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3QMP

Selenium SAD structure solution of proteinase K grown in SO4-less solution and soaked in selenate.

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 CA A 280
ChainResidue
APRO175
AVAL177
AASP200
AHOH408
AHOH451
AHOH495
AHOH496

site_idAC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE GOL A 281
ChainResidue
ALYS242
ATHR243
ASER247
ATYR251
AASN263
AHOH288
AHOH491
AHOH510
AARG188
AARG189

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SE4 A 282
ChainResidue
APRO7
ATRP8
AARG185
ALEU209
AHOH341
AHOH393
AHOH703
AHOH720

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CA A 283
ChainResidue
ASER62
AHOH484
AHOH539

site_idAC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CA A 285
ChainResidue
AHOH540
AHOH541

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

219140

PDB entries from 2024-05-01

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