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1WME

Crystal Structure of alkaline serine protease KP-43 from Bacillus sp. KSM-KP43 (1.50 angstrom, 293 K)

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 Residues6
DetailsBINDING SITE FOR RESIDUE CA A 1001
ChainResidue
AGLU186
ASER194
AASP197
AHIS201
AHOH2176
AHOH2177

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 1002
ChainResidue
AASP391
AASN392
AHOH2178
AASP384
ATHR386
APRO388

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 1003
ChainResidue
AASP367
ALEU368
AASP369
AASP394
AGLU400
AHOH2179

Functional Information from PROSITE/UniProt
site_idPS00137
Number of Residues11
DetailsSUBTILASE_HIS Serine proteases, subtilase family, histidine active site. HGThVAGsVLG
ChainResidueDetails
AHIS68-GLY78

site_idPS00138
Number of Residues11
DetailsSUBTILASE_SER Serine proteases, subtilase family, serine active site. GTSmAtPiVAG
ChainResidueDetails
AGLY253-GLY263

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1sca
ChainResidueDetails
AHIS68
AASP30
ASER255

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PDB entries from 2025-07-02

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