6DJ5

HIV-1 protease with mutation L76V in complex with GRL-0519 (tris-tetrahydrofuran as P2 ligand)

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	binding site for residue NA A 101

Chain	Residue
A	ASP60
A	HOH201
A	HOH218
A	HOH231

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site_id	AC2
Number of Residues	3
Details	binding site for residue CL A 102

Chain	Residue
A	THR74
A	ASN88
B	ARG41

---

site_id	AC3
Number of Residues	7
Details	binding site for residue GOL A 103

Chain	Residue
A	HOH227
B	GLN61
B	GLN92
B	HOH1118
B	HOH1132
A	LYS45
A	MET46

---

site_id	AC4
Number of Residues	6
Details	binding site for residue GOL A 104

Chain	Residue
A	LYS14
A	ILE15
A	GLY16
A	GLY17
A	ILE63
A	LYS70

---

site_id	AC5
Number of Residues	31
Details	binding site for residue G52 B 201

Chain	Residue
A	ARG8
A	ASP25
A	GLY27
A	ALA28
A	ASP29
A	ASP30
A	GLY48
A	GLY49
A	ILE50
A	PRO81
A	VAL82
A	ILE84
A	HOH206
A	HOH245
B	LEU23
B	ASP25
B	GLY27
B	ALA28
B	ASP29
B	ASP30
B	VAL32
B	GLY48
B	GLY49
B	ILE50
B	PRO81
B	VAL82
B	ILE84
B	HOH1102
B	HOH1124
B	HOH1142
B	HOH1147

---

site_id	AC6
Number of Residues	4
Details	binding site for residue NA B 202

Chain	Residue
B	ASP60
B	GOL208
B	HOH1123
B	HOH1155

---

site_id	AC7
Number of Residues	2
Details	binding site for residue CL B 203

Chain	Residue
B	TRP6
B	PRO44

---

site_id	AC8
Number of Residues	4
Details	binding site for residue CL B 204

Chain	Residue
B	GLY73
B	THR74
B	ASN88
B	HOH1131

---

site_id	AC9
Number of Residues	1
Details	binding site for residue CL B 205

Chain	Residue
B	THR12

---

site_id	AD1
Number of Residues	2
Details	binding site for residue CL B 206

Chain	Residue
B	LYS7
B	ARG8

---

site_id	AD2
Number of Residues	6
Details	binding site for residue GOL B 207

Chain	Residue
A	TRP6
B	ASP29
B	ARG87
B	ASN88
B	HOH1122
B	HOH1133

---

site_id	AD3
Number of Residues	8
Details	binding site for residue GOL B 208

Chain	Residue
B	ARG41
B	LYS43
B	GLN58
B	TYR59
B	ASP60
B	NA202
B	HOH1101
B	HOH1123

---

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	ALA22-ILE33

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI2
Number of Residues	20
Details	Region: {"description":"Dimerization of protease","evidences":[{"source":"PubMed","id":"2162350","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	2
Details	Active site: {"description":"For protease activity; shared with dimeric partner","evidences":[{"source":"PROSITE-ProRule","id":"PRU10094","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"33542150","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

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Catalytic Information from CSA

site_id	MCSA1
Number of Residues	3
Details	M-CSA 175

Chain	Residue	Details
A	ASP25	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
A	THR26	electrostatic stabiliser, transition state stabiliser
A	GLY27	electrostatic stabiliser, hydrogen bond donor

---

site_id	MCSA2
Number of Residues	3
Details	M-CSA 175

Chain	Residue	Details
B	ASP25	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
B	THR26	electrostatic stabiliser, transition state stabiliser
B	GLY27	electrostatic stabiliser, hydrogen bond donor

---