1PJ8

Structure of a ternary complex of proteinase K, mercury and a substrate-analogue hexapeptide at 2.2 A resolution

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004252	molecular_function	serine-type endopeptidase activity
A	0006508	biological_process	proteolysis
A	0008236	molecular_function	serine-type peptidase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE HG A 600

Chain	Residue
A	ASP39
A	HIS69
A	CYS73

---

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE HG A 601

Chain	Residue
A	HIS72
A	CYS73
A	MET225
A	HOH324

---

site_id	AC3
Number of Residues	20
Details	BINDING SITE FOR CHAIN I OF 6-RESIDUE PEPTIDE (N-AC-PAPFPA-NH2)

Chain	Residue
A	ASN99
A	GLY100
A	LEU133
A	SER139
A	ALA158
A	GLY160
A	ASN161
A	SER207
A	SER219
A	ILE220
A	SER221
A	GLY222
A	THR223
A	SER224
A	MET225
A	HOH376
I	HOH483
I	HOH486
A	ASN67
A	HIS69

---

Functional Information from PROSITE/UniProt

site_id	PS00136
Number of Residues	12
Details	SUBTILASE_ASP Serine proteases, subtilase family, aspartic acid active site. VYVIDTGIeasH

Chain	Residue	Details
A	VAL35-HIS46

---

site_id	PS00137
Number of Residues	11
Details	SUBTILASE_HIS Serine proteases, subtilase family, histidine active site. HGThCAGtVGS

Chain	Residue	Details
A	HIS69-SER79

---

site_id	PS00138
Number of Residues	11
Details	SUBTILASE_SER Serine proteases, subtilase family, serine active site. GTSmAtPhVAG

Chain	Residue	Details
A	GLY222-GLY232

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	3
Details	ACT_SITE: Charge relay system => ECO:0000255|PROSITE-ProRule:PRU01240

Chain	Residue	Details
A	ASP39
A	HIS69
A	SER224

---

site_id	SWS_FT_FI2
Number of Residues	5
Details	BINDING:

Chain	Residue	Details
A	THR16
A	PRO175
A	VAL177
A	ASP200
A	ASP260

---

Catalytic Information from CSA

site_id	CSA1
Number of Residues	3
Details	Annotated By Reference To The Literature 1sca

Chain	Residue	Details
A	SER224
A	ASP39
A	HIS69

---