4OBF

Crystal Structure of Nelfinavir-Resistant, Inactive HIV-1 Protease Variant (D30N/N88D) in Complex with the p1-p6 substrate variant (S451N)

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	5
Details	BINDING SITE FOR RESIDUE GOL A 101

Chain	Residue
A	LYS7
A	ARG8
A	HOH232
B	ARG87
E	ARG9

---

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE EDO A 102

Chain	Residue
A	HOH241
A	ARG14
A	ILE15
A	GLY16
A	GLY17

---

site_id	AC3
Number of Residues	1
Details	BINDING SITE FOR RESIDUE EDO A 103

Chain	Residue
A	LYS70

---

site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE EDO A 104

Chain	Residue
A	LEU5
A	TRP6
A	HOH214
A	HOH236
B	ARG87
B	HOH226

---

site_id	AC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE PO4 A 105

Chain	Residue
A	GLU35
A	MET36
A	ASN37
A	HOH226
B	PRO39
B	GLY40

---

site_id	AC6
Number of Residues	2
Details	BINDING SITE FOR RESIDUE ACT A 106

Chain	Residue
A	PRO1
A	HOH223

---

site_id	AC7
Number of Residues	3
Details	BINDING SITE FOR RESIDUE GOL B 101

Chain	Residue
A	ARG87
B	LYS7
B	ARG8

---

site_id	AC8
Number of Residues	3
Details	BINDING SITE FOR RESIDUE EDO B 102

Chain	Residue
B	ARG14
B	GLY16
B	GLY17

---

site_id	AC9
Number of Residues	5
Details	BINDING SITE FOR RESIDUE GOL C 101

Chain	Residue
C	ARG87
C	HOH222
D	TRP6
D	LYS7
D	ARG8

---

site_id	BC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE EDO C 102

Chain	Residue
B	GLY52
B	PHE53
C	ILE72
C	GLN92

---

site_id	BC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE EDO C 103

Chain	Residue
C	LYS7
C	ARG8
D	ARG87
F	ARG9

---

site_id	BC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE EDO C 104

Chain	Residue
C	ASP29
C	ASN30
C	VAL32
C	ILE47
F	GLY3
F	ASN4

---

site_id	BC4
Number of Residues	8
Details	BINDING SITE FOR RESIDUE GOL D 101

Chain	Residue
C	GLY16
C	PRO63
D	ARG14
D	GLY16
D	GLY17
D	PRO63
D	HOH218
D	HOH243

---

site_id	BC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE EDO D 102

Chain	Residue
C	PRO39
C	GLY40
D	MET36
D	ASN37
D	HOH234

---

site_id	BC6
Number of Residues	7
Details	BINDING SITE FOR RESIDUE PO4 D 103

Chain	Residue
B	TRP42
B	LYS55
B	ARG57
B	HOH246
D	VAL11
D	THR12
D	CYS67

---

site_id	BC7
Number of Residues	3
Details	BINDING SITE FOR RESIDUE EDO E 101

Chain	Residue
A	ARG8
E	ASN8
E	ARG9

---

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

---

site_id	SWS_FT_FI4
Number of Residues	2
Details	Site: {"description":"Cleavage; by viral protease","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---