scPDB - 3nxq entry

Protein Data Bank Entry:

PDB ID : 3nxq

Resolution :1.990 Å

Experimental Method : X-ray

Deposition Date : 2010-07-14

Activity from ChEMBL: What is pChEMBL ?

	Min	Mean	Median	Standard Deviation	Max	Count
pChEMBL:	5.130	6.640	6.640	1.520	8.160	2

List of CHEMBLId :

CHEMBL1235767

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:	24.965
Number of residues:	37
Including
Standard Amino Acids:	33
Non Standard Amino Acids:	1
Water Molecules:	3
Cofactors:
Metals:	ZN

Cavity properties

Ligandability	Volume (Å3)
0.431	1950.750

% Hydrophobic	% Polar
35.12	64.88
According to VolSite

Ligand :

HET Code:	RX4
Formula:	C21H29N4O8P
Molecular weight:	496.451 g/mol
DrugBank ID:	-
Buried Surface Area:	58.81 %
Polar Surface area:	220.45 Å2

Number of
H-Bond Acceptors:	8
H-Bond Donors:	4
Rings:	1
Aromatic rings:	1
Anionic atoms:	2
Cationic atoms:	0
Rule of Five Violation:	1
Rotatable Bonds:	13

Mass center Coordinates

X	Y	Z
-2.41747	-17.0134	-22.255

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
O	NE2	GLN- 259	3.04	168.95	H-Bond (Protein Donor)	false
OAH	NE2	HIS- 331	2.74	177.53	H-Bond (Protein Donor)	false
CAB	CB	ALA- 332	4.25	0	Hydrophobic	false
CAQ	CB	SER- 333	3.69	0	Hydrophobic	false
OAI	N	ALA- 334	2.82	170.59	H-Bond (Protein Donor)	false
NAU	O	ALA- 334	2.98	150.57	H-Bond (Ligand Donor)	false
CAB	CG2	THR- 358	4.18	0	Hydrophobic	false
O4	OE1	GLU- 362	2.75	145.74	H-Bond (Protein Donor)	false
CAR	CB	HIS- 365	4.4	0	Hydrophobic	false
OAG	OH	TYR- 369	2.54	168.34	H-Bond (Protein Donor)	false
OAK	CZ	ARG- 381	3.66	0	Ionic (Protein Cationic)	false
OAG	CZ	ARG- 381	3.69	0	Ionic (Protein Cationic)	false
OAK	NH2	ARG- 381	2.55	148.25	H-Bond (Protein Donor)	false
OAG	NH1	ARG- 381	3.19	152.86	H-Bond (Protein Donor)	false
OAG	NH2	ARG- 381	3.27	148.39	H-Bond (Protein Donor)	false
CB	CE1	PHE- 435	3.94	0	Hydrophobic	false
O	NZ	LYS- 489	2.95	165.66	H-Bond (Protein Donor)	false
OAH	NE2	HIS- 491	2.9	133.51	H-Bond (Protein Donor)	false
CAP	CG2	THR- 496	3.79	0	Hydrophobic	false
O	OH	TYR- 498	2.76	152.8	H-Bond (Protein Donor)	false
O3	OH	TYR- 501	2.58	169.38	H-Bond (Protein Donor)	false
CB	CD2	TYR- 501	3.63	0	Hydrophobic	false
O4	ZN	ZN- 650	2.42	0	Metal Acceptor	false
O3	ZN	ZN- 650	2.22	0	Metal Acceptor	false
NAW	O	HOH- 666	3.03	172.32	H-Bond (Ligand Donor)	false