3PRK

INHIBITION OF PROTEINASE K BY METHOXYSUCCINYL-ALA-ALA-PRO-ALA-CHLOROMETHYL KETONE. AN X-RAY STUDY AT 2.2-ANGSTROMS RESOLUTION

Functional Information from GO Data

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE CA E 500

Chain	Residue
E	PRO175
E	VAL177
E	ASP200
E	HOH293
E	HOH294
E	HOH295
E	HOH296

---

site_id	AC2
Number of Residues	13
Details	BINDING SITE FOR CHAIN I OF METHOXYSUCCINYL-ALA-ALA-PRO-ALA-CHLOROMETHYL KETONE

Chain	Residue
E	GLY100
E	GLY102
E	TYR104
E	SER132
E	LEU133
E	GLY134
E	ASN161
E	THR223
E	SER224
I	HOH453
I	HOH455
E	HIS69
E	LEU96

---

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
E	VAL35-HIS46

---

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

Chain	Residue	Details
E	HIS69-SER79

---

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

Chain	Residue	Details
E	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
E	ASP39
E	HIS69
E	SER224

---

site_id	SWS_FT_FI2
Number of Residues	5
Details	BINDING:

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

---

Catalytic Information from CSA

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

Chain	Residue	Details
E	SER224
E	ASP39
E	HIS69

---