3S85

Discovery of New HIV Protease Inhibitors with Potential for Convenient Dosing and Reduced Side Effects: A-790742 and A-792611.

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004190	molecular_function	aspartic-type endopeptidase activity
A	0006508	biological_process	proteolysis
B	0004190	molecular_function	aspartic-type endopeptidase activity
B	0006508	biological_process	proteolysis
C	0004190	molecular_function	aspartic-type endopeptidase activity
C	0006508	biological_process	proteolysis
D	0004190	molecular_function	aspartic-type endopeptidase activity
D	0006508	biological_process	proteolysis
E	0004190	molecular_function	aspartic-type endopeptidase activity
E	0006508	biological_process	proteolysis
F	0004190	molecular_function	aspartic-type endopeptidase activity
F	0006508	biological_process	proteolysis
G	0004190	molecular_function	aspartic-type endopeptidase activity
G	0006508	biological_process	proteolysis
H	0004190	molecular_function	aspartic-type endopeptidase activity
H	0006508	biological_process	proteolysis
I	0004190	molecular_function	aspartic-type endopeptidase activity
I	0006508	biological_process	proteolysis
J	0004190	molecular_function	aspartic-type endopeptidase activity
J	0006508	biological_process	proteolysis
K	0004190	molecular_function	aspartic-type endopeptidase activity
K	0006508	biological_process	proteolysis
L	0004190	molecular_function	aspartic-type endopeptidase activity
L	0006508	biological_process	proteolysis

Functional Information from PDB Data

site_id	AC1
Number of Residues	17
Details	BINDING SITE FOR RESIDUE LK0 B 1000

Chain	Residue
A	ARG8
B	ASP25
B	GLY27
B	ALA28
B	ASP29
B	GLY48
B	GLY49
B	PRO81
B	VAL82
A	ASP25
A	GLY27
A	ALA28
A	ASP29
A	GLY48
A	GLY49
A	ILE50
B	ARG8

---

site_id	AC2
Number of Residues	17
Details	BINDING SITE FOR RESIDUE LK0 E 1001

Chain	Residue
C	TRP6
E	ARG8
E	ASP25
E	GLY27
E	ALA28
E	ASP29
E	GLY48
E	GLY49
F	ARG8
F	ASP25
F	GLY27
F	ALA28
F	ASP29
F	ASP30
F	GLY48
F	GLY49
F	PRO81

---

site_id	AC3
Number of Residues	17
Details	BINDING SITE FOR RESIDUE LK0 C 1002

Chain	Residue
C	ARG8
C	ASP25
C	GLY27
C	ASP29
C	GLY48
C	GLY49
C	ILE50
C	PRO81
D	ARG8
D	ASP25
D	GLY27
D	ALA28
D	ASP29
D	GLY48
D	GLY49
D	PRO81
F	TRP6

---

site_id	AC4
Number of Residues	16
Details	BINDING SITE FOR RESIDUE LK0 H 1003

Chain	Residue
A	TRP6
G	ASP25
G	GLY27
G	ALA28
G	ASP29
G	GLY48
G	GLY49
G	PRO81
H	ARG8
H	ASP25
H	GLY27
H	ALA28
H	ASP29
H	GLY48
H	GLY49
H	PRO81

---

site_id	AC5
Number of Residues	17
Details	BINDING SITE FOR RESIDUE LK0 K 1004

Chain	Residue
G	GLU35
K	ASP25
K	GLY27
K	ASP29
K	GLY48
K	GLY49
K	PRO81
K	VAL82
L	ARG8
L	ASP25
L	GLY27
L	ASP29
L	ASP30
L	ILE47
L	GLY48
L	GLY49
L	PRO81

---

site_id	AC6
Number of Residues	17
Details	BINDING SITE FOR RESIDUE LK0 I 1005

Chain	Residue
J	GLY49
J	PRO81
A	GLU35
I	ASP25
I	GLY27
I	ALA28
I	ASP29
I	GLY48
I	GLY49
I	ILE50
I	PRO81
J	ARG8
J	ASP25
J	GLY27
J	ALA28
J	ASP29
J	GLY48

---

Functional Information from PROSITE/UniProt

site_id	PS00141
Number of Residues	12
Details	ASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. ALLDTGADDTVL

Chain	Residue	Details
A	ALA22-LEU33

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	12
Details	ACT_SITE: For protease activity; shared with dimeric partner => ECO:0000255|PROSITE-ProRule:PRU10094

Chain	Residue	Details
A	ASP25
J	ASP25
K	ASP25
L	ASP25
B	ASP25
C	ASP25
D	ASP25
E	ASP25
F	ASP25
G	ASP25
H	ASP25
I	ASP25

---

site_id	SWS_FT_FI2
Number of Residues	12
Details	SITE: Cleavage; by viral protease => ECO:0000250

Chain	Residue	Details
A	PHE99
J	PHE99
K	PHE99
L	PHE99
B	PHE99
C	PHE99
D	PHE99
E	PHE99
F	PHE99
G	PHE99
H	PHE99
I	PHE99

---