6K8M

High resolution crystal structure of proteinase K with thiourea

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	5
Details	binding site for residue TOU E 301

Chain	Residue
E	PRO175
E	SER197
E	VAL198
E	LEU199
E	ASP200

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site_id	AC2
Number of Residues	3
Details	binding site for residue TOU E 302

Chain	Residue
E	ASP184
E	ARG188
E	HOH543

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site_id	AC3
Number of Residues	4
Details	binding site for residue TOU E 303

Chain	Residue
E	GLY215
E	THR217
E	HOH421
E	HIS46

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site_id	AC4
Number of Residues	6
Details	binding site for residue SO4 E 304

Chain	Residue
E	PRO7
E	TRP8
E	ARG185
E	HOH452
E	HOH515
E	HOH539

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site_id	AC5
Number of Residues	3
Details	binding site for residue CL E 305

Chain	Residue
E	VAL56
E	LYS57
E	SER63

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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

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

Chain	Residue	Details
E	HIS69-SER79

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

Chain	Residue	Details
E	GLY222-GLY232

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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

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site_id	SWS_FT_FI2
Number of Residues	5
Details	BINDING:

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

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