1HEG

The crystal structures at 2.2 angstroms resolution of hydroxyethylene-based inhibitors bound to human immunodeficiency virus type 1 protease show that the inhibitors are present in two distinct orientations

Functional Information from GO Data

Chain	GOid	namespace	contents
E	0004190	molecular_function	aspartic-type endopeptidase activity
E	0006508	biological_process	proteolysis

Functional Information from PDB Data

site_id	AC1
Number of Residues	19
Details	BINDING SITE FOR RESIDUE PSI E 201

Chain	Residue
E	ARG8
E	GLY48
E	GLY49
E	GLY49
E	ILE50
E	ILE50
E	PRO81
E	VAL82
E	ILE84
E	HOH130
E	HOH131
E	LEU23
E	ASP25
E	ASP25
E	GLY27
E	GLY27
E	ASP29
E	ASP29
E	GLY48

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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
E	ALA22-LEU33

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	69
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	10
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	1
Details	Active site: {"description":"For protease activity; shared with dimeric partner","evidences":[{"source":"PROSITE-ProRule","id":"PRU10094","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"12924029","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	Annotated By Reference To The Literature 1a30

Chain	Residue	Details
E	ASP25
E	THR26

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

Chain	Residue	Details
E	ASP25

---