Method : X-ray

Deposition Date : 2006-12-20

Activity from ChEMBL: What is pChEMBL ?

	Min	Mean	Median	Standard Deviation	Max	Count
pChEMBL:	5.600	7.060	7.060	1.460	8.520	2

List of CHEMBLId :

CHEMBL571716

Binding Site :

Uniprot Annotation

Name:	Angiotensin-converting enzyme
ID:	ACE_HUMAN
AC:	P12821
Organism:	Homo sapiens
Reign:	Eukaryota
TaxID:	9606
EC Number:	3.2.1

Chains:

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

Ligand binding site composition:

B-Factor:	16.719
Number of residues:	44
Including
Standard Amino Acids:	43
Non Standard Amino Acids:	1
Water Molecules:	0
Cofactors:
Metals:	ZN

Cavity properties

Ligandability	Volume (Å3)
0.260	2413.125

% Hydrophobic	% Polar
40.84	59.16
According to VolSite

Ligand :

HET Code:	RX3
Formula:	C33H34N3O7P
Molecular weight:	615.613 g/mol
DrugBank ID:	-
Buried Surface Area:	56.65 %
Polar Surface area:	173.29 Å2

Number of
H-Bond Acceptors:	7
H-Bond Donors:	3
Rings:	5
Aromatic rings:	4
Anionic atoms:	2
Cationic atoms:	0
Rule of Five Violation:	1
Rotatable Bonds:	13

Mass center Coordinates

X	Y	Z
41.7382	36.2003	46.8451

Binding mode :

What is Poseview ?

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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
O6	NE2	GLN- 281	3.31	133.12	H-Bond (Protein Donor)	false
O5	NE2	HIS- 353	2.86	156.27	H-Bond (Protein Donor)	false
C22	CB	ALA- 354	3.64	0	Hydrophobic	false
C11	CB	SER- 355	4.17	0	Hydrophobic	false
C13	CB	SER- 355	3.57	0	Hydrophobic	false
O2	N	ALA- 356	2.7	151.56	H-Bond (Protein Donor)	false
C2	CB	ALA- 356	4.33	0	Hydrophobic	false
C33	CG1	VAL- 379	4.36	0	Hydrophobic	false
C21	CG1	VAL- 380	4.01	0	Hydrophobic	false
C32	CB	HIS- 383	4.21	0	Hydrophobic	false
O4	OE2	GLU- 384	2.64	155.7	H-Bond (Protein Donor)	false
C2	CB	HIS- 387	4.16	0	Hydrophobic	false
C2	CZ	PHE- 391	4.07	0	Hydrophobic	false
C5	CZ	PHE- 391	3.35	0	Hydrophobic	false
C6	CB	HIS- 410	4.27	0	Hydrophobic	false
C25	CZ	PHE- 457	3.45	0	Hydrophobic	false
O6	NZ	LYS- 511	2.58	172.5	H-Bond (Protein Donor)	false
O6	NZ	LYS- 511	2.58	0	Ionic (Protein Cationic)	false
C10	CE2	PHE- 512	4.35	0	Hydrophobic	false
O5	NE2	HIS- 513	2.91	128.91	H-Bond (Protein Donor)	false
C14	CG2	VAL- 518	3.23	0	Hydrophobic	false
O6	OH	TYR- 520	2.63	159.85	H-Bond (Protein Donor)	false
C25	CZ	TYR- 520	4.2	0	Hydrophobic	false
O3	OH	TYR- 523	2.65	162.62	H-Bond (Protein Donor)	false
C18	CE2	TYR- 523	4.16	0	Hydrophobic	false
C25	CD2	TYR- 523	3.69	0	Hydrophobic	false
O3	ZN	ZN- 701	1.97	0	Metal Acceptor	false
O4	ZN	ZN- 701	2.46	0	Metal Acceptor	false