1DW6

Structural and kinetic analysis of drug resistant mutants of HIV-1 protease

Functional Information from GO Data

Chain	GOid	namespace	contents
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	22
Details	BINDING SITE FOR RESIDUE 0Q4 D 401

Chain	Residue
C	ARG8
D	HOH26
D	ARG108
D	LEU123
D	ASP125
D	GLY127
D	ALA128
D	ASP129
D	ASP130
D	MET146
D	ILE147
C	ASP25
D	GLY148
D	GLY149
D	VAL182
C	GLY27
C	ALA28
C	ASP29
C	ASP30
C	GLY48
C	GLY49
C	ILE84

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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
C	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"},{"source":"PubMed","id":"12924029","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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Catalytic Information from CSA

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

Chain	Residue	Details
D	THR126
D	ASP125
C	ASP25
C	THR26

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site_id	CSA2
Number of Residues	2
Details	Annotated By Reference To The Literature 1a30

Chain	Residue	Details
C	ASP25
D	ASP125

---