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5KXV

Structure Proteinase K at 0.98 Angstroms

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 NO3 A 301
ChainResidue
ATYR60
ATYR61
ALYS94
AASP97
AASP98
AHOH423
AHOH581

site_idAC2
Number of Residues9
Detailsbinding site for residue GOL A 302
ChainResidue
ALYS242
ATHR243
ASER247
AASN263
AHOH471
AHOH616
AHOH631
AARG188
AARG189

site_idAC3
Number of Residues9
Detailsbinding site for residue GOL A 303
ChainResidue
APRO175
AVAL177
AASP200
ACA304
AHOH414
AHOH488
AHOH492
AHOH588
AHOH636

site_idAC4
Number of Residues6
Detailsbinding site for residue CA A 304
ChainResidue
APRO175
AVAL177
AASP200
AGOL303
AHOH492
AHOH534

site_idAC5
Number of Residues6
Detailsbinding site for residue CA A 305
ChainResidue
ATHR16
AASP260
AHOH567
AHOH647
AHOH688
AHOH698

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

225946

PDB entries from 2024-10-09

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