4JEC

Joint neutron and X-ray structure of per-deuterated HIV-1 protease in complex with clinical inhibitor amprenavir

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	2
Details	BINDING SITE FOR RESIDUE CL A 601

Chain	Residue
A	TRP6
A	LYS55

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site_id	AC2
Number of Residues	18
Details	BINDING SITE FOR RESIDUE 478 B 401

Chain	Residue
A	DOD767
B	ASP125
B	GLY127
B	ALA128
B	ASP130
B	VAL132
B	GLY148
B	GLY149
B	ILE150
B	VAL182
B	DOD517
A	ASP25
A	GLY27
A	ASP29
A	ASP30
A	GLY48
A	GLY49
A	ILE50

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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. ALLDTGADDTVI

Chain	Residue	Details
A	ALA22-ILE33

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	138
Details	Domain: {"description":"Peptidase A2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00275","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	20
Details	Region: {"description":"Dimerization of protease","evidences":[{"source":"UniProtKB","id":"P04585","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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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"}]}

Chain

Residue

Details

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