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6RUK

Cu-substituted alpha-Keggin bound to Proteinase K solved by MR

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 Residues37
Detailsbinding site for residue XCU A 301
ChainResidue
AASP26
AGLN54
AMET55
ASER62
ASER63
AARG64
ALYS87
ALEU240
ALYS242
AGLY259
AASP260
AGLU27
ALEU261
ASER262
AASN263
AILE264
APHE266
AASN270
AASN276
AGLN278
AHOH403
AHOH405
ASER28
AHOH411
AHOH414
AHOH422
AHOH430
AHOH453
AHOH468
AHOH513
AHOH588
AGLN31
AGLU43
AALA44
ASER45
AGLY51
AALA53

site_idAC2
Number of Residues7
Detailsbinding site for residue SO4 A 302
ChainResidue
APRO7
ATRP8
AARG185
AHOH466
AHOH472
AHOH569
AHOH570

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

222624

PDB entries from 2024-07-17

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