2WEC

ACID PROTEINASE (PENICILLOPEPSIN) (E.C.3.4.23.20) COMPLEX WITH PHOSPHONATE INHIBITOR: METHYL(2S)-[1-(((N-(1-NAPHTHALENEACETYL))-L-VALYL)AMINOMETHYL)HYDROXY PHOSPHINYLOXY]-3-PHENYLPROPANOATE, SODIUM SALT

Replaces: 1WEC

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004190	molecular_function	aspartic-type endopeptidase activity
A	0005576	cellular_component	extracellular region
A	0006508	biological_process	proteolysis
A	0008233	molecular_function	peptidase activity
A	0016787	molecular_function	hydrolase activity

Functional Information from PDB Data

Functional Information from PROSITE/UniProt

site_id	PS00141
Number of Residues	12
Details	ASP_PROTEASE Eukaryotic and viral aspartyl proteases active site. LNFDTGSADLWV

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	303
Details	Domain: {"description":"Peptidase A1","evidences":[{"source":"PROSITE-ProRule","id":"PRU01103","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	2
Details	Active site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01103","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"5475460","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	1
Details	Glycosylation: {"description":"O-linked (Man...) serine","evidences":[{"source":"PubMed","id":"9836576","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"journal article","publicationDate":"1998","firstPage":"4610","lastPage":"4621","volume":"120","journal":"J. Am. Chem. Soc.","title":"Macrocyclic inhibitors of penicillopepsin. II. X-Ray crystallographic analyses of penicillopepsin complexed with a P3-P1 macrocyclic peptidyl inhibitor and with its two acyclic analogues.","authors":["Ding J.","Fraser M.E.","Meyer J.H.","Bartlett P.A.","James M.N.G."],"citationCrossReferences":[{"database":"DOI","id":"10.1021/ja973714r"}]}}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	1
Details	Glycosylation: {"description":"O-linked (Man...) threonine","evidences":[{"source":"PubMed","id":"9836576","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"journal article","publicationDate":"1998","firstPage":"4610","lastPage":"4621","volume":"120","journal":"J. Am. Chem. Soc.","title":"Macrocyclic inhibitors of penicillopepsin. II. X-Ray crystallographic analyses of penicillopepsin complexed with a P3-P1 macrocyclic peptidyl inhibitor and with its two acyclic analogues.","authors":["Ding J.","Fraser M.E.","Meyer J.H.","Bartlett P.A.","James M.N.G."],"citationCrossReferences":[{"database":"DOI","id":"10.1021/ja973714r"}]}}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	CSA1
Number of Residues	1
Details	Annotated By Reference To The Literature 1am5

Chain	Residue	Details
A	ASP33

site_id	CSA2
Number of Residues	1
Details	Annotated By Reference To The Literature 1am5

Chain	Residue	Details
A	ASP213

site_id	CSA3
Number of Residues	4
Details	Annotated By Reference To The Literature 1am5

site_id	CSA4
Number of Residues	4
Details	Annotated By Reference To The Literature 1am5

site_id	CSA5
Number of Residues	3
Details	Annotated By Reference To The Literature 1am5

site_id	CSA6
Number of Residues	4
Details	Annotated By Reference To The Literature 1am5

site_id	CSA7
Number of Residues	4
Details	Annotated By Reference To The Literature 1am5