4AUC

Bovine chymosin in complex with Pepstatin A

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	6
Details	binding site for residue NA A 401

Chain	Residue
A	ASN314
A	ASN314
A	HOH672
A	HOH672
A	HOH676
A	HOH676

---

site_id	AC2
Number of Residues	6
Details	binding site for residue CD A 402

Chain	Residue
A	HOH507
A	HOH586
A	HOH604
A	ASP151
A	ASP249
A	ASP251

---

site_id	AC3
Number of Residues	3
Details	binding site for residue EDO A 403

Chain	Residue
A	ASP151
A	ALA313
A	HOH658

---

site_id	AC4
Number of Residues	5
Details	binding site for residue EDO A 404

Chain	Residue
A	GLN150
A	ASP247
A	ILE248
A	CYS283
A	HOH685

---

site_id	AC5
Number of Residues	3
Details	binding site for residue EDO A 405

Chain	Residue
A	TYR190
A	HOH697
B	STA6

---

site_id	AC6
Number of Residues	4
Details	binding site for residue EDO A 406

Chain	Residue
A	GLN212
A	GLU245
A	PHE282
A	HOH501

---

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

---

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

---

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

---