1AM5

THE CRYSTAL STRUCTURE AND PROPOSED AMINO ACID SEQUENCE OF A PEPSIN FROM ATLANTIC COD (GADUS MORHUA)

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004190	molecular_function	aspartic-type endopeptidase activity
A	0006508	biological_process	proteolysis
A	0007586	biological_process	digestion

Functional Information from PDB Data

site_id	CAT
Number of Residues	2
Details	THE CATALYTIC ASPARTIC RESIDUES, ASP 32 AND ASP 215, ARE CONNECTED THROUGH A NETWORK OF HYDROGEN BONDS.

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. VIFDTGSSNLWV

Chain	Residue	Details
A	VAL29-VAL40
A	ALA212-ALA223

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10094

Chain	Residue	Details
A	ASP32
A	ASP215

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Catalytic Information from CSA

site_id	MCSA1
Number of Residues	7
Details	M-CSA 396

Chain	Residue	Details
A	ASP32	proton acceptor, proton donor
A	SER35	electrostatic stabiliser, modifies pKa
A	ASN37	electrostatic stabiliser, modifies pKa
A	TRP39	electrostatic stabiliser, modifies pKa
A	TYR75	electrostatic stabiliser, modifies pKa
A	ASP215	proton acceptor, proton donor
A	THR218	electrostatic stabiliser, modifies pKa

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