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1PJ8

Structure of a ternary complex of proteinase K, mercury and a substrate-analogue hexapeptide at 2.2 A resolution

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 600
ChainResidue
AASP39
AHIS69
ACYS73

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE HG A 601
ChainResidue
AHIS72
ACYS73
AMET225
AHOH324

site_idAC3
Number of Residues20
DetailsBINDING SITE FOR CHAIN I OF 6-RESIDUE PEPTIDE (N-AC-PAPFPA-NH2)
ChainResidue
AASN99
AGLY100
ALEU133
ASER139
AALA158
AGLY160
AASN161
ASER207
ASER219
AILE220
ASER221
AGLY222
ATHR223
ASER224
AMET225
AHOH376
IHOH483
IHOH486
AASN67
AHIS69

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

226262

PDB entries from 2024-10-16

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