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6K2P

Crystal structure of proteinase K from Engyodontium album

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 1001
ChainResidue
APRO175
AVAL177
AASP200
AHOH1121
AHOH1144
AHOH1192
AHOH1249

site_idAC2
Number of Residues6
Detailsbinding site for residue CA A 1002
ChainResidue
AHOH1160
AHOH1186
AHOH1219
AHOH1278
ATHR16
AASP260

site_idAC3
Number of Residues5
Detailsbinding site for residue NO3 A 1003
ChainResidue
ATYR61
ALYS94
AASP97
AASP98
AHOH1231

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

246704

PDB entries from 2025-12-24

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