3LFY

CTD of Tarocystatin in complex with papain

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0006508	biological_process	proteolysis
A	0008234	molecular_function	cysteine-type peptidase activity
C	0006508	biological_process	proteolysis
C	0008234	molecular_function	cysteine-type peptidase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	2
Details	BINDING SITE FOR RESIDUE SER A 213

Chain	Residue
A	TRP177
A	ASN214

---

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ASN A 214

Chain	Residue
A	GLN142
A	TRP177
A	SER213
A	HOH296

---

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE SER C 213

Chain	Residue
C	HIS159
C	TRP177
C	GLY214
C	GLN19
C	OCS25
C	ASP158

---

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE GLY C 214

Chain	Residue
C	GLY20
C	TRP177
C	SER213
C	ASN215

---

site_id	AC5
Number of Residues	3
Details	BINDING SITE FOR RESIDUE ASN C 215

Chain	Residue
C	GLN142
C	TRP177
C	GLY214

---

Functional Information from PROSITE/UniProt

site_id	PS00139
Number of Residues	12
Details	THIOL_PROTEASE_CYS Eukaryotic thiol (cysteine) proteases cysteine active site. QGsCGSCWAfSA

Chain	Residue	Details
A	GLN19-ALA30

---

site_id	PS00639
Number of Residues	11
Details	THIOL_PROTEASE_HIS Eukaryotic thiol (cysteine) proteases histidine active site. VDHAVAAVGYG

Chain	Residue	Details
A	VAL157-GLY167

---

site_id	PS00640
Number of Residues	20
Details	THIOL_PROTEASE_ASN Eukaryotic thiol (cysteine) proteases asparagine active site. YILiKNSWgtgWGenGYIrI

Chain	Residue	Details
A	TYR170-ILE189

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	Active site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU10088","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"5681232","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"6502713","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"952885","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"1860874","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"1PAD","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"9PAP","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	2
Details	Active site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU10089","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"6502713","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"952885","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1PAD","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"9PAP","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	2
Details	Active site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU10090","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"5681232","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"6502713","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"952885","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1PAD","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"9PAP","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	2
Details	Binding site: {"description":"covalent","evidences":[{"source":"PubMed","id":"8416808","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1POP","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

Catalytic Information from CSA

site_id	MCSA1
Number of Residues	4
Details	M-CSA 174

Chain	Residue	Details
A	GLN19	electrostatic stabiliser, hydrogen bond donor
A	ALA27	electrostatic stabiliser
A	ALA163	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
A	THR179	activator, electrostatic stabiliser, hydrogen bond acceptor

---

site_id	MCSA2
Number of Residues	4
Details	M-CSA 174

Chain

Residue

Details

---