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5CW1

Proteinase K complexed with 4-iodopyrazole

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 Residues7
Detailsbinding site for residue SO4 A 301
ChainResidue
AHIS69
AASN161
ASER221
AGLY222
ASER224
AMET225
AHOH493

site_idAC2
Number of Residues5
Detailsbinding site for residue SO4 A 302
ChainResidue
AHOH406
AHOH413
AHOH475
ASER62
ASER63

site_idAC3
Number of Residues8
Detailsbinding site for residue PYZ A 303
ChainResidue
ALEU133
AGLY134
AALA158
AGLY160
ASER224
AHOH401
AHOH639
AHOH657

site_idAC4
Number of Residues9
Detailsbinding site for residue PYZ A 304
ChainResidue
AGLU174
APRO175
AVAL177
ATHR179
AVAL198
AASP200
AHOH489
AHOH519
AHOH538

site_idAC5
Number of Residues5
Detailsbinding site for residue PYZ A 305
ChainResidue
ATYR104
AILE107
AGLY135
AGLY136
ASER170

site_idAC6
Number of Residues1
Detailsbinding site for residue IOD A 306
ChainResidue
AHOH476

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

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PDB entries from 2024-07-17

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