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3F7O

Crystal structure of Cuticle-Degrading Protease from Paecilomyces lilacinus (PL646)

Functional Information from GO Data
ChainGOidnamespacecontents
A0004252molecular_functionserine-type endopeptidase activity
A0006508biological_processproteolysis
A0008236molecular_functionserine-type peptidase activity
B0004252molecular_functionserine-type endopeptidase activity
B0006508biological_processproteolysis
B0008236molecular_functionserine-type peptidase activity
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MSU X 1
ChainResidue
AGLY105
ATYR107
AHOH542
XALA2

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 286
ChainResidue
AHOH287
AGLU177
AVAL180
ATHR182
ALEU201
AASP203

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MSU Y 1
ChainResidue
BGLY105
BSER106
BTYR107
BSER108
YALA2

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA B 286
ChainResidue
BGLU177
BVAL180
BTHR182
BLEU201
BASP203

Functional Information from PROSITE/UniProt
site_idPS00136
Number of Residues12
DetailsSUBTILASE_ASP Serine proteases, subtilase family, aspartic acid active site. AYVIDTGVeasH
ChainResidueDetails
AALA37-HIS48

site_idPS00137
Number of Residues11
DetailsSUBTILASE_HIS Serine proteases, subtilase family, histidine active site. HGThCAGtIGS
ChainResidueDetails
AHIS72-SER82

site_idPS00138
Number of Residues11
DetailsSUBTILASE_SER Serine proteases, subtilase family, serine active site. GTSmAtPhIVG
ChainResidueDetails
AGLY225-GLY235

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1sca
ChainResidueDetails
AHIS72
ASER227
AASP41

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1sca
ChainResidueDetails
BHIS72
BSER227
BASP41

223790

PDB entries from 2024-08-14

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