1BBS

X-RAY ANALYSES OF PEPTIDE INHIBITOR COMPLEXES DEFINE THE STRUCTURAL BASIS OF SPECIFICITY FOR HUMAN AND MOUSE RENINS

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	CA1
Number of Residues	2
Details

Chain	Residue
B	ASP32
B	ASP215

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site_id	CAT
Number of Residues	2
Details

Chain	Residue
A	ASP32
A	ASP215

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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. VVFDTGSSNVWV

Chain	Residue	Details
A	VAL29-VAL40
A	ALA212-GLY223

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	ACT_SITE: ACT_SITE => ECO:0000269|PubMed:20927107

Chain	Residue	Details
A	ASP32
A	ASP215
B	ASP32
B	ASP215

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site_id	SWS_FT_FI2
Number of Residues	4
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:2493678

Chain	Residue	Details
A	ASN-2
A	ASN67
B	ASN-2
B	ASN67

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Catalytic Information from CSA

site_id	CSA1
Number of Residues	3
Details	a catalytic site defined by CSA, PubMed 1608447, 8816746, 11714911

Chain	Residue	Details
A	ASP215
A	SER35
A	ASP32

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site_id	CSA2
Number of Residues	3
Details	a catalytic site defined by CSA, PubMed 1608447, 8816746, 11714911

Chain	Residue	Details
B	ASP215
B	SER35
B	ASP32

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