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1WMF

Crystal Structure of alkaline serine protease KP-43 from Bacillus sp. KSM-KP43 (oxidized form, 1.73 angstrom)

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
AHOH3001
AHOH3002

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 1002
ChainResidue
AASP391
AASN392
AHOH3003
AASP384
ATHR386
APRO388

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 1003
ChainResidue
AASP367
ALEU368
AASP369
AASP394
AGLU400
AHOH3004

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE DIO A 2001
ChainResidue
ATRP130
AGLY131
AALA159
AGLY161
ATHR254
ASER255

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 2101
ChainResidue
AALA133
AASN135
AGLU163
AALA319
ATYR320
AHOH3141
AHOH3242

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

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PDB entries from 2024-04-24

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