1PEK

STRUCTURE OF THE COMPLEX OF PROTEINASE K WITH A SUBSTRATE-ANALOGUE HEXA-PEPTIDE INHIBITOR 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	13
Details	BINDING SITE FOR CHAIN C OF PEPTIDE PRO-ALA-PRO-PHE

Chain	Residue
E	LEU133
E	GLY134
E	GLY135
E	ALA158
E	GLY160
E	ASN161
E	SER224
C	HOH515
D	DAL5
E	HIS69
E	LEU96
E	GLY100
E	SER132

---

site_id	AC2
Number of Residues	10
Details	BINDING SITE FOR CHAIN D OF D-DAL-ALA-NH2

Chain	Residue
C	PRO3
C	PHE4
D	HOH483
E	HIS69
E	ASN161
E	ILE220
E	SER221
E	GLY222
E	THR223
E	SER224

---

site_id	ACT
Number of Residues	3
Details

Chain	Residue
E	ASP39
E	HIS69
E	SER224

---

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

---