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1EGQ

ENHANCEMENT OF ENZYME ACTIVITY THROUGH THREE-PHASE PARTITIONING: CRYSTAL STRUCTURE OF A MODIFIED SERINE PROTEINASE AT 1.5 A RESOLUTION

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 280
ChainResidue
APRO175
AVAL177
AASP200
AHOH501
AHOH502
AHOH503
AHOH504

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CA A 281
ChainResidue
AHOH505
AHOH506
ATHR16
AASP260

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ACY A 301
ChainResidue
ATYR61
ALYS94
AASP97
AASP98
AHOH530

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ACY A 303
ChainResidue
AHIS69
AASN161
ASER221
AGLY222
ASER224

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 Residues3
DetailsACT_SITE: Charge relay system => ECO:0000255|PROSITE-ProRule:PRU01240
ChainResidueDetails
AASP39
AHIS69
ASER224

site_idSWS_FT_FI2
Number of Residues5
DetailsBINDING:
ChainResidueDetails
ATHR16
APRO175
AVAL177
AASP200
AASP260

218853

PDB entries from 2024-04-24

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