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3GT4

Structure of proteinase K with the magic triangle I3C

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 Residues9
DetailsBINDING SITE FOR RESIDUE I3C A 301
ChainResidue
AGLU43
AALA44
ASER45
AGLY259
AHOH416
AHOH530
AHOH557
AHOH607
AHOH694

site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE I3C A 302
ChainResidue
AGLY134
AASN161
AGLY222
ATHR223
ASER224
AHOH303
AHOH628
AHOH645
AHOH731

site_idAC3
Number of Residues12
DetailsBINDING SITE FOR RESIDUE I3C A 305
ChainResidue
AARG189
ATYR195
AASP254
ATHR255
AASN263
APRO265
APHE266
AHOH306
AHOH307
AHOH308
AHOH635
AHOH723

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 A 309
ChainResidue
APRO7
ATRP8
AARG185
AHOH459
AHOH544
AHOH551
AHOH672

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

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1sca
ChainResidueDetails
ASER224
AASP39
AHIS69

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PDB entries from 2024-05-01

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