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THE THREE-DIMENSIONAL STRUCTURE OF RECOMBINANT BOVINE CHYMOSIN AT 2.3 ANGSTROMS RESOLUTION

Functional Information from GO Data

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	1
Details	ACTIVE SITE ASPARTATE1

Chain	Residue
A	ASP34

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site_id	AC2
Number of Residues	1
Details	ACTIVE SITE ASPARTATE2

Chain	Residue
A	ASP216

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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. VLFDTGSSDFWV

Chain	Residue	Details
A	VAL31-VAL42
A	ALA213-GLY224

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	304
Details	Domain: {"description":"Peptidase A1","evidences":[{"source":"PROSITE-ProRule","id":"PRU01103","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	2
Details	Active site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU10094","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"329280","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"4612029","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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