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1PTK

STUDIES ON THE INHIBITORY ACTION OF MERCURY UPON PROTEINASE K

Functional Information from GO Data
ChainGOidnamespacecontents
A0004252molecular_functionserine-type endopeptidase activity
A0006508biological_processproteolysis
A0008236molecular_functionserine-type peptidase activity
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE HG A 280
ChainResidue
ACYS73
AASP39
AHIS69

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 281
ChainResidue
APRO175
AVAL177
AASP200
AHOH284
AHOH321
AHOH374

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE HG A 282
ChainResidue
AHIS72
ACYS73
ATHR76
AMET225

site_idACT
Number of Residues3
DetailsACTIVE SITE
ChainResidue
AASP39
AHIS69
ASER224

site_idHG1
Number of Residues1
DetailsHIGH AFFINITY MERCURY BINDING SITE
ChainResidue
ACYS73

site_idHG2
Number of Residues3
DetailsSECOND MERCURY BINDING SITE
ChainResidue
ACYS73
AHIS72
ATHR76

Functional Information from PROSITE/UniProt
site_idPS00136
Number of Residues12
DetailsSUBTILASE_ASP Serine proteases, subtilase family, aspartic acid active site. VYVIDTGIeasH
ChainResidueDetails
AVAL35-HIS46

site_idPS00137
Number of Residues11
DetailsSUBTILASE_HIS Serine proteases, subtilase family, histidine active site. HGThCAGtVGS
ChainResidueDetails
AHIS69-SER79

site_idPS00138
Number of Residues11
DetailsSUBTILASE_SER Serine proteases, subtilase family, serine active site. GTSmAtPhVAG
ChainResidueDetails
AGLY222-GLY232

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsACT_SITE: Charge relay system => ECO:0000255|PROSITE-ProRule:PRU01240
ChainResidueDetails
AASP39
AHIS69
ASER224

site_idSWS_FT_FI2
Number of Residues5
DetailsBINDING:
ChainResidueDetails
ATHR16
APRO175
AVAL177
AASP200
AASP260

218853

PDB entries from 2024-04-24

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