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1BOQ

PRO REGION C-TERMINUS: PROTEASE ACTIVE SITE INTERACTIONS ARE CRITICAL IN CATALYZING THE FOLDING OF ALPHA-LYTIC PROTEASE

Functional Information from GO Data
ChainGOidnamespacecontents
A0004252molecular_functionserine-type endopeptidase activity
A0006508biological_processproteolysis
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 199
ChainResidue
AHIS36
AARG89
AARG140
AGLY141
ASER143
AHOH225

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 A 200
ChainResidue
APRO186
AHOH231
AHOH258
AHOH304
AHOH318
AALA1
AASN2
AARG183

Functional Information from PROSITE/UniProt
site_idPS00134
Number of Residues6
DetailsTRYPSIN_HIS Serine proteases, trypsin family, histidine active site. VTAGHC
ChainResidueDetails
AVAL32-CYS37

site_idPS00135
Number of Residues12
DetailsTRYPSIN_SER Serine proteases, trypsin family, serine active site. CMgrGDSGGSWI
ChainResidueDetails
ACYS137-ILE148

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsACT_SITE: Charge relay system => ECO:0000250
ChainResidueDetails
AHIS36
AASP63
ASER143

Catalytic Information from CSA
site_idCSA1
Number of Residues5
DetailsAnnotated By Reference To The Literature 1ssx
ChainResidueDetails
ASER143
AGLY141
AASP63
AHIS36
ASER159

site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 1ssx
ChainResidueDetails
ASER143
AGLY141
AASP63
AHIS36

site_idMCSA1
Number of Residues5
DetailsM-CSA 609
ChainResidueDetails
AHIS36proton acceptor, proton donor
AASP63electrostatic stabiliser
AGLY141electrostatic stabiliser
ASER143electrostatic stabiliser
ASER159electrostatic stabiliser

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PDB entries from 2024-05-01

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