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3AJ9

X-ray analysis of Crystal of Proteinase K Obtained from D2O Solution Using PEG 8000

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 407
ChainResidue
APRO175
AVAL177
AASP200
AHOH419
AHOH429
AHOH443
AHOH446

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 408
ChainResidue
AHOH479
AHOH499
AHOH526
AHOH572
ATHR16
AASP260

site_idAC3
Number of Residues10
DetailsBINDING SITE FOR RESIDUE GOL A 409
ChainResidue
AARG188
AARG189
ALYS242
ATHR243
ASER247
ATYR251
AASN263
AHOH363
AHOH431
AHOH433

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 Residues272
DetailsDomain: {"description":"Peptidase S8","evidences":[{"source":"PROSITE-ProRule","id":"PRU01240","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues3
DetailsActive site: {"description":"Charge relay system","evidences":[{"source":"PROSITE-ProRule","id":"PRU01240","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues5
DetailsBinding site: {}
ChainResidueDetails

239803

PDB entries from 2025-08-06

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