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1GBD

ALPHA-LYTIC PROTEASE WITH MET 190 REPLACED BY ALA AND GLY 216 REPLACED BY ALA COMPLEX WITH METHOXYSUCCINYL-ALA-ALA-PRO-PHENYLALANINE BORONIC ACID

Functional Information from GO Data
ChainGOidnamespacecontents
A0004252molecular_functionserine-type endopeptidase activity
A0006508biological_processproteolysis
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 A 1
ChainResidue
ASER120
ASER124
ATHR125
AARG192
AHOH254
AHOH294
AHOH389

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 A 2
ChainResidue
AARG230
APRO233
AHOH270
AHOH281
AHOH366
AALA15
AASN15

site_idAC3
Number of Residues14
DetailsBINDING SITE FOR CHAIN P OF METHOXYSUCCINYL-ALA-ALA-PRO-PHENYLALANINE BORONIC ACID INHIBITOR
ChainResidue
AHIS57
AARG122
ATYR171
AALA190
AGLY191
AGLY193
AASP194
ASER195
ASER214
AGLY215
AALA216
AVAL218
PHOH145
PHOH152

Functional Information from PROSITE/UniProt
site_idPS00134
Number of Residues6
DetailsTRYPSIN_HIS Serine proteases, trypsin family, histidine active site. VTAGHC
ChainResidueDetails
AVAL53-CYS58

site_idPS00135
Number of Residues12
DetailsTRYPSIN_SER Serine proteases, trypsin family, serine active site. CAgrGDSGGSWI
ChainResidueDetails
ACYS189-ILE200

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsACT_SITE: Charge relay system => ECO:0000250
ChainResidueDetails
AHIS57
AASP102
ASER195

Catalytic Information from CSA
site_idCSA1
Number of Residues5
DetailsAnnotated By Reference To The Literature 1ssx
ChainResidueDetails
AASP102
ASER195
AGLY193
AHIS57
ASER214

site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 1ssx
ChainResidueDetails
AASP102
ASER195
AGLY193
AHIS57

site_idMCSA1
Number of Residues5
DetailsM-CSA 609
ChainResidueDetails
AHIS57proton acceptor, proton donor
AASP102electrostatic stabiliser
AGLY193electrostatic stabiliser
ASER195electrostatic stabiliser
ASER214electrostatic stabiliser

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PDB entries from 2024-11-06

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