2MIP

CRYSTAL STRUCTURE OF HUMAN IMMUNODEFICIENCY VIRUS (HIV) TYPE 2 PROTEASE IN COMPLEX WITH A REDUCED AMIDE INHIBITOR AND COMPARISON WITH HIV-1 PROTEASE STRUCTURES

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	29
Details	BINDING SITE FOR CHAIN E OF INHIBITOR BI-LA-398

Chain	Residue
A	ASP25
A	ILE50
A	PRO81
A	ILE82
A	ILE84
B	ARG8
B	ASP25
B	GLY27
B	ASP29
B	GLY48
B	GLY49
A	GLY27
B	ILE50
D	TYR14
E	HOH501
G	PHE1
G	VAL2
G	PHE3
G	LEU4
G	GLU5
G	ILE6
G	NH27
A	ALA28
A	ASP29
A	ASP30
A	ILE32
A	VAL47
A	GLY48
A	GLY49

---

site_id	AC2
Number of Residues	31
Details	BINDING SITE FOR CHAIN F OF INHIBITOR BI-LA-398

Chain	Residue
B	ASN40
B	ASN41
B	GLU65
C	LEU23
C	ASP25
C	GLY27
C	ALA28
C	ASP29
C	GLY48
C	GLY49
C	ILE50
C	ILE82
C	ILE84
D	ASP25
D	GLY27
D	ALA28
D	ASP29
D	ASP30
D	VAL47
D	GLY48
D	GLY49
D	PRO81
D	ILE82
F	HOH701
H	PHE1
H	VAL2
H	PHE3
H	LEU4
H	GLU5
H	ILE6
H	NH27

---

site_id	AC3
Number of Residues	28
Details	BINDING SITE FOR CHAIN G OF INHIBITOR BI-LA-398

Chain	Residue
A	ASP25
A	GLY27
A	ALA28
A	ASP29
A	ASP30
A	GLY48
A	GLY49
A	ILE50
A	PRO81
A	ILE84
B	ARG8
B	ASP25
B	GLY27
B	ALA28
B	ASP29
B	ASP30
B	VAL47
B	GLY48
B	ILE50
B	HOH505
E	PHE1
E	VAL2
E	PHE3
E	LEU4
E	GLU5
E	ILE6
E	NH27
E	HOH501

---

site_id	AC4
Number of Residues	32
Details	BINDING SITE FOR CHAIN H OF INHIBITOR BI-LA-398

Chain	Residue
C	GLY49
C	ILE50
C	ILE82
D	ASP25
D	GLY27
D	ALA28
D	ASP29
D	VAL47
D	GLY48
D	GLY49
D	ILE50
D	PRO81
D	ILE82
F	PHE1
F	VAL2
F	PHE3
F	LEU4
F	GLU5
F	ILE6
F	NH27
F	HOH701
B	TYR14
B	ASN40
B	ASN41
B	TYR42
C	ASP25
C	GLY27
C	ALA28
C	ASP29
C	ASP30
C	VAL47
C	GLY48

---

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	VAL22-VAL33

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	276
Details	Domain: {"description":"Peptidase A2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00275","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	40
Details	Region: {"description":"Dimerization of protease","evidences":[{"source":"UniProtKB","id":"P04585","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	4
Details	Active site: {"description":"For protease activity; shared with dimeric partner","evidences":[{"source":"PROSITE-ProRule","id":"PRU10094","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

Catalytic Information from CSA

site_id	CSA1
Number of Residues	4
Details	Annotated By Reference To The Literature 1a30

Chain	Residue	Details
A	ASP25
A	THR26
B	ASP25
B	THR26

---

site_id	CSA2
Number of Residues	4
Details	Annotated By Reference To The Literature 1a30

Chain	Residue	Details
D	ASP25
D	THR26
C	ASP25
C	THR26

---

site_id	CSA3
Number of Residues	2
Details	Annotated By Reference To The Literature 1a30

Chain	Residue	Details
A	ASP25
B	ASP25

---

site_id	CSA4
Number of Residues	2
Details	Annotated By Reference To The Literature 1a30

Chain	Residue	Details
C	ASP25
D	ASP25

---